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amyloid beta-peptide 1-40 + H2O
?
-
cleavage occurs at peptide bonds Phe19-Phe20, Phe20-Ala21, and Leu34-Met35, with the latter cleavage site being the initial and principal one
-
?
amyloid beta-peptide 1-42 + H2O
?
-
cleavage occurs at peptide bonds Phe19-Phe20, Phe20-Ala21, and Leu34-Met35, with the latter cleavage site being the initial and principal one
-
?
(7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH + H2O
?
fluorogenic substrate derived from the reported Abeta1-40 core peptide cleavage sequence. The R183Q mutant enzyme exhibits significantly decreased rate of fluorogenic peptide hydrolysis, yet retains similar binding affinity by comparison with the wild-type enzyme
-
-
?
(7-methoxycoumarin-4-yl)acetyl-NPPGFSAFK-2,4-dinitrophenyl + H2O
?
-
bradykinin mimetic substrate V
-
-
?
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-RPPGFSAFK(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-RPPGFSAFK-2,4-dinitrophenyl + H2O
?
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-RPPGF-SAFK-2,4-dinitrophenyl + H2O
?
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-RPPGFSAFK-2,4-dinitrophenyl + H2O
?
7-methoxycoumarin-4-ylacetyl-NPPGFSAFK-2,4-dinitrophenyl + H2O
?
-
-
-
-
?
Abz-GGFLRKHGQ-EDDnp + H2O
?
-
-
-
?
Abz-GGFLRKHGQ-EDDnp + H2O
Abz-GGFLR + KHGQ-EDDnp
-
substrate or small peptide activation occurs through a cis effect
-
-
?
amylin + H2O
amylin peptide fragments
amyloid alpha-peptide + H2O
?
-
-
-
?
amyloid beta + H2O
amyloid beta peptide fragments
-
-
-
-
?
amyloid beta peptide + H2O
?
amyloid beta-peptide (Abeta1-40) + H2O
?
recombinant R183Q mutant enzyme is less active than the recombinant wild-type enzyme against recombinant amyloid beta-peptide (Abeta1-40)
-
-
?
amyloid beta-peptide + H2O
?
amyloid beta-peptide1-40 + H2O
?
degradation
-
-
?
amyloid beta-protein + H2O
?
amyloid beta-protein A21G + H2O
?
-
Flemish genetic variant
-
-
?
amyloid beta-protein E22K + H2O
?
-
Italian genetic variant
-
-
?
amyloid beta-protein E22Q + H2O
?
-
Dutch genetic variant
-
-
?
amyloid beta1-40 + H2O
?
-
-
-
-
?
amyloid beta40 + H2O
amyloid beta40 peptide fragments
amyloid beta42 + H2O
amyloid beta42 peptide fragments
Atrial natriuretic factor + H2O
?
-
-
-
-
?
atrial natriuretic peptide + H2O
?
-
-
-
?
ATTO 655-Cys-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Trp + H2O
?
-
-
-
?
beta-amyloid (Abeta)1-40 + H2O
?
-
-
-
?
beta-amyloid protein + H2O
?
-
-
-
?
beta-endorphin + H2O
?
-
-
-
?
beta-endorphin + H2O
gamma-endorphin + ?
-
-
-
-
?
calcitonin + H2O
?
-
-
-
?
CH3NH-Ala-Ala-Ala-CONHCH3 + H2O
?
-
energetic profile of proteolysis mechanism of IDE
-
-
?
CH3NH-Leu-Tyr-Leu-CONHCH3 + H2O
?
-
energetic profile of proteolysis mechanism of IDE
-
-
?
Dabcyl-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Glu(EDANS)-NH2 + H2O
?
-
fluorogenic derivative of amyloid beta containing residues 10-25
-
-
?
epidermal growth factor + H2O
epidermal growth factor peptide fragments
-
identification of cleavage sites by mass spectrometry and NMR
-
-
?
glucagon + H2O
glucagon peptide fragments
-
-
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
-
-
-
-
?
haemoglobin + H2O
?
-
damaged haemoglobin oxidatively degraded
-
?
Insulin + H2O
Hydrolyzed insulin
insulin + H2O
insulin peptide fragments
Insulin B-chain + H2O
?
-
-
-
-
?
Insulin growth factor II + H2O
?
-
-
-
-
?
insulin-like growth factor I + H2O
insulin-like growth factor I peptide fragments
-
-
-
-
?
insulin-like growth factor II + H2O
insulin-like growth factor II peptide fragments
-
-
-
-
?
insulin-like growth factor-II + H2O
insulin-like growth factor-II peptide fragments
-
identification of cleavage sites by mass spectrometry and NMR
-
-
?
insulin-like peptide 3 + H2O
processed insulin-like peptide 3 + WSTEA
kallidin + H2O
?
-
cleavage at Pro/Phe site
-
-
?
Lysozyme + H2O
?
-
degradation of oxidatively damaged lysozyme
-
?
o-aminobenzoic acid-GGFLRKHGQ-ethylenediamine-2,4-dinitrophenyl + H2O
?
-
-
-
?
Oxidatively damaged hemoglobin + H2O
?
-
-
-
-
?
peptide containing the mitochondrial targeting sequence of E1alpha subunit of human pyruvate dehydrogenase + H2O
?
-
hydrolysis occurs at several sites
-
-
?
peptide V + H2O
?
-
a bradykinin-mimetic fluorogenic peptide substrate V
-
-
?
protein ANP + H2O
?
-
-
-
-
?
protein BNP + H2O
?
-
-
-
-
?
protein CNP + H2O
?
-
-
-
-
?
protein DNP + H2O
?
-
-
-
-
?
reduced amylin + H2O
reduced amylin peptide fragments
-
identification of cleavage sites by mass spectrometry
-
-
?
Transforming growth factor + H2O
?
-
-
-
-
?
transforming growth factor alpha + H2O
?
-
-
-
?
transforming growth factor-alpha + H2O
transforming growth factor-alpha peptide fragments
-
identification of cleavage sites by mass spectrometry
-
-
?
ubiquitin + H2O
?
-
IDE cleaves ubiquitin in a biphasic manner, first, by rapidly removing the two C-terminal glycines (kcat = 2/sec) followed by a slow cleavage between residues 72-73 (kcat = 0.07/sec), thereby producing the inactive Ub1-74 and Ub1-72
-
-
?
urodilatin + H2O
?
-
-
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH + H2O
[(7-methoxycoumarin-4-yl)acetyl]-RPPGF + SAFK(Dnp)-OH
-
-
-
ir
additional information
?
-
(7-methoxycoumarin-4-yl)acetyl-RPPGFSAFK-2,4-dinitrophenyl + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-RPPGFSAFK-2,4-dinitrophenyl + H2O
?
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-RPPGFSAFK-2,4-dinitrophenyl + H2O
?
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-RPPGFSAFK-2,4-dinitrophenyl + H2O
?
-
fluorogenic bradykinin-mimetic IDE substrate V
-
-
?
amylin + H2O
?
-
-
-
?
amylin + H2O
?
-
degradation
-
-
?
amylin + H2O
amylin peptide fragments
-
-
-
-
?
amylin + H2O
amylin peptide fragments
-
identification of cleavage sites by mass spectrometry and NMR. The presence of a disulfide bond in amylin allows IDE to cut at an additional site in the middle of the peptide, amino acids 18-19, binding structure, overview
-
-
?
amyloid beta + H2O
?
-
-
-
?
amyloid beta + H2O
?
-
-
-
-
?
amyloid beta + H2O
?
role of insulin-degrading enzyme in the intracytosolic clearance of amyloid beta and other amyloid-like peptides
-
-
?
amyloid beta peptide + H2O
?
-
-
-
-
?
amyloid beta peptide + H2O
?
-
the catalytic mechanisms for the hydrolysis of the three different peptide bonds (Lys28-Gly29, Phe19-Phe20, and His14-Gln15) of amyloid beta peptide is determined: For all these peptides, the nature of the substrate is found to influence the structure of the active enzyme-substrate complex. (1) activation of the metal-bound water molecule, (2) formation of the gem-diol intermediate, and (3) cleavage of the peptide bond. The process of water activation is found to be the rate-determining step for all three substrates
-
-
?
amyloid beta-peptide + H2O
?
-
-
-
?
amyloid beta-peptide + H2O
?
-
-
-
-
?
amyloid beta-peptide + H2O
?
-
degradation
-
-
?
amyloid beta-peptide + H2O
?
-
degradation, amyloid beta-peptide is the key component of Alzheimer disease-associated senile plaques, genetic linkage and association of Alzheimer disease on chromosome 10q23-24 in the region harboring the IDE gene, chromosome 10-linked Alzheimer disease families show decreased enzyme activity, overview
-
-
?
amyloid beta-peptide + H2O
?
degradation, IDE has no effect on the secreted ectodomain of the amyloid precursor protein derivative generated by alpha-secretase
-
-
?
amyloid beta-peptide + H2O
?
-
degradation, role for insulysin in regulating amyloid beta peptide levels in the brain
-
-
?
amyloid beta-peptide + H2O
?
-
activation in trans is observed with extended substrates that occupy both the active and distal sites
-
-
?
amyloid beta-protein + H2O
?
-
-
-
?
amyloid beta-protein + H2O
?
-
-
-
-
?
amyloid beta-protein + H2O
?
-
-
-
?
amyloid beta40 + H2O
amyloid beta40 peptide fragments
Abeta40, an Alzheimer amyloid beta peptide
-
-
?
amyloid beta40 + H2O
amyloid beta40 peptide fragments
an Alzheimer amyloid beta peptide
-
-
?
amyloid beta42 + H2O
amyloid beta42 peptide fragments
Abeta42, an Alzheimer amyloid beta peptide
-
-
?
amyloid beta42 + H2O
amyloid beta42 peptide fragments
an Alzheimer amyloid beta peptide
-
-
?
amyloid-beta + H2O
?
activity is driven by the dynamic equilibrium between Abeta monomers and higher ordered aggregates. Met35-Val36 is a cleavage site in the amyloid-beta sequence. Amyloid-beta fragments resulting from cleavage by insulin-degrading enzyme form non-toxic amorphous aggregates
-
-
?
amyloid-beta + H2O
?
amyloid-beta monomers, either alone in solution or in dynamic equilibrium with higher aggregates, are cleaved at multiple sites by activity of insulin-degrading enzyme. Met35-Val36 is a cleavage site in the amyloid-beta sequence. Amyloid-beta fragments resulting from cleavage by insulin-degrading enzyme form non-toxic amorphous aggregates
-
-
?
bradykinin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
cleavage at Pro/Phe site
-
-
?
Glucagon + H2O
?
-
-
-
?
Glucagon + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
degradation
-
-
?
Glucagon + H2O
?
the enzyme modulates blood glucose levels by cleaving insulin, a hormone that promotes glucose clearance. It also degrades glucagon, a hormone that elevates glucose levels and opposes the effect of insulin
-
-
?
insulin + H2O
?
-
-
-
?
insulin + H2O
?
-
-
-
-
?
insulin + H2O
?
-
-
-
-
?
insulin + H2O
?
-
-
-
-
?
insulin + H2O
?
-
degradation
-
-
?
insulin + H2O
?
-
insulin degrading enzyme is unlikely to be the relevant enzyme for endosomal proteolysis of internalized insulin in liver parenchyma
-
-
?
insulin + H2O
?
-
implicated in the process of membrane fusion and cell development
-
-
?
insulin + H2O
?
-
insulin degradation
-
-
?
insulin + H2O
?
-
the enzyme may play a general role in hormone metabolism and cellular regulation
-
-
?
insulin + H2O
?
-
degradation, insulin internalized into Hep-G2 cells is able cross-link with intracellular insulysin
-
-
?
insulin + H2O
?
-
degradation, insulin occurs only in grade 3 tumors, whereas grade 2 carcinomas and the normal mammary gland are each insulin-negative, overview
-
-
?
insulin + H2O
?
-
degradation, reduced insulin degradation leads to type 2 diabetes, regulation, overview
-
-
?
insulin + H2O
?
-
degradation, tissue-specific regulation, overview
-
-
?
insulin + H2O
?
-
IDE is involved in the cellular insulin metabolism, insulin inhibits protein degradation via an interaction with IDE, regulation of protein degradation by insulin-degrading enzyme, overview
-
-
?
insulin + H2O
?
-
bovine substrate, degradation, identification of clevage sites in the alpha- and beta-chains, and of the produced proteolytic fragments by AP/MALDI-mass spectrometry, method evaluation, overview
-
-
?
insulin + H2O
?
in HEK cells the enzyme has little impact on insulin clearance
-
-
?
insulin + H2O
?
the enzyme modulates blood glucose levels by cleaving insulin, a hormone that promotes glucose clearance. It also degrades glucagon, a hormone that elevates glucose levels and opposes the effect of insulin
-
-
?
Insulin + H2O
Hydrolyzed insulin
-
-
-
-
?
Insulin + H2O
Hydrolyzed insulin
-
much better degradation than insulin growth factor II
-
-
?
Insulin + H2O
Hydrolyzed insulin
-
specific for insulin
degradation products are smaller than the A-chain of insulin
?
insulin + H2O
insulin peptide fragments
-
-
-
-
?
insulin + H2O
insulin peptide fragments
-
high specificity
-
-
?
insulin + H2O
insulin peptide fragments
-
rapid degradation into inactive peptide fragments
-
-
?
insulin + H2O
insulin peptide fragments
-
IDE forms an enclosed catalytic chamber that completely engulfs and intimately interacts with a partially unfolded insulin molecule. The unique size, shape, charge distribution, and exosite of the IDE catalytic chamber contribute to its high affinity for insulin, IDE-insulin binding structure and interaction analysis, overview
-
-
?
insulin + H2O
insulin peptide fragments
-
IDE uses the size and charge distribution of the catalytic chamber and structural flexibility of the substrates to selectively recognize and degrade insulin
-
-
?
insulin-like peptide 3 + H2O
processed insulin-like peptide 3 + WSTEA
-
IDE cleaves the peptide bond between R26 and W27 of the B-chain, and releases a pentapeptide, WSTEA, from the C-terminal of the B-chain
-
-
?
insulin-like peptide 3 + H2O
processed insulin-like peptide 3 + WSTEA
-
IDE cleaves the peptide bond between R26 and W27 of the B-chain, and releases a pentapeptide, WSTEA, from the C-terminal of the B-chain, cleavage product identification by mass spectrometry, INSL-3 structure, overview
-
-
?
somatostatin + H2O
?
-
cleavage at Phe6-Phe7 bond
-
-
?
somatostatin + H2O
?
somatostatin in addition to being a substrate, is also able to bind to two additional exosites, which play different roles according to the size of the substrate and its binding mode to the catalytic cleft of the enzyme. One exosite, which displays high affinity for somatostatin, regulates only the interaction of insulin-degrading-enzyme with larger substrates (such as insulin and beta-amyloid1-40) in a differing fashion according to their various modes of binding to the enzyme. A second exosite, which is involved in the regulation of enzymatic processing by the enzyme of all substrates investigated (including a 10-25 amino acid long amyloid-like peptide, bradykinin and somatostatin itself), probably acts through the alteration of an open-closed equilibrium
-
-
?
additional information
?
-
-
fructose 1,6-bisphosphatase
-
-
?
additional information
?
-
-
hexosephosphate isomerase
-
-
?
additional information
?
-
-
aldolase
-
-
?
additional information
?
-
-
the conserved glutamate in the zinc-binding site of human enzyme is a major catalytic residue, while a conserved cysteine in this region is not essential for catalysis
-
-
?
additional information
?
-
-
no inactivation of: lactate dehydrogenase
-
-
?
additional information
?
-
-
thyroid-stimulating hormone
-
-
?
additional information
?
-
-
prolactin
-
-
?
additional information
?
-
-
hexokinase
-
-
?
additional information
?
-
-
not: growth hormone
-
-
?
additional information
?
-
-
does not act on glucagon-like peptide 1, nerve growth factor, somatostatin, bradykinin, vasopressin, platelet-derived growth factor, and vasoactive intestinal peptide, proinsulin, epidermal growth factor and IGF-I bind to the enzyme but are not efficiently degraded
-
?
additional information
?
-
-
enzyme can degrade cleaved mitochondrial targeting sequences, role of enzyme within mitochondria
-
-
?
additional information
?
-
-
hyperinsulinemia is probably elevated through insulin's competitition with amyloid beta-peptide for the enzyme, IDE deficiency might be involved in development of Alzheimer's disease, regulation, overview
-
-
?
additional information
?
-
-
membrane-bound, but not cytosolic, enzyme selectively decreases during hippocampal development from mild cognitive impairment to mild to severe Alzheimer's disease, overview
-
-
?
additional information
?
-
-
no association of IDE haplotypes with the risk of dementia, IDE may be indirectly related to dementia via its regulation of insulin levels, but it is not a major gene for Alzheimers disease
-
-
?
additional information
?
-
-
regulation of enzyme expression in the liver, overview
-
-
?
additional information
?
-
-
the human enzyme interacts with Varicella-zoster virus glycoprotein E, gE, facilitating viral infection and cell-to-cell spread of the virus, and thus serving as a cellular receptor for the virus, the binding region of the viral protein is located at amino acids 32 to 71 of gE, deletion of this sequence leads to loss of binding ability, overview, the secondary structure of the IDE binding domain is likely important for its interaction with IDE
-
-
?
additional information
?
-
-
the insulin-degrading enzyme is genetically associated with Alzheimer's disease in the Finnish population, overview
-
-
?
additional information
?
-
-
IDE has a preference for basic or hydrophobic amino acids at the carboxyl side of cleavage sites, overview, the catalytic domain of IDE is located in the amino subunit
-
-
?
additional information
?
-
-
the enzyme is a neutral thiol metalloprotease with the active site sequence HEXXH
-
-
?
additional information
?
-
-
IDE is a neutral thiol metalloprotease
-
-
?
additional information
?
-
-
IDE is involved in the clearance of many bioactive peptide substrates, including insulin and amyloid beta, peptides vital to the development of diabetes and Alzheimer's disease, respectively. IDE can also rapidly degrade hormones that are held together by intramolecular disulfide bond(s) without their reduction. Furthermore, IDE exhibits a remarkable ability to preferentially degrade structurally similar peptides such as the selective degradation of insulin-like growth factor-II and transforming growth factor-alpha, TGF-alpha, over IGF-I and epidermal growth factor, respectively. IDE cleaves its substrates at multiple sites in a biased stochastic manner
-
-
?
additional information
?
-
active site structure of IDE, overview. Interactions of the two full-length Alzheimer amyloid beta peptides, Abeta40 and Abeta42, with the fully active form of IDE through unrestrained, all-atom molecular dynamics simulations, using free and small fragment-bound, Asp1-Glu3 and Lys16-Asp23 of Abeta40 and Asp1-Glu3 and Lys16-Glu22 of Abeta42, mutated forms of IDE and NMR structures of the full-length Abeta40 and Abeta42, overview. In comparison to Abeta40, Abeta42 is more flexible and interacts through a smaller number, 17-22, of hydrogen bonds in the catalytic chamber of IDE. Both the substrates adopt more beta-sheet character in the IDE environment. Hydrogen bonding interactions between IDE and substrates amyloidbeta40 and amyloidbeta42, overview
-
-
?
additional information
?
-
-
IDE shows catalytic activity toward two peptides of different length, simulating a portion of B chain of insulin, analysis by density functional theory method and the hybrid exchange-correlation functional B3LYP in gas phase and in the protein environment, modelling, reaction mechanism, overview. The proteolysis reaction is exothermic and proceeds quickly as the barrier in the rate-limiting step falls widely within the range of values expected for an enzymatic catalysis
-
-
?
additional information
?
-
-
the putative ATP-binding domain is a key modulator of IDE proteolytic activity
-
-
?
additional information
?
-
-
the substrates often possess disulfide bonds that are involved in enzyme-substrate interactions, e.g. insulin possesses three disulfide bonds. The exosite interaction serves as a molecular tether allowing the proper positioning of the C-terminal end of the substrate to the catalytic site, exosite binding ligands can activate the enzyme, the exosite has regulatory function. Tyr831 is also involved in substrate positioning, enzyme-substrate interactions required for the regulation of the enzyme with open and closed stages, mechanism, overview. The closed stage in absence of substrate is unstable. IDE is an allosteric enzyme
-
-
?
additional information
?
-
the enzyme selectively degrades biologically important substrates associated with type 2 diabetes and Alzheimer's disease
-
-
?
additional information
?
-
a functional requirement for active site residues F115, A140, F141, Y150, W199, F202, F820, and Y831 is established, and specific contributions of residue charge, size, and hydrophobicity to substrate binding, specificity, and proteolysis are demonstrated
-
-
?
additional information
?
-
-
a functional requirement for active site residues F115, A140, F141, Y150, W199, F202, F820, and Y831 is established, and specific contributions of residue charge, size, and hydrophobicity to substrate binding, specificity, and proteolysis are demonstrated
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
amylin + H2O
?
-
degradation
-
-
?
amylin + H2O
amylin peptide fragments
amyloid alpha-peptide + H2O
?
-
-
-
?
amyloid beta + H2O
?
role of insulin-degrading enzyme in the intracytosolic clearance of amyloid beta and other amyloid-like peptides
-
-
?
amyloid beta + H2O
amyloid beta peptide fragments
-
-
-
-
?
amyloid beta-peptide + H2O
?
amyloid beta40 + H2O
amyloid beta40 peptide fragments
Abeta40, an Alzheimer amyloid beta peptide
-
-
?
amyloid beta42 + H2O
amyloid beta42 peptide fragments
Abeta42, an Alzheimer amyloid beta peptide
-
-
?
amyloid-beta + H2O
?
activity is driven by the dynamic equilibrium between Abeta monomers and higher ordered aggregates. Met35-Val36 is a cleavage site in the amyloid-beta sequence. Amyloid-beta fragments resulting from cleavage by insulin-degrading enzyme form non-toxic amorphous aggregates
-
-
?
beta-endorphin + H2O
gamma-endorphin + ?
-
-
-
-
?
epidermal growth factor + H2O
epidermal growth factor peptide fragments
-
identification of cleavage sites by mass spectrometry and NMR
-
-
?
glucagon + H2O
glucagon peptide fragments
-
-
-
-
?
insulin + H2O
insulin peptide fragments
insulin-like growth factor I + H2O
insulin-like growth factor I peptide fragments
-
-
-
-
?
insulin-like growth factor II + H2O
insulin-like growth factor II peptide fragments
-
-
-
-
?
insulin-like growth factor-II + H2O
insulin-like growth factor-II peptide fragments
-
identification of cleavage sites by mass spectrometry and NMR
-
-
?
insulin-like peptide 3 + H2O
processed insulin-like peptide 3 + WSTEA
-
IDE cleaves the peptide bond between R26 and W27 of the B-chain, and releases a pentapeptide, WSTEA, from the C-terminal of the B-chain
-
-
?
reduced amylin + H2O
reduced amylin peptide fragments
-
identification of cleavage sites by mass spectrometry
-
-
?
transforming growth factor-alpha + H2O
transforming growth factor-alpha peptide fragments
-
identification of cleavage sites by mass spectrometry
-
-
?
additional information
?
-
amylin + H2O
amylin peptide fragments
-
-
-
-
?
amylin + H2O
amylin peptide fragments
-
identification of cleavage sites by mass spectrometry and NMR. The presence of a disulfide bond in amylin allows IDE to cut at an additional site in the middle of the peptide, amino acids 18-19, binding structure, overview
-
-
?
amyloid beta-peptide + H2O
?
-
-
-
?
amyloid beta-peptide + H2O
?
-
-
-
-
?
amyloid beta-peptide + H2O
?
-
degradation
-
-
?
amyloid beta-peptide + H2O
?
-
degradation, amyloid beta-peptide is the key component of Alzheimer disease-associated senile plaques, genetic linkage and association of Alzheimer disease on chromosome 10q23-24 in the region harboring the IDE gene, chromosome 10-linked Alzheimer disease families show decreased enzyme activity, overview
-
-
?
amyloid beta-peptide + H2O
?
degradation, IDE has no effect on the secreted ectodomain of the amyloid precursor protein derivative generated by alpha-secretase
-
-
?
amyloid beta-peptide + H2O
?
-
degradation, role for insulysin in regulating amyloid beta peptide levels in the brain
-
-
?
Glucagon + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
degradation
-
-
?
Glucagon + H2O
?
the enzyme modulates blood glucose levels by cleaving insulin, a hormone that promotes glucose clearance. It also degrades glucagon, a hormone that elevates glucose levels and opposes the effect of insulin
-
-
?
insulin + H2O
?
-
-
-
?
insulin + H2O
?
-
-
-
-
?
insulin + H2O
?
-
-
-
-
?
insulin + H2O
?
-
degradation
-
-
?
insulin + H2O
?
-
insulin degrading enzyme is unlikely to be the relevant enzyme for endosomal proteolysis of internalized insulin in liver parenchyma
-
-
?
insulin + H2O
?
-
implicated in the process of membrane fusion and cell development
-
-
?
insulin + H2O
?
-
insulin degradation
-
-
?
insulin + H2O
?
-
the enzyme may play a general role in hormone metabolism and cellular regulation
-
-
?
insulin + H2O
?
-
degradation, insulin internalized into Hep-G2 cells is able cross-link with intracellular insulysin
-
-
?
insulin + H2O
?
-
degradation, insulin occurs only in grade 3 tumors, whereas grade 2 carcinomas and the normal mammary gland are each insulin-negative, overview
-
-
?
insulin + H2O
?
-
degradation, reduced insulin degradation leads to type 2 diabetes, regulation, overview
-
-
?
insulin + H2O
?
-
degradation, tissue-specific regulation, overview
-
-
?
insulin + H2O
?
-
IDE is involved in the cellular insulin metabolism, insulin inhibits protein degradation via an interaction with IDE, regulation of protein degradation by insulin-degrading enzyme, overview
-
-
?
insulin + H2O
?
in HEK cells the enzyme has little impact on insulin clearance
-
-
?
insulin + H2O
?
the enzyme modulates blood glucose levels by cleaving insulin, a hormone that promotes glucose clearance. It also degrades glucagon, a hormone that elevates glucose levels and opposes the effect of insulin
-
-
?
insulin + H2O
insulin peptide fragments
-
-
-
-
?
insulin + H2O
insulin peptide fragments
-
high specificity
-
-
?
insulin + H2O
insulin peptide fragments
-
rapid degradation into inactive peptide fragments
-
-
?
additional information
?
-
-
enzyme can degrade cleaved mitochondrial targeting sequences, role of enzyme within mitochondria
-
-
?
additional information
?
-
-
hyperinsulinemia is probably elevated through insulin's competitition with amyloid beta-peptide for the enzyme, IDE deficiency might be involved in development of Alzheimer's disease, regulation, overview
-
-
?
additional information
?
-
-
membrane-bound, but not cytosolic, enzyme selectively decreases during hippocampal development from mild cognitive impairment to mild to severe Alzheimer's disease, overview
-
-
?
additional information
?
-
-
no association of IDE haplotypes with the risk of dementia, IDE may be indirectly related to dementia via its regulation of insulin levels, but it is not a major gene for Alzheimers disease
-
-
?
additional information
?
-
-
regulation of enzyme expression in the liver, overview
-
-
?
additional information
?
-
-
the human enzyme interacts with Varicella-zoster virus glycoprotein E, gE, facilitating viral infection and cell-to-cell spread of the virus, and thus serving as a cellular receptor for the virus, the binding region of the viral protein is located at amino acids 32 to 71 of gE, deletion of this sequence leads to loss of binding ability, overview, the secondary structure of the IDE binding domain is likely important for its interaction with IDE
-
-
?
additional information
?
-
-
the insulin-degrading enzyme is genetically associated with Alzheimer's disease in the Finnish population, overview
-
-
?
additional information
?
-
-
IDE is a neutral thiol metalloprotease
-
-
?
additional information
?
-
-
IDE is involved in the clearance of many bioactive peptide substrates, including insulin and amyloid beta, peptides vital to the development of diabetes and Alzheimer's disease, respectively. IDE can also rapidly degrade hormones that are held together by intramolecular disulfide bond(s) without their reduction. Furthermore, IDE exhibits a remarkable ability to preferentially degrade structurally similar peptides such as the selective degradation of insulin-like growth factor-II and transforming growth factor-alpha, TGF-alpha, over IGF-I and epidermal growth factor, respectively. IDE cleaves its substrates at multiple sites in a biased stochastic manner
-
-
?
additional information
?
-
the enzyme selectively degrades biologically important substrates associated with type 2 diabetes and Alzheimer's disease
-
-
?
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((((S)-1-benzylcarbamoyl-2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid
-
((((S)-2-(1H-imidazol-4-yl)-1-(3-methyl-(1,2,4)oxadiazol-5-yl)-ethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid
-
((((S)-2-(1H-imidazol-4-yl)-1-(3-methyl-(1,2,4)oxadiazol-5-yl)-ethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid methyl ester
less than 10% inhibition at 0.1 mM
((((S)-2-(1H-imidazol-4-yl)-1-methylcarbamoylethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid
BDM43079
((((S)-2-(1H-imidazol-4-yl)-1-methylcarbamoylethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid methyl ester
less than 10% inhibition at 0.1 mM
((((S)-2-hydroxy-1-(1H-imidazol-4-ylmethyl)-ethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid
-
(11R,12S,13S)-13-(hydroxymethyl)-12-(2'-methylbiphenyl-4-yl)-9-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,9-diazabicyclo[9.2.0]tridecan-2-one
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00006 mM
(3R,6S,9S,12E,16S)-9-(4-aminobutyl)-3-(4-benzoylbenzyl)-6-(cyclohexylmethyl)-2,5,8,11,14-pentaoxo-1,4,7,10,15-pentaazacycloicos-12-ene-16-carboxamide
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00005 mM
(7R,8S,9S)-8-(2',3'-dimethylbiphenyl-4-yl)-9-(hydroxymethyl)-5-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,5-diazabicyclo[5.2.0]nonan-2-one
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00012 mM
(8R,9R,10S)-N-cyclopentyl-10-(hydroxymethyl)-9-(2'-methylbiphenyl-4-yl)-1,6-diazabicyclo[6.2.0]decane-6-carboxamide
the inhibitor fully blocks insulin degradation in a concentration-dependent manner, while only weakly and partially inhibiting glucagon degradation. It inhibits wild-type enzyme, but does not inhibit A479L exo-site variant. It displays decreased affinity
(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-10-(fluoromethyl)-6-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,6-diazabicyclo[6.2.0]decane
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000024 mM
(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-10-(hydroxymethyl)-6-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,6-diazabicyclo[6.2.0]decan-2-one
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00008 mM
(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-10-(methoxymethyl)-6-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,6-diazabicyclo[6.2.0]decane
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000075 mM
(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,6-diazabicyclo[6.2.0]decane-10-carboxylic acid
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0005 mM
(9R,10S,11S)-10-(2',3'-dimethylbiphenyl-4-yl)-11-(hydroxymethyl)-7-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,7-diazabicyclo[7.2.0]undecan-2-one
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0001 mM
(benzyl-(((S)-1-benzylcarbamoyl-2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
-
(benzyl-(((S)-1-carbamoyl-2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
-
(benzyl-(((S)-1-dimethylcarbamoyl-2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
-
(benzyl-(((S)-2-(1H-imidazol-4-yl)-1-methylcarbamoylethylcarbamoyl)-methyl)-amino)-acetic acid
-
(benzyl-(((S)-2-hydroxy-1-(1H-imidazol-4-ylmethyl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
-
(benzyl-((2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
less than 10% inhibition at 0.1 mM
(S)-2-(2-((4-tert-butyl-benzyl)-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(benzoyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(benzyl-(1H-tetrazol-5-ylmethyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-N-methyl-propionamide
less than 10% inhibition at 0.1 mM
(S)-2-(2-(benzyl-(2-carboxy-ethyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(benzyl-(2-hydroxy-3,4-dioxo-cyclobut-1-enyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(benzyl-carbamoylmethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid
less than 10% inhibition at 0.1 mM
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid isopropyl ester
-
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid tert-butyl ester
-
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(1H-indol-3-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(3H-imidazol-4-yl)-propionic acid isobutyl ester
-
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-phenyl-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-5-guanidino-pentanoic acid methyl ester
-
(S)-2-(2-(benzyl-hydroxycarbamoylmethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(benzyl-methoxycarbonylmethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(benzyloxycarbonyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(carboxymethyl-(1-methyl-3-phenyl-propyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-(2-(1H-indol-3-yl)-ethyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-(3-phenyl-propionyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(carboxymethyl-(3-phenyl-propyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-(3-phenyl-propyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid tert-butyl ester
-
(S)-2-(2-(carboxymethyl-(4-fluoro-benzyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-(4-methyl-benzyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-(4-phenyl-butyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-(4-trifluoromethyl-benzyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-(n-hexyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-amino)-acetylamino)-3-(1Himidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(carboxymethyl-methyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(carboxymethyl-naphthalen-2-ylmethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-phenethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-(carboxymethyl-phenyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(carboxymethyl-phenylacetyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
(S)-2-(2-(carboxymethyl-pyridin-4-ylmethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
-
(S)-2-(2-benzylamino-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
less than 10% inhibition at 0.1 mM
1-[(8R,9R,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]-N,N-dimethylmethanamine
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0001 mM
1-[(8R,9R,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]-N-methylmethanamine
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000007 mM
3-(((S)-1-methoxy-1-oxo-3-imidazol-2-yl)carbamoyl)-1,2,3,4-tetrahydroisoquinoline-2-ethanoic acid
-
3-benzyl-4-((S)-2-(1H-imidazol-4-yl)-1-methylcarbamoylethylcarbamoyl)-butyric acid
less than 10% inhibition at 0.1 mM
4'-[(8R,9S,10S)-10-(hydroxymethyl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-9-yl]biphenyl-3-ol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0073 mM
ATP
-
interacts via the phosphate moiety, inhibits IDE and shifts the oligomeric equilibrium promoting the transition from tetramer to dimer and from closed to open state
insulin-like peptide 3
-
IDE degrades insulin quickly, and addition of INSL3 significantly decreases insulin degradation, competitive inhibition
-
methyl 5-[[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-10-(hydroxymethyl)-1,6-diazabicyclo[6.2.0]dec-6-yl]sulfonyl]-1-methyl-1H-pyrrole-2-carboxylate
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: above 0.005 mM
methyl [(2S)-2-(5-[5-[4-([(2S)-2-[(3S)-3-amino-2-oxopiperidin-1-yl]-2-cyclohexylacetyl]amino)phenyl]pentyl]-2-fluorophenyl)-3-(quinolin-3-yl)propyl]carbamate
-
methyl [(2S)-2-[4-([5-[4-([(2S)-2-[(3S)-3-amino-2-oxopiperidin-1-yl]-2-cyclohexylacetyl]amino)phenyl]pentyl]oxy)phenyl]-3-(quinolin-3-yl)butyl]carbamate
-
N-(4-[[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-10-(hydroxymethyl)-1,6-diazabicyclo[6.2.0]dec-6-yl]sulfonyl]-3-methylphenyl)acetamide
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0016 mM
N-[[(2R,3S,4S)-1-acetyl-3-(2',3'-dimethylbiphenyl-4-yl)-4-(hydroxymethyl)azetidin-2-yl]methyl]-2-(trifluoromethyl)benzenesulfonamide
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000115 mM
N-[[(2R,3S,4S)-3-(2',3'-dimethylbiphenyl-4-yl)-4-(hydroxymethyl)-1-(prop-2-en-1-yl)azetidin-2-yl]methyl]-2-(trifluoromethyl)benzenesulfonamide
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0001 mM
N-[[(2R,3S,4S)-3-(2',3'-dimethylbiphenyl-4-yl)-4-(hydroxymethyl)azetidin-2-yl]methyl]-2-(trifluoromethyl)benzenesulfonamide
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0006 mM
N2-[(2S)-4-(hydroxyamino)-2-(naphthalen-2-ylmethyl)-4-oxobutanoyl]-L-arginyl-L-tryptophyl-L-glutamine
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0000006 mM
nestin
-
potently inhibits the cleavage of ubiquitin by IDE
-
nitric oxide
-
amyloid beta peptide degradation by IDE is inhibited by NO donor Sin-1
Sulfhydryl-alkylating agents
-
-
-
sulfhydryl-modifying reagents
-
Drosophila, human and rat enzyme inhibited, bacterial enzyme not
-
Ub1-72
-
cleaved ubiquitin
-
Ub1-74
-
cleaved ubiquitin
-
[(3Z,8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-(6,7,8,9-tetrahydro-5H-imidazo[1,2-a]azepin-3-ylsulfonyl)-1,6-diazabicyclo[6.2.0]dec-3-en-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000042 mM
[(3Z,8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(1,2-dimethyl-1H-imidazol-5-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-3-en-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000001 mM
[(3Z,8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(1-ethyl-5-methyl-1H-pyrazol-4-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-3-en-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000016 mM
[(3Z,8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(1-propyl-1H-pyrazol-5-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-3-en-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000018 mM
[(3Z,8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(2-methylpyridin-3-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-3-en-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000022 mM
[(3Z,8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[[1-methyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]sulfonyl]-1,6-diazabicyclo[6.2.0]dec-3-en-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000065 mM
[(8R,9S,10S)-6-(cyclohexylsulfonyl)-9-(2',3'-dimethylbiphenyl-4-yl)-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00046 mM
[(8R,9S,10S)-6-[(2-methylphenyl)sulfonyl]-9-[2'-methyl-3'-(trifluoromethyl)biphenyl-4-yl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000095 mM
[(8R,9S,10S)-9-(2',3'-dichlorobiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000009 mM
[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(1,3-dimethyl-1H-pyrazol-5-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000024 mM
[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(1-methyl-1H-imidazol-2-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0000005 mM
[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(1-methyl-1H-pyrazol-5-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00006 mM
[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0000015 mM
[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[(4-methylpiperazin-1-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000032 mM
[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[[1-(propan-2-yl)-1H-pyrazol-5-yl]sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000015 mM
[(8R,9S,10S)-9-(2',3'-dimethylbiphenyl-4-yl)-6-[[2-(trifluoromethyl)phenyl]sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000001 mM
[(8R,9S,10S)-9-(2',5'-dimethylbiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000054 mM
[(8R,9S,10S)-9-(2'-methoxybiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00025 mM
[(8R,9S,10S)-9-(2'-methylbiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000032 mM
[(8R,9S,10S)-9-(3',4'-dimethylbiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00014 mM
[(8R,9S,10S)-9-(3',5'-dimethylbiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000061 mM
[(8R,9S,10S)-9-(3'-chloro-2'-methylbiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.000035 mM
[(8R,9S,10S)-9-(3'-fluoro-2'-methylbiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00007 mM
[(8R,9S,10S)-9-(3'-fluorobiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00007 mM
[(8R,9S,10S)-9-(3'-methoxybiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0005 mM
[(8R,9S,10S)-9-(3'-methylbiphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
the inhibitor fully blocks insulin degradation in a concentration-dependent manner, while only weakly and partially inhibiting glucagon degradation. It inhibits wild-type enzyme, but does not inhibit A479L exo-site variant. It displays decreased affinity
[(8R,9S,10S)-9-(biphenyl-4-yl)-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0004 mM
[(8R,9S,10S)-9-[3'-fluoro-2'-(trifluoromethyl)biphenyl-4-yl]-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.00017 mM
[(8R,9S,10S)-9-[4-(1,3-benzodioxol-5-yl)phenyl]-6-[(2-methylphenyl)sulfonyl]-1,6-diazabicyclo[6.2.0]dec-10-yl]methanol
half-maximum effective concentration in fluorogenic decapeptide ([(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH) cleavage assay: 0.0029 mM
1,10-phenanthroline
-
-
1,10-phenanthroline
-
a Zn2+ chelator
bacitracin
-
-
bacitracin
the inhibitory effect in enhanced by ATP
EDTA
-
-
EDTA
-
the activation of IDE disappears upon inactivation by EDTA, which chelates the catalytic Zn2+ ion
hydrogen peroxide
-
-
hydrogen peroxide
-
the oxidative burst of BV-2 microglial cells leads to oxidation of secreted IDE at Cys residues, e.g. Cys819, Cys110, Cys257, and Cys178, leading to the reduced activity after 4 h versus amyloid beta degradation, increases IDE oligomerization, and decreases IDE thermostability. Within the first 4 h of incubation at 37°C, the control and H2O2-treated enzyme does not lose any relative activity. The inhibitory response of IDE is substrate-dependent, biphasic for amyloid beta degradation but monophasic for a shorter bradykinin-mimetic substrate, mutational analysis, overview. Only Cys819 modification plays a prominent role in the change of enzyme properties
NEM
-
-
NEM
-
modifies Cys819 and inhibits IDE
S-nitrosoglutathione
-
potent inhibition at physiologically relevant concentrations
S-nitrosoglutathione
-
the oxidative burst of BV-2 microglial cells leads nitrosylation of secreted IDE at Cys residues, e.g. Cys819, Cys110, Cys257, and Cys178, leading to the reduced activity versus amyloid beta degradation, increases IDE oligomerization, and decreases IDE thermostability. This inhibitory response of IDE is substrate-dependent, biphasic for amyloid beta degradation but monophasic for a shorter bradykinin-mimetic substrate, mutational analysis, overview. Only Cys819 modification plays a prominant role in the change of enzyme properties
additional information
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not: phosphoramidon
-
additional information
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not: phenylmethanesulfonyl fluoride
-
additional information
-
not: the enzyme is inhibited by cysteine protease inhibitors as well as metalloprotease inhibitors
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additional information
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in patients with V97L mutation of presenilin 1, insulysin activity on the plasma membranes is reduction concomitantly with increased levels of extracellular and intracellular amyloid beta42. In the presenilin 1 V97L mutant-transfected SH-SY5Y cell line, increase of intracellular amyloid beta42 is associated with decreased expression and activity of insulysin in the cytosol and endoplasmic reticulum
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additional information
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amyloid beta-induced oxidation of IDE by 4-hydroxy-nonenal does not affect IDE activity in human neuroblastoma SH-SY5Y cells, but rapidly induces IDE expression
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Alzheimer Disease
A common genetic system for functional studies of pitrilysin and related M16A proteases.
Alzheimer Disease
A neglected modulator of insulin-degrading enzyme activity and conformation: The pH.
Alzheimer Disease
Accumulation of BRI2-BRICHOS ectodomain correlates with a decreased clearance of A? by insulin degrading enzyme (IDE) in Alzheimer's disease.
Alzheimer Disease
Altered expression of insulin-degrading enzyme and regulator of calcineurin in the rat intracerebral streptozotocin model and human apolipoprotein E-?4-associated Alzheimer's disease.
Alzheimer Disease
Amylin and its analogs: a friend or foe for the treatment of Alzheimer's disease?
Alzheimer Disease
Amyloid-beta peptide levels in brain are inversely correlated with insulysin activity levels in vivo.
Alzheimer Disease
Association Between Polymorphisms of the Insulin-Degrading Enzyme Gene and Late-Onset Alzheimer Disease.
Alzheimer Disease
Association of insulin degrading enzyme gene polymorphisms with Alzheimer's disease: a meta-analysis.
Alzheimer Disease
Association studies between risk for late-onset Alzheimer's disease and variants in insulin degrading enzyme.
Alzheimer Disease
C allele of the rs2209972 single nucleotide polymorphism of the insulin degrading enzyme gene and Alzheimer's disease in type 2 diabetes, a case control study.
Alzheimer Disease
Catalytic Mechanism of Amyloid-? Peptide Degradation by Insulin Degrading Enzyme: Insights from Quantum Mechanics and Molecular Mechanics Style Møller-Plesset Second Order Perturbation Theory Calculation.
Alzheimer Disease
CDK5 Participates in Amyloid-? Production by Regulating PPAR? Phosphorylation in Primary Rat Hippocampal Neurons.
Alzheimer Disease
Characteristics of Insulin-degrading Enzyme in Alzheimer's Disease: A Meta-analysis.
Alzheimer Disease
Characterization of insulin-degrading enzyme-mediated cleavage of A? in distinct aggregation states.
Alzheimer Disease
Chia Seed Does Not Improve Cognitive Impairment in SAMP8 Mice Fed with High Fat Diet.
Alzheimer Disease
Cognitive and Disease-Modifying Effects of 11?-Hydroxysteroid Dehydrogenase Type 1 Inhibition in Male Tg2576 Mice, a Model of Alzheimer's Disease.
Alzheimer Disease
Combined risk effects of IDE and NEP gene variants on Alzheimer disease.
Alzheimer Disease
Concordant association of insulin degrading enzyme gene (IDE) variants with IDE mRNA, Abeta, and Alzheimer's disease.
Alzheimer Disease
Copper(I) and copper(II) inhibit A? peptides proteolysis by insulin-degrading enzyme differently: implications for metallostasis alteration in Alzheimer's disease.
Alzheimer Disease
Decreased catalytic activity of the insulin-degrading enzyme in chromosome 10-linked Alzheimer disease families.
Alzheimer Disease
Degradation of soluble amyloid beta-peptides 1-40, 1-42, and the Dutch variant 1-40Q by insulin degrading enzyme from Alzheimer disease and control brains.
Alzheimer Disease
Deletion of the fission yeast homologue of human insulinase reveals a TORC1-dependent pathway mediating resistance to proteotoxic stress.
Alzheimer Disease
Detergent resistant membrane-associated IDE in brain tissue and cultured cells: Relevance to Abeta and insulin degradation.
Alzheimer Disease
Development of monoclonal antibodies and quantitative ELISAs targeting insulin-degrading enzyme.
Alzheimer Disease
Drug Target Engagement Using Coupled Cellular Thermal Shift Assay-Acoustic Reverse-Phase Protein Array.
Alzheimer Disease
Enhanced Phospholipase A2 Group 3 Expression by Oxidative Stress Decreases the Insulin-Degrading Enzyme.
Alzheimer Disease
Enzyme kinetics from circular dichroism of insulin reveals mechanistic insights into the regulation of insulin-degrading enzyme.
Alzheimer Disease
Evidence for genetic linkage of Alzheimer's disease to chromosome 10q.
Alzheimer Disease
Functional human insulin-degrading enzyme can be expressed in bacteria.
Alzheimer Disease
Gain of PITRM1 peptidase in cortical neurons affords protection of mitochondrial and synaptic function in an advanced age mouse model of Alzheimer's disease.
Alzheimer Disease
Ginsenoside Rg1 Decreases A?1-42 Level by Upregulating PPAR? and IDE Expression in the Hippocampus of a Rat Model of Alzheimer's Disease.
Alzheimer Disease
GLP-1 receptor regulates cell growth through regulating IDE expression level in A?1-42-treated PC12 cells.
Alzheimer Disease
Identification and functional characterization of a putative IDE, C28F5.4 (ceIDE-1), in Caenorhabditis elegans: Implications for Alzheimer's disease.
Alzheimer Disease
Identification of the allosteric regulatory site of insulysin.
Alzheimer Disease
Impact of Insulin Degrading Enzyme and Neprilysin in Alzheimer's Disease Biology: Characterization of Putative Cognates for Therapeutic Applications.
Alzheimer Disease
Insulin degrading enzyme (IDE) genetic variants and risk of Alzheimer's disease: evidence of effect modification by apolipoprotein E (APOE).
Alzheimer Disease
Insulin degrading enzyme activity selectively decreases in the hippocampal formation of cases at high risk to develop Alzheimer's disease.
Alzheimer Disease
Insulin degrading enzyme and alpha-3 catenin polymorphisms in Italian patients with Alzheimer disease.
Alzheimer Disease
Insulin degrading enzyme contributes to the pathology in a mixed model of Type 2 diabetes and Alzheimer's disease: possible mechanisms of IDE in T2D and AD.
Alzheimer Disease
Insulin, insulin-degrading enzyme and amyloid-beta peptide in Alzheimer's disease: review and hypothesis.
Alzheimer Disease
Insulin-degrading enzyme and Alzheimer disease: a genetic association study in the Han Chinese.
Alzheimer Disease
Insulin-degrading enzyme antagonizes insulin-dependent tissue growth and Abeta-induced neurotoxicity in Drosophila.
Alzheimer Disease
Insulin-degrading enzyme as a downstream target of insulin receptor signaling cascade: implications for Alzheimer's disease intervention.
Alzheimer Disease
Insulin-degrading enzyme deficiency accelerates cerebrovascular amyloidosis in an animal model.
Alzheimer Disease
Insulin-degrading enzyme in the Alzheimer's disease brain: prominent localization in neurons and senile plaques.
Alzheimer Disease
Insulin-Degrading Enzyme in the Fight against Alzheimer's Disease.
Alzheimer Disease
Insulin-degrading enzyme inhibition, a novel therapy for type 2 diabetes?
Alzheimer Disease
Insulin-degrading enzyme is exported via an unconventional protein secretion pathway.
Alzheimer Disease
Insulin-degrading enzyme is genetically associated with Alzheimer's disease in the Finnish population.
Alzheimer Disease
Insulin-degrading enzyme prevents ?-synuclein fibril formation in a nonproteolytical manner.
Alzheimer Disease
Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo.
Alzheimer Disease
Insulin-degrading enzyme secretion from astrocytes is mediated by an autophagy-based unconventional secretory pathway in Alzheimer disease.
Alzheimer Disease
Insulin-degrading enzyme, apolipoprotein E, and Alzheimer's disease.
Alzheimer Disease
Insulin-Degrading Enzyme: A Link between Alzheimer's and Type 2 Diabetes Mellitus.
Alzheimer Disease
Insulin-degrading enzyme: new therapeutic target for diabetes and Alzheimer's disease?
Alzheimer Disease
Insulysin hydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques.
Alzheimer Disease
Insulysin: an allosteric enzyme as a target for Alzheimer's disease.
Alzheimer Disease
Lack of association of 5 SNPs in the vicinity of the insulin-degrading enzyme (IDE) gene with late-onset Alzheimer's disease.
Alzheimer Disease
Links between Alzheimer's disease and diabetes.
Alzheimer Disease
Meta-analysis of the insulin degrading enzyme polymorphisms and susceptibility to Alzheimer's disease.
Alzheimer Disease
Metformin Ameliorates A? Pathology by Insulin-Degrading Enzyme in a Transgenic Mouse Model of Alzheimer's Disease.
Alzheimer Disease
Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme.
Alzheimer Disease
Multiple insulin degrading enzyme variants alter in vitro reporter gene expression.
Alzheimer Disease
Mutation screening of a haplotype block around the insulin degrading enzyme gene and association with Alzheimer's disease.
Alzheimer Disease
Neprilysin and insulin-degrading enzyme levels are increased in Alzheimer disease in relation to disease severity.
Alzheimer Disease
No association between the insulin degrading enzyme gene and Alzheimer's disease in a Japanese population.
Alzheimer Disease
Non-covalent interaction of ubiquitin with insulin-degrading enzyme.
Alzheimer Disease
Optimization of Peptide hydroxamate inhibitors of insulin-degrading enzyme reveals marked substrate-selectivity.
Alzheimer Disease
Physiological effects of manipulating the level of insulin-degrading enzyme in insulin-producing cells of Drosophila.
Alzheimer Disease
Plaque-associated overexpression of insulin-degrading enzyme in the cerebral cortex of aged transgenic tg2576 mice with Alzheimer pathology.
Alzheimer Disease
Polymorphisms of insulin degrading enzyme gene are not associated with Alzheimer's disease.
Alzheimer Disease
Positive association between risk for late-onset Alzheimer disease and genetic variation in IDE.
Alzheimer Disease
PPARgamma transcriptionally regulates the expression of insulin-degrading enzyme in primary neurons.
Alzheimer Disease
Promoter polymorphisms which modulate insulin degrading enzyme expression may increase susceptibility to Alzheimer's disease.
Alzheimer Disease
Protective effect of Notoginsenoside R1 on an APP/PS1 mouse model of Alzheimer's disease by up-regulating insulin degrading enzyme and inhibiting A? accumulation.
Alzheimer Disease
QM/MM Simulations of Amyloid-? 42 Degradation by IDE in the Presence and Absence of ATP.
Alzheimer Disease
Redox regulation of insulin degradation by insulin-degrading enzyme.
Alzheimer Disease
Reduced hippocampal insulin-degrading enzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele.
Alzheimer Disease
Regulatory feedback cycle of the insulin-degrading enzyme and the amyloid precursor protein intracellular domain: Implications for Alzheimer's disease.
Alzheimer Disease
Sequence variants of IDE are associated with the extent of beta-amyloid deposition in the Alzheimer's disease brain.
Alzheimer Disease
Sequence variation in the proximity of IDE may impact age at onset of both Parkinson disease and Alzheimer disease.
Alzheimer Disease
Small-molecule activators of insulin-degrading enzyme discovered through high-throughput compound screening.
Alzheimer Disease
Somatostatin: a novel substrate and a modulator of insulin-degrading enzyme activity.
Alzheimer Disease
Statins induce insulin-degrading enzyme secretion from astrocytes via an autophagy-based unconventional secretory pathway.
Alzheimer Disease
Structure based discovery of small molecules to regulate the activity of human insulin degrading enzyme.
Alzheimer Disease
Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE.
Alzheimer Disease
Substantial linkage disequilibrium across the insulin-degrading enzyme locus but no association with late-onset Alzheimer's disease.
Alzheimer Disease
The Association Between Small Vessel Infarcts and the Activities of Amyloid-? Peptide Degrading Proteases in Apolipoprotein E4 AlleleCarriers.
Alzheimer Disease
The association between two single nucleotide polymorphisms within the insulin-degrading enzyme gene and Alzheimer's disease in a Chinese Han population.
Alzheimer Disease
The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid beta peptide: implications for Alzheimer disease pathogenesis.
Alzheimer Disease
The core sequence of PIF competes for insulin/amyloid ? in insulin degrading enzyme: potential treatment for Alzheimer's disease.
Alzheimer Disease
The extracellular matrix enriched with membrane metalloendopeptidase and insulin-degrading enzyme suppresses the deposition of amyloid-beta peptide in Alzheimer's disease cell models.
Alzheimer Disease
The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: a biological perspective.
Alzheimer Disease
The metalloendopeptidase gene Pitrm1 is regulated by hedgehog signaling in the developing mouse limb and is expressed in muscle progenitors.
Alzheimer Disease
The role of insulin, insulin growth factor, and insulin-degrading enzyme in brain aging and Alzheimer's disease.
Alzheimer Disease
Toward Allosterically Increased Catalytic Activity of Insulin-Degrading Enzyme against Amyloid Peptides.
Alzheimer Disease
Ubiquitin is a novel substrate for human insulin-degrading enzyme.
Alzheimer Disease
[Cerebral proteolysis of amiloid-b peptide: relevance of insulin-degrading enzyme in Alzheimer's disease]
Alzheimer Disease
[Effect of tongluo xingnao effervescent tablet on learning and memory of AD rats and expression of insulin-degrading enzyme in hippocampus].
Alzheimer Disease
[Kidney-reinforcing and Governor Vessel-regulating EA Intervention May Improve Learningmemory Possibly by Suppressing Formation of Senile Plaques in Hippocampus in APP/PS 1 Double Transgenic Alzheimer's Disease Mice].
Amyloidosis
Insulin-degrading enzyme deficiency accelerates cerebrovascular amyloidosis in an animal model.
Atherosclerosis
Insulin-degrading enzyme deficiency in bone marrow cells increases atherosclerosis in LDL receptor-deficient mice.
Brain Infarction
The Association Between Small Vessel Infarcts and the Activities of Amyloid-? Peptide Degrading Proteases in Apolipoprotein E4 AlleleCarriers.
Brain Ischemia
Pyrrolidine dithiocarbamate attenuates brain A? increase and improves long-term neurological outcome in rats after transient focal brain ischemia.
Carcinoma
Complex formation between metabolic enzymes in tumor cells: Unfolding the MDR1-IDE paradigm.
Carcinoma, Hepatocellular
Association of insulin-degrading enzyme with a 70 kDa cytosolic protein in hepatoma cells.
Carcinoma, Hepatocellular
Dexamethasone inhibits insulin binding to insulin-degrading enzyme and cytosolic insulin-binding protein p82.
Carcinoma, Hepatocellular
Identification of insulin-degrading enzyme on the surface of cultured human lymphocytes, rat hepatoma cells, and primary cultures of rat hepatocytes.
Carcinoma, Hepatocellular
In vivo association of [125I]-insulin with a cytosolic insulin-degrading enzyme: detection by covalent cross-linking and immunoprecipitation with a monoclonal antibody.
Carcinoma, Hepatocellular
Inhibition of insulin-degrading enzyme increases translocation of insulin to the nucleus in H35 rat hepatoma cells: evidence of a cytosolic pathway.
Cardiovascular Diseases
Effect of the Interplay Between Genetic and Behavioral Risks on Survival After Age 75.
Cerebellar Ataxia
Loss of function of the mitochondrial peptidase PITRM1 induces proteotoxic stress and Alzheimer's disease-like pathology in human cerebral organoids.
Cerebral Amyloid Angiopathy
Insulin-degrading enzyme in brain microvessels: proteolysis of amyloid {beta} vasculotropic variants and reduced activity in cerebral amyloid angiopathy.
Cerebral Amyloid Angiopathy
Memantine, a Noncompetitive N-Methyl-D-Aspartate Receptor Antagonist, Attenuates Cerebral Amyloid Angiopathy by Increasing Insulin-Degrading Enzyme Expression.
Cerebral Amyloid Angiopathy
Metformin attenuates vascular pathology by increasing expression of insulin-degrading enzyme in a mixed model of cerebral amyloid angiopathy and type 2 diabetes mellitus.
Chickenpox
Binding varicella zoster virus: an underestimated facet of insulin-degrading enzyme´s implication for Alzheimer´s disease pathology?
Chickenpox
Development of monoclonal antibodies and quantitative ELISAs targeting insulin-degrading enzyme.
Chickenpox
Insulin degrading enzyme binds to the nonglycosylated precursor of varicella zoster virus gE protein found in the endoplasmic reticulum.
Colonic Neoplasms
Immunohistochemical localization of insulin-degrading enzyme along the rat intestine, in the human colon adenocarcinoma cell line (Caco-2), and in human ileum.
Colonic Neoplasms
Insulin-degrading enzyme in a human colon adenocarcinoma cell line (Caco-2).
Dementia
Accumulation of BRI2-BRICHOS ectodomain correlates with a decreased clearance of A? by insulin degrading enzyme (IDE) in Alzheimer's disease.
Dementia
Differential degradation of amyloid beta genetic variants associated with hereditary dementia or stroke by insulin-degrading enzyme.
Dementia
IDE Gene Polymorphism Influences on BPSD in Mild Dementia of Alzheimer's Type.
Dementia
Insulin-degrading enzyme degrades amyloid peptides associated with British and Danish familial dementia.
Dementia
Insulin-degrading enzyme haplotypes affect insulin levels but not dementia risk.
Dementia
Machine Learning and Molecular Dynamics Based Insights into Mode of Actions of Insulin Degrading Enzyme Modulators.
Dementia
Transducible P11-CNTF rescues the learning and memory impairments induced by amyloid-beta peptide in mice.
Dementia
[Effect of tongluo xingnao effervescent tablet on learning and memory of AD rats and expression of insulin-degrading enzyme in hippocampus].
Dementia, Vascular
[Effect of rehabilitation training on insulin-resistance and hippocampus amyloid-beta peptide in rats with vascular dementia].
Diabetes Mellitus
Development of monoclonal antibodies and quantitative ELISAs targeting insulin-degrading enzyme.
Diabetes Mellitus
Han ethnicity-specific type 2 diabetic treatment from traditional Chinese medicine?
Diabetes Mellitus
Insulin-degrading enzyme antagonizes insulin-dependent tissue growth and Abeta-induced neurotoxicity in Drosophila.
Diabetes Mellitus
Insulin-degrading enzyme is exported via an unconventional protein secretion pathway.
Diabetes Mellitus
Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo.
Diabetes Mellitus
Insulin-Degrading Enzyme: A Link between Alzheimer's and Type 2 Diabetes Mellitus.
Diabetes Mellitus
Interleukin-6 increases the expression and activity of insulin-degrading enzyme.
Diabetes Mellitus
Metformin attenuates vascular pathology by increasing expression of insulin-degrading enzyme in a mixed model of cerebral amyloid angiopathy and type 2 diabetes mellitus.
Diabetes Mellitus
PPARgamma transcriptionally regulates the expression of insulin-degrading enzyme in primary neurons.
Diabetes Mellitus
Redox regulation of insulin degradation by insulin-degrading enzyme.
Diabetes Mellitus
Structure based discovery of small molecules to regulate the activity of human insulin degrading enzyme.
Diabetes Mellitus
Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus.
Diabetes Mellitus, Type 2
A neglected modulator of insulin-degrading enzyme activity and conformation: The pH.
Diabetes Mellitus, Type 2
Association and haplotype analysis of the insulin-degrading enzyme (IDE) gene, a strong positional and biological candidate for type 2 diabetes susceptibility.
Diabetes Mellitus, Type 2
Association of polymorphisms in the insulin-degrading enzyme gene with type 2 diabetes in the Korean population.
Diabetes Mellitus, Type 2
C allele of the rs2209972 single nucleotide polymorphism of the insulin degrading enzyme gene and Alzheimer's disease in type 2 diabetes, a case control study.
Diabetes Mellitus, Type 2
Development of monoclonal antibodies and quantitative ELISAs targeting insulin-degrading enzyme.
Diabetes Mellitus, Type 2
Ensemble cryoEM elucidates the mechanism of insulin capture and degradation by human insulin degrading enzyme.
Diabetes Mellitus, Type 2
Enzyme kinetics from circular dichroism of insulin reveals mechanistic insights into the regulation of insulin-degrading enzyme.
Diabetes Mellitus, Type 2
FADD Phosphorylation Modulates Blood Glucose Levels by Decreasing the Expression of Insulin-Degrading Enzyme.
Diabetes Mellitus, Type 2
GLP-1 receptor regulates cell growth through regulating IDE expression level in A?1-42-treated PC12 cells.
Diabetes Mellitus, Type 2
Han ethnicity-specific type 2 diabetic treatment from traditional Chinese medicine?
Diabetes Mellitus, Type 2
High-Density Haplotype Structure and Association Testing of the Insulin-Degrading Enzyme (IDE) Gene With Type 2 Diabetes in 4,206 People.
Diabetes Mellitus, Type 2
IDE (rs6583817) polymorphism and type 2 diabetes differentially modify executive function in older adults.
Diabetes Mellitus, Type 2
Insulin degrading enzyme contributes to the pathology in a mixed model of Type 2 diabetes and Alzheimer's disease: possible mechanisms of IDE in T2D and AD.
Diabetes Mellitus, Type 2
Insulin-degrading enzyme antagonizes insulin-dependent tissue growth and Abeta-induced neurotoxicity in Drosophila.
Diabetes Mellitus, Type 2
Insulin-degrading enzyme inhibition, a novel therapy for type 2 diabetes?
Diabetes Mellitus, Type 2
Insulin-degrading enzyme is exported via an unconventional protein secretion pathway.
Diabetes Mellitus, Type 2
Insulin-degrading enzyme prevents ?-synuclein fibril formation in a nonproteolytical manner.
Diabetes Mellitus, Type 2
Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo.
Diabetes Mellitus, Type 2
Insulin-Degrading Enzyme: A Link between Alzheimer's and Type 2 Diabetes Mellitus.
Diabetes Mellitus, Type 2
Insulin-degrading enzyme: new therapeutic target for diabetes and Alzheimer's disease?
Diabetes Mellitus, Type 2
Interleukin-6 increases the expression and activity of insulin-degrading enzyme.
Diabetes Mellitus, Type 2
Metformin attenuates vascular pathology by increasing expression of insulin-degrading enzyme in a mixed model of cerebral amyloid angiopathy and type 2 diabetes mellitus.
Diabetes Mellitus, Type 2
Pancreatic beta-cell-specific deletion of insulin-degrading enzyme leads to dysregulated insulin secretion and beta-cell functional immaturity.
Diabetes Mellitus, Type 2
Polymorphisms in the insulin-degrading enzyme gene are associated with type 2 diabetes in men from the NHLBI Framingham Heart Study.
Diabetes Mellitus, Type 2
Polymorphisms within insulin-degrading enzyme (IDE) gene determine insulin metabolism and risk of type 2 diabetes.
Diabetes Mellitus, Type 2
PPARgamma transcriptionally regulates the expression of insulin-degrading enzyme in primary neurons.
Diabetes Mellitus, Type 2
Quantitative trait loci near the insulin-degrading enzyme (IDE) gene contribute to variation in plasma insulin levels.
Diabetes Mellitus, Type 2
Redox regulation of insulin degradation by insulin-degrading enzyme.
Diabetes Mellitus, Type 2
Regulation of insulin degrading enzyme activity by obesity-associated factors and pioglitazone in liver of diet-induced obese mice.
Diabetes Mellitus, Type 2
Structure based discovery of small molecules to regulate the activity of human insulin degrading enzyme.
Diabetes Mellitus, Type 2
Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus.
Epilepsy
In-frame deletion in canine PITRM1 is associated with a severe early-onset epilepsy, mitochondrial dysfunction and neurodegeneration.
Glioma
Expression of IDE and PITRM1 genes in ERN1 knockdown U87 glioma cells: effect of hypoxia and glucose deprivation.
Glucose Intolerance
Alternative splicing of human insulin-degrading enzyme yields a novel isoform with a decreased ability to degrade insulin and amyloid beta-protein.
Glucose Intolerance
Catalytic site inhibition of insulin-degrading enzyme by a small molecule induces glucose intolerance in mice.
Glucose Intolerance
Liver-specific ablation of insulin-degrading enzyme causes hepatic insulin resistance and glucose intolerance, without affecting insulin clearance in mice.
Granuloma
Severe insulin resistance associated with subcutaneous amyloid deposition.
Heart Failure
Synthesis, secretion, function, metabolism and application of natriuretic peptides in heart failure.
Herpes Zoster
Binding varicella zoster virus: an underestimated facet of insulin-degrading enzyme´s implication for Alzheimer´s disease pathology?
Herpes Zoster
Development of monoclonal antibodies and quantitative ELISAs targeting insulin-degrading enzyme.
Herpes Zoster
Insulin degrading enzyme binds to the nonglycosylated precursor of varicella zoster virus gE protein found in the endoplasmic reticulum.
Hyperglycemia
Rat brain insulin degrading enzyme in insulin and thyroid hormones imbalances.
Hyperglycemia
Type 2 Diabetes Mellitus and Alzheimer's Disease: from physiopathology to treatment implications.
Hyperinsulinism
Alternative splicing of human insulin-degrading enzyme yields a novel isoform with a decreased ability to degrade insulin and amyloid beta-protein.
Hyperinsulinism
Hyperinsulinemia caused by dexamethasone treatment is associated with reduced insulin clearance and lower hepatic activity of insulin-degrading enzyme.
Hyperinsulinism
Nigella sativa Oil and Chromium Picolinate Ameliorate Fructose-Induced Hyperinsulinemia by Enhancing Insulin Signaling and Suppressing Insulin-Degrading Enzyme in Male Rats.
Hyperinsulinism
Rat brain insulin degrading enzyme in insulin and thyroid hormones imbalances.
Hyperinsulinism
Reduced Insulin Clearance and Insulin-Degrading Enzyme Activity Contribute to Hyperinsulinemia in African Americans.
Hyperinsulinism
[Dementia and diabetes: Casual or causal relationship?]
Hypertension
Angiotensin-converting enzyme as a potential target for treatment of Alzheimer's disease: inhibition or activation?
Hypertension
Effects of Hypertension and Anti-Hypertensive Treatment on Amyloid-? (A?) Plaque Load and A?-Synthesizing and A?-Degrading Enzymes in Frontal Cortex.
Hyperthyroidism
Rat brain insulin degrading enzyme in insulin and thyroid hormones imbalances.
Hypothyroidism
Rat brain insulin degrading enzyme in insulin and thyroid hormones imbalances.
Infections
The amino terminus of varicella-zoster virus (VZV) glycoprotein E is required for binding to insulin-degrading enzyme, a VZV receptor.
Infections
The insulin degrading enzyme binding domain of varicella-zoster virus (VZV) glycoprotein E is important for cell-to-cell spread and VZV infectivity, while a glycoprotein I binding domain is essential for infection.
Infections
Varicella-zoster virus glycoprotein E is a critical determinant of virulence in the SCID mouse-human model of neuropathogenesis.
Insulin Resistance
Diet-induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease.
Insulin Resistance
Effect of pioglitazone on altered expression of A? metabolism-associated molecules in the brain of fructose-drinking rats, a rodent model of insulin resistance.
Insulin Resistance
Links between Alzheimer's disease and diabetes.
Insulin Resistance
Liver-specific ablation of insulin-degrading enzyme causes hepatic insulin resistance and glucose intolerance, without affecting insulin clearance in mice.
Insulin Resistance
Modulation of Insulin Sensitivity by Insulin-Degrading Enzyme.
Insulin Resistance
Reduced insulin clearance and lower insulin-degrading enzyme expression in the liver might contribute to the thrifty phenotype of protein-restricted mice.
Insulin Resistance
Reduced insulin sensitivity and increased ?/? cell mass is associated with reduced hepatic insulin-degrading enzyme activity in pregnant rats.
Insulin Resistance
Relationship between insulin-degrading enzyme activity and insulin sensitivity in cell model of insulin-resistance.
Insulin Resistance
Therapeutic Strategies for Alzheimer's Disease in the View of Diabetes Mellitus.
Insulin Resistance
[Dementia and diabetes: Casual or causal relationship?]
Insulinoma
An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures.
insulysin deficiency
Insulin-degrading enzyme deficiency accelerates cerebrovascular amyloidosis in an animal model.
insulysin deficiency
Insulin-degrading enzyme deficiency in bone marrow cells increases atherosclerosis in LDL receptor-deficient mice.
insulysin deficiency
Loss of function of the mitochondrial peptidase PITRM1 induces proteotoxic stress and Alzheimer's disease-like pathology in human cerebral organoids.
insulysin deficiency
Role of PITRM1 in Mitochondrial Dysfunction and Neurodegeneration.
Intellectual Disability
Defective PITRM1 mitochondrial peptidase is associated with A? amyloidotic neurodegeneration.
Liver Cirrhosis
Insulin-degrading activity in experimental liver cirrhosis of the rat.
Metabolic Syndrome
Insulin-degrading enzyme higher in subjects with metabolic syndrome.
Metabolic Syndrome
Variants in the insulin-degrading enzyme gene are associated with metabolic syndrome in Chinese elders.
Neoplasms
Adiponectin receptor fragmentation in mouse models of type 1 and type 2 diabetes.
Neoplasms
Attenuation of Aluminum Chloride-Induced Neuroinflammation and Caspase Activation Through the AKT/GSK-3? Pathway by Hesperidin in Wistar Rats.
Neoplasms
Autophagy-dependent secretion: mechanism, factors secreted, and disease implications.
Neoplasms
Dendrobiumpolysaccharides attenuate cognitive impairment in senescence-accelerated mouse prone 8 mice via modulation of microglial activation.
Neoplasms
Immunohistochemical evidence of ubiquitous distribution of the metalloendoprotease insulin-degrading enzyme (IDE; insulysin) in human non-malignant tissues and tumor cell lines.
Neoplasms
Insulin supplementation attenuates cancer-induced cardiomyopathy and slows tumor disease progression.
Neoplasms
Intracellular insulin in human tumors: examples and implications.
Neoplasms
Isorhynchophylline ameliorates cognitive impairment via modulating amyloid pathology, tau hyperphosphorylation and neuroinflammation: Studies in a transgenic mouse model of Alzheimer's disease.
Neoplasms
Lack of association between IDE genetic variability and Down's syndrome.
Neoplasms
No major role for insulin-degrading enzyme in antigen presentation by MHC molecules.
Neoplasms
One for all and all for one: RB defends the cell while IDE, PTEN and IGFBP-7 antagonize insulin and IGFs to protect RB.
Neoplasms
Production of an antigenic peptide by insulin-degrading enzyme.
Neuroblastoma
Novel Platinum(II) compounds modulate insulin-degrading enzyme activity and induce cell death in neuroblastoma cells.
Neuroblastoma
Regulation by retinoic acid of insulin-degrading enzyme and of a related endoprotease in human neuroblastoma cell lines.
Neurodegenerative Diseases
Age-associated neurodegeneration and oxidative damage to lipids, proteins and DNA.
Neurodegenerative Diseases
Insulin-degrading enzyme: an ally against metabolic and neurodegenerative diseases.
Neuroinflammatory Diseases
Intranasal Losartan Decreases Perivascular Beta Amyloid, Inflammation, and the Decline of Neurogenesis in Hypertensive Rats.
Neuroinflammatory Diseases
Sodium orthovanadate improves learning and memory in intracerebroventricular-streptozotocin rat model of Alzheimer's disease through modulation of brain insulin resistance induced tau pathology.
Obesity
Dissecting the nutrigenomics, diabetes, and gastrointestinal disease interface: from risk assessment to health intervention.
Obesity
High-Fat Diet Modulates Hepatic Amyloid ? and Cerebrosterol Metabolism in the Triple Transgenic Mouse Model of Alzheimer's Disease.
Obesity
In vitro inhibition of insulin-degrading enzyme by long-chain fatty acids and their coenzyme A thioesters.
Obesity
Interleukin-6 increases the expression and activity of insulin-degrading enzyme.
Ovarian Neoplasms
Expression of metalloprotease insulin-degrading enzyme insulysin in normal and malignant human tissues.
Parkinson Disease
6-Hydroxydopamine induces secretion of PARK7/DJ-1 via autophagy-based unconventional secretory pathway.
Parkinsonian Disorders
6-Hydroxydopamine induces secretion of PARK7/DJ-1 via autophagy-based unconventional secretory pathway.
Polycystic Ovary Syndrome
Association of genetic variants of insulin degrading enzyme with metabolic features in women with polycystic ovary syndrome.
Prediabetic State
Relationship Between Cognitive Functions and Insulin-degrading Enzyme in Individuals With Prediabetes.
Retinoblastoma
Intracellular insulin in human tumors: examples and implications.
Retinoblastoma
Retinoblastoma protein co-purifies with proteasomal insulin-degrading enzyme: implications for cell proliferation control.
Spinocerebellar Ataxias
Defective PITRM1 mitochondrial peptidase is associated with A? amyloidotic neurodegeneration.
Spinocerebellar Ataxias
In-frame deletion in canine PITRM1 is associated with a severe early-onset epilepsy, mitochondrial dysfunction and neurodegeneration.
Stroke
Differential degradation of amyloid beta genetic variants associated with hereditary dementia or stroke by insulin-degrading enzyme.
Varicella Zoster Virus Infection
Development of monoclonal antibodies and quantitative ELISAs targeting insulin-degrading enzyme.
Virus Diseases
Development of monoclonal antibodies and quantitative ELISAs targeting insulin-degrading enzyme.
Virus Diseases
Insulin degrading enzyme is a cellular receptor mediating varicella-zoster virus infection and cell-to-cell spread.
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0.0022
amyloid beta-peptide 1-40
pH not specified in the publication, temperature not specified in the publication
-
0.0004
amyloid beta-peptide 1-42
pH not specified in the publication, temperature not specified in the publication
-
1.2 - 7.5
(7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH
0.028
(7-methoxycoumarin-4-yl)acetyl-NPPGFSAFK-2,4-dinitrophenyl
-
pH not specified in the publication, 37°C
0.29 - 1.1
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
0.23
(7-methoxycoumarin-4-yl)acetyl-RPPGFSAFK(2,4-dinitrophenyl)-OH
37°C, pH not specified in the publication
0.088 - 0.24
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
1.2 - 6.5
7-methoxycoumarin-4-yl-acetyl-RPPGFSAFK-2,4-dinitrophenyl
0.003 - 2.42
Abz-GGFLRKHGQ-EDDnp
70
amyloid beta
-
pH 8.0, 37°C, wild-type enzyme
-
8 - 20
amyloid beta-peptide1-40
-
0.17 - 0.88
amyloid beta-protein
-
8
amyloid beta1-40
-
pH 7.3, 37°C
-
61 - 62.7
Dabcyl-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Glu(EDANS)-NH2
0.0025
insulin-like peptide 3
-
pH 7.7, 37°C
-
10
protein ANP
-
pH not specified in the publication, 37°C
-
0.2
protein BNP
-
pH not specified in the publication, 37°C
-
20
protein CNP
-
pH not specified in the publication, 37°C
-
0.1
protein DNP
-
pH not specified in the publication, 37°C
-
0.38
Somatostatin
-
pH 7.3, 37°C
2
urodilatin
-
pH not specified in the publication, 37°C
-
1.2
(7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH
pH 7.0, 37°C, mutant enzyme R183Q
7.5
(7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH
pH 7.0, 37°C, wild-type enzyme
0.29
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F820Y
0.298
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme Y150K
0.33
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme 141A
0.338
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme Y150F
0.45
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme Y150W
0.53
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F202D
0.57
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme W199Y
0.57
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, wild-type enzyme
0.625
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme 141W
0.72
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F115Y
0.725
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F115A
0.73
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F115W
0.735
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F202Y
0.78
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme 141Y
0.803
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F202W
0.85
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F820W
1.1
(7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme Y150F
0.088
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme W199K
0.095
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme Y150K
0.097
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F202D
0.097
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F202K
0.1
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F141W
0.108
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F820Y
0.123
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F141N
0.143
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme Y150W
0.148
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F202W
0.16
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F820W
0.16
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme W199Y
0.17
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F202N
0.177
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme W199N
0.178
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F141Y
0.18
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme W199A
0.198
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, wild-type enzyme
0.2
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F115Y
0.22
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F141A
0.22
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme Y150F
0.24
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme F202Y
0.24
(7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH
pH 7.3, 37°C, mutant enzyme W199F
1.2
7-methoxycoumarin-4-yl-acetyl-RPPGFSAFK-2,4-dinitrophenyl
pH 7.0, 37°C, mutant enzyme R183Q
6.5
7-methoxycoumarin-4-yl-acetyl-RPPGFSAFK-2,4-dinitrophenyl
pH 7.0, 37°C, wild-type enzyme
0.003
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, mutant Y609F IDE:IDE mutant E111F/Y609F
0.01
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, IDE:IDE mutant E111F/Y609F
0.01
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, mutant Y609F IDE:IDE mutant E111F
0.03
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, IDE:IDE mutant H112Q/Y609F
0.03
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, mutant Y609F IDE:IDE mutant Y609F
0.05
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, mutant Y609F IDE:IDE mutant H112Q
0.06
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, mutant Y609F IDE:IDE mutant H112Q/Y609F
0.12
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, IDE:IDE mutant H112Q
0.14
Abz-GGFLRKHGQ-EDDnp
-
pH 7.4, 37°C, IDE:IDE, wild-type
1.13
Abz-GGFLRKHGQ-EDDnp
pH 7.7, 37°C, mutant enzyme D426A
1.68
Abz-GGFLRKHGQ-EDDnp
pH 7.7, 37°C, mutant enzyme F807A
1.7
Abz-GGFLRKHGQ-EDDnp
pH 7.7, 37°C, wild-type enzyme
1.83
Abz-GGFLRKHGQ-EDDnp
pH 7.7, 37°C, mutant enzyme K364A
1.97
Abz-GGFLRKHGQ-EDDnp
pH 7.7, 37°C, mutant enzyme S137A
2.42
Abz-GGFLRKHGQ-EDDnp
pH 7.7, 37°C, mutant enzyme K898A
8
amyloid beta-peptide1-40
recombinant wild-type enzyme, pH 7.4, 37°C
-
20
amyloid beta-peptide1-40
recombinant mutant D426C/K899C, pH 7.4, 37°C
-
0.17
amyloid beta-protein
isoform 15b-IDE, pH 7.4, 37°C
-
0.88
amyloid beta-protein
isoform 15a-IDE, pH 7.4, 37°C
-
61
Dabcyl-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Glu(EDANS)-NH2
-
pH 7.3, 37°C, presence of 0.04 mM somatostatin
62.7
Dabcyl-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Glu(EDANS)-NH2
-
pH 7.3, 37°C
0.017
Insulin
isoform 15b-IDE, pH 7.4, 37°C
-
0.025
Insulin
isoform 15a-IDE, pH 7.4, 37°C
-
0.048
Insulin
pH 7.4, 37°C
-
0.05
Insulin
-
pH 7.7, 37°C
-
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0.0004
((((S)-1-benzylcarbamoyl-2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0005
((((S)-2-(1H-imidazol-4-yl)-1-(3-methyl-(1,2,4)oxadiazol-5-yl)-ethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0001
((((S)-2-(1H-imidazol-4-yl)-1-methylcarbamoylethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0016
((((S)-2-hydroxy-1-(1H-imidazol-4-ylmethyl)-ethylcarbamoyl)-methyl)-(3-phenyl-propyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0014
(benzyl-(((S)-1-benzylcarbamoyl-2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0014
(benzyl-(((S)-1-carbamoyl-2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0069
(benzyl-(((S)-1-dimethylcarbamoyl-2-(1H-imidazol-4-yl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0006
(benzyl-(((S)-2-(1H-imidazol-4-yl)-1-methylcarbamoylethylcarbamoyl)-methyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0041
(benzyl-(((S)-2-hydroxy-1-(1H-imidazol-4-ylmethyl)-ethylcarbamoyl)-methyl)-amino)-acetic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0029
(S)-2-(2-((4-tert-butyl-benzyl)-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0125
(S)-2-(2-(benzyl-(2-hydroxy-3,4-dioxo-cyclobut-1-enyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0003
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid isopropyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0029
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0008
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid tert-butyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0006
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-3-(3H-imidazol-4-yl)-propionic acid isobutyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0363
(S)-2-(2-(benzyl-carboxymethyl-amino)-acetylamino)-5-guanidino-pentanoic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0032
(S)-2-(2-(benzyl-hydroxycarbamoylmethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0006
(S)-2-(2-(carboxymethyl-(1-methyl-3-phenyl-propyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0012
(S)-2-(2-(carboxymethyl-(2-(1H-indol-3-yl)-ethyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.001
(S)-2-(2-(carboxymethyl-(3-phenyl-propyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0004
(S)-2-(2-(carboxymethyl-(3-phenyl-propyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid tert-butyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0025
(S)-2-(2-(carboxymethyl-(4-fluoro-benzyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0017
(S)-2-(2-(carboxymethyl-(4-methyl-benzyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0006
(S)-2-(2-(carboxymethyl-(4-phenyl-butyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.002
(S)-2-(2-(carboxymethyl-(4-trifluoromethyl-benzyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0004
(S)-2-(2-(carboxymethyl-(n-hexyl)-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0012
(S)-2-(2-(carboxymethyl-naphthalen-2-ylmethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0014
(S)-2-(2-(carboxymethyl-phenethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0063
(S)-2-(2-(carboxymethyl-pyridin-4-ylmethyl-amino)-acetylamino)-3-(1H-imidazol-4-yl)-propionic acid methyl ester
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.0036
3-(((S)-1-methoxy-1-oxo-3-imidazol-2-yl)carbamoyl)-1,2,3,4-tetrahydroisoquinoline-2-ethanoic acid
Homo sapiens
in HEPES 50 mM, NaCl 100 mM, pH 7.4, at 37°C
0.9
hydrogen peroxide
Homo sapiens
-
pH 8.0, 37°C
0.000018
methyl [(2S)-2-(5-[5-[4-([(2S)-2-[(3S)-3-amino-2-oxopiperidin-1-yl]-2-cyclohexylacetyl]amino)phenyl]pentyl]-2-fluorophenyl)-3-(quinolin-3-yl)propyl]carbamate
Homo sapiens
37°C, pH 7.5
0.000015
methyl [(2S)-2-[4-([5-[4-([(2S)-2-[(3S)-3-amino-2-oxopiperidin-1-yl]-2-cyclohexylacetyl]amino)phenyl]pentyl]oxy)phenyl]-3-(quinolin-3-yl)butyl]carbamate
Homo sapiens
37°C, pH 7.5
0.04
protein ANP
Homo sapiens
-
pH not specified in the publication, 37°C
-
0.12
protein BNP
Homo sapiens
-
pH not specified in the publication, 37°C
-
0.07
protein CNP
Homo sapiens
-
pH not specified in the publication, 37°C
-
1.3
protein DNP
Homo sapiens
-
pH not specified in the publication, 37°C
-
1.2
S-nitrosoglutathione
Homo sapiens
-
pH 8.0, 37°C
0.09
ubiquitin
Homo sapiens
-
pH not specified in the publication, 37°C
0.8
urodilatin
Homo sapiens
-
pH not specified in the publication, 37°C
-
0.11
bacitracin
Homo sapiens
recombinant wild-type enzyme, in in presence of ATP
0.18
bacitracin
Homo sapiens
recombinant mutant D426C/K899C, in in presence of ATP
0.2
bacitracin
Homo sapiens
recombinant mutant D426C/K899C, in absence of ATP
0.4
bacitracin
Homo sapiens
recombinant wild-type enzyme, in absence of ATP
0.001
Ub1-72
Homo sapiens
-
pH not specified in the publication, 37°C
-
0.1
Ub1-72
Homo sapiens
-
pH not specified in the publication, 37°C
-
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A140D
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
A140F
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
A140K
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
A140N
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
A140W
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
A140Y
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
C819A
-
thiol-directed modification of C819 likely causes local structure perturbation to reduce substrate binding and catalysis
D426A
mutation diminishes activity
E107Q
catalytically inactive mutant
E110Q
-
structure comparison to wild-type enzyme structure
E111F
-
a mixed dimer in which one subunit contains the wild-type sequence and the other contains a E111F mutation that permits substrate binding, but not catalysis (E111F), exhibits a decrease in turnover number. A mixed dimer consisting of IDE:mutant E111F/Y609F IDE shows a high reduction in kcat, Km (Abz-GGFLRKHGQ-EDDnp) is 66% reduced compared to wild-type. Mixed dimer IDE:mutant E111F in which the inactive subunit can bind substrate exhibites a decreased activity than wild-type IDE towards substrate amyloid beta peptide
E341A
-
mutant is active in degrading substrate V, relative activity closed to wild-type
E341K
-
mutant is active in degrading substrate V, relative activity 15% compared to wild-type. Exosite mutant is unable to further degrade the Ub1-74 fragment
E341Q
-
mutant is active in degrading substrate V, relative activity 20% compared to wild-type. Exosite mutant is unable to further degrade the Ub1-74 fragment
F530A
the mutation renders the enzyme hyperactive, with up to a 20fold enhancement in degrading activity
F807A
mutation decreass the Km-value of the amyloid beta substrate
G339P
-
mutant is active in degrading substrate V, relative activity 75% compared to wild-type. Exosite mutant is unable to further degrade the Ub1-74 fragment
G361A/G362A
the mutant has reduced enzymatic activity
G361P
-
mutant is active in degrading substrate V, relative activity 80% compared to wild-type. Exosite mutant is unable to further degrade the Ub1-74 fragment
H112Q
-
a mixed dimer composed of one wild-type subunit and the other subunit containing a H112Q mutation that neither permits substrate binding nor catalysis exhibits the same turnover number per active subunit as wild-type IDE. Mixed oligomer IDE:IDE mutant H112Q shows similar kcat and Km (Abz-GGFLRKHGQ-EDDnp) compared to wild-type. Mixed dimer IDE:mutant H112Q IDE in which the inactive subunit does not bind substrate exhibits a slightly higher activity than wild-type IDE towards substrate amyloid beta peptide
K364A
mutation does not change the activity
N184C/Q828C
-
30-40fold increase in activity compared to wild-type
P284G
the mutation results in a slight reduction of enzyme catalysis
P286G
the mutation results in a significant reduction of enzyme catalysis
P289G
the mutant shows wild type activity
P292G
the mutation results in intermediate reduction of enzyme catalysis
R183a
about 35% of the activity compared to wild-type enzyme with the substrate
R183D
less than 5% of the activity compared to wild-type enzyme with the substrate (7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH
R183E
about less than 5% of the activity compared to wild-type enzyme with the substrate (7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH
R183K
about 30% of the activity compared to wild-type enzyme with the substrate (7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH
R183N
about 10% of the activity compared to wild-type enzyme with the substrate (7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH
R183Q
mutant Pitrm1 R183Q is implicated in inherited amyloidogenic neuropathy. Recombinant R183Q mutant is less active than the recombinant wild-type enzyme against recombinant amyloid beta-peptide (Abeta1-40). R183Q mutant enzyme exhibits significantly decreased rate of fluorogenic peptide hydrolysis ((7-methoxycoumarin-4-yl)acetyl-KLVFFAEDK(Dnp)-OH), yet retains similar binding affinity by comparison with the wild-type enzyme. Residue R183 is positioned within an N-terminal strand-loop-strand motif that is essential for enzyme function. A requirement for charged residues within 4.5 A of residue R183 is demonstrated. The R183Q mutant enzyme exhibits increased sensitivity to heat inactivation
R767A
the mutant exists mostly as a monomer
S137A
mutation decreass the Km-value of the amyloid beta substrate
Y496A
the mutation dramatically impairs the enzymatic activity
Y609F
-
mutation Y609F in the distal part of the substrate binding site of the active subunit blocks allosteric activation regardless of the activity of the other subunit. A mixed dimer consisting of mutant Y609F IDE: mutant E111F IDE shows a high reduction in kcat and a reduction in Km compared to wild-type. A mixed dimer consisting of mutant Y609F IDE: mutant E111F/Y609F IDE shows a high reduction in kcat, Km (Abz-GGFLRKHGQ-EDDnp) is 50% reduced compared to wild-type. Substrate amyloid beta peptide: When the distal site is mutated on both subunits (Y609F IDE:IDE Y609F) there is an even greater decrease in the reaction rate
Y831A
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
Y831D
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
Y831K
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
Y831N
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
Y831W
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
D426C/K899C
-
30-40fold increase in activity compared to wild-type
D426C/K899C
site-directed mutagenesis, hyperactive IDE mutation, the mutant shows increased activity, but reduced activationby ATP compared to the wild-type enzyme
E111Q
-
catalytically inactive mutant
E111Q
-
crystallization data
E111Q
site-directed mutagenesis, inactive mutant
E111Q
inactive enzyme form
E111Q
-
site-directed mutagenesis, the mtant shows highly reduced catalytic activity compared to the wild-typ enzyme
E111Q
-
catalysitcally inactive. Mutant forms ordered crystals of considerable size at a more rapid rate than the wild type
E111Q
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
K898A
mutation decreass the Km-value of the amyloid beta substrate
K898A
mutation results in increased catalytic activity
S132C/E817C
-
30-40fold increase in activity compared to wild-type
S132C/E817C
the mutant preferentially stays in the closed state
Y831F
site-directed mutagenesis, the mutant shows catalytic activity similar to the wild-type enzyme
Y831F
specific activity with the substrates (7-methoxycoumarin-4-yl)acetyl-VEALYLVCGEK(2,4-dinitrophenyl)-OH and (7-methoxycoumarin-4-yl)acetyl-QKLVFFAEDVK(2,4-dinitrophenyl)-OH is below 1 nmol/min*mg
additional information
-
chromosome 10-linked Alzheimer disease families show decreased enzyme activity
additional information
-
construction of transgenic mice, termed H1/siRNAinsulin-CMV/hIDE transgenic mice, TG9385, co-expressing specific insulin siRNA sequences and the human insulin degrading enzyme, hIDE, gene resulting in changes in the proteins in the endoplasmic reticulum stress signal pathway and a diabetes-like phenotype with impaired glucose tolerance and lower serum insulin levels compared to the wild-type mice, expression pattern in muscle, lung, brain, liver, kidney, heart, and intestine, tissue-specific regulation, overview
additional information
-
enzyme deficiency leads to development of either Alzheimer's disease and type 2 diabetes, overview
additional information
-
genotyping of single nucleotide polymorphisms in the IDE gene in Finnish patients with Alzheimer's disease, SNPs rs4646953 and rs4646955 to be associated with Alzheimer's disease, the insulin-degrading enzyme is genetically associated with Alzheimer's disease in the Finnish population, overview
additional information
-
human enzyme co-expression with specific insulin siRNA in H1/siRNAinsulin-CMV/hIDE transgenic mice, TG9385, using a chromosome integrated dual-recombinant expression system, in lung, brain, liver, kidney, heart, and intestine, with significantly increased enzyme level and activity in the liver, the transgenic mice show impaired glucose tolerance and reduced serum insulin levels compared to wild-type mice, down-regulation of gene transcripts in the liver of H1/siRNAinsulin-CMV/hIDE mice, gene ontology, overview
additional information
-
no correlation of single nucleotide polymorphisms and IDE haplotypes with the risk of dementia, overview
additional information
-
overexpression of insulysin in human amyloid precursor protein transgenic mice leads to a decrease in amyloid beta peptide levels
additional information
-
siRNA-mediated gene silencing of IDE in Hep-G2 cells leading to 50% reduction of IDE mRNA and protein, short-lived protein degradation is unchanged in the cells with reduced IDE expression, while long-lived and very-long-lived protein degradation is reduced, overview
additional information
-
construction of mutants lacking one or severall cysteine resiudes. A mutant devoid of all 13 cysteine residues is insensitive to the inhibition by S-nitrosoglutathione, hydrogen peroxide, or N-ethylmaleimide
additional information
-
construction of Cys residue mutants of IDE, properties of oxidized and/or nitrosylated mutant enzymes compared to wild-type enzyme, overview
additional information
-
IDE genotyping and identification of genetic variants, the A/T allele of IDE gene variant rs11187033 is associated with the metabolic syndrome, and might contribute to metabolic syndrome susceptibility in Chinese elders, overview
additional information
-
IDE genotyping identification of polymorphisms, three polymorphisms occur in IDE promoter: -1002T/G (rs3758505), -179T/C (rs4646953) and -51C/T (rs4646954). The -1002T and -51C alleles are overrepresented in 357 sporadic Alzheimer disease patients when compared to those in 331 healthy individuals. Furthermore, -1002T/G and -51C/T are in strong linkage disequilibrium and they construct a relatively risky -1002T/-51C and a relatively protective -1002G/-51T
additional information
-
identification of a genetic variant 311 rs6583817, found in two Croatian isolated populations, unequivocally associated with increased IDE expression that is also associated with reduced plasma amyloidbeta40 and decreased late onset Alzheimer's disease susceptibility. rs6583817 increases reporter gene expression in Be(2)-C and Hep-G2 cell lines. Additional eleven IDE haplotypes, that also show significant association, overview
additional information
-
silencing of IDE in Hep-Ge cells by siRNA inhibits insulin degradation by up to 76%
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Ding, L.; Becker, A.B.; Suzuki, A.; Roth, R.A.
Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III
J. Biol. Chem.
267
2414-2420
1992
Homo sapiens
brenda
Affholter, J.A.; Fried, V.A.; Roth, R.A.
Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III
Science
242
1415-1418
1988
Homo sapiens
brenda
Duckworth, W.C.; Hamel, F.G.; Bennett, R.; Ryan, M.P.; Roth, R.A.
Human red blood cell insulin-degrading enzyme and rat skeletal muscle insulin protease share antigenic sites and generate identical products from insulin
J. Biol. Chem.
265
2984-2987
1990
Homo sapiens, Rattus norvegicus
brenda
Becker, A.B.; Roth, R.A.
Insulysin and pitrilysin: insulin-degrading enzymes of mammals and bacteria
Methods Enzymol.
248
693-703
1995
Drosophila melanogaster, Homo sapiens, Mammalia, Rattus norvegicus
brenda
Rawlings, N.D.; Barrett, A.J.
Homologues of insulinase, a new superfamily of metalloendopeptidases
Biochem. J.
275
389-391
1991
Homo sapiens
brenda
Kolb, H.J.; Standl, E.
Purification to homogeneity of an insulin-degrading enzyme from human erythrocytes
Hoppe-Seyler's Z. Physiol. Chem.
361
1029-1039
1980
Homo sapiens
brenda
Ebrahim, A.; Hamel, F.G.; Bennett, R.G.; Duckworth, W.C.
Identification of the metal associated with the insulin degrading enzyme
Biochem. Biophys. Res. Commun.
181
1398-1406
1991
Homo sapiens, Rattus norvegicus
brenda
Perlman, R.K.; Gehm, B.D.; Kuo, W.L.; Rosner, M.R.
Functional analysis of conserved residues in the active site of insulin-degrading enzyme
J. Biol. Chem.
268
21538-21544
1993
Drosophila melanogaster, Homo sapiens, Rattus norvegicus
brenda
Authier, F.; Rachubinski, R.A.; Posner, B.I.; Bergeron, J.M.
Endosomal proteolysis of insulin by an acidic thiol metalloprotease unrelated to insulin degrading enzyme
J. Biol. Chem.
269
3010-3016
1994
Drosophila melanogaster, Homo sapiens, Rattus norvegicus
brenda
Chesneau, V.; Vekrellis, K.; Rosner, M.R.; Selkoe, D.J.
Purified recombinant insulin-degrading enzyme degrades amyloid beta-protein but does not promote its oligomerization
Biochem. J.
351
509-516
2000
Homo sapiens
brenda
Kurochkin, I.V.
Insulin-degrading enzyme: embarking on amyloid destruction
Trends Biochem. Sci.
26
421-425
2001
Drosophila melanogaster, Homo sapiens, Rattus norvegicus
brenda
Morelli, L.; Llovera, R.E.; Alonso, L.G.; Frangione, B.; de Prat-Gay, G.; Ghiso, J.; Castano, E.M.
Insulin-degrading enzyme degrades amyloid peptides associated with British and Danish familial dementia
Biochem. Biophys. Res. Commun.
332
808-816
2005
Homo sapiens, Rattus norvegicus
brenda
Li, P.; Kuo, W.L.; Yousef, M.; Rosner, M.R.; Tang, W.J.
The C-terminal domain of human insulin degrading enzyme is required for dimerization and substrate recognition
Biochem. Biophys. Res. Commun.
343
1032-1037
2006
Homo sapiens
brenda
Leissring, M.A.; Farris, W.; Wu, X.; Christodoulou, D.C.; Haigis, M.C.; Guarente, L.; Selkoe, D.J.
Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria
Biochem. J.
383
439-446
2004
Homo sapiens
brenda
Farris, W.; Leissring, M.A.; Hemming, M.L.; Chang, A.Y.; Selkoe, D.J.
Alternative splicing of human insulin-degrading enzyme yields a novel isoform with a decreased ability to degrade insulin and amyloid beta-protein
Biochemistry
44
6513-6525
2005
Homo sapiens (P14735), Homo sapiens
brenda
Li, Q.; Ali, M.A.; Cohen, J.I.
Insulin degrading enzyme is a cellular receptor mediating Varicella-zoster virus infection and cell-to-cell spread
Cell
127
305-316
2006
Homo sapiens
brenda
Duckworth, W.C.; Fawcett, J.; Reddy, S.; Page, J.C.
Insulin-degrading activity in wound fluid
J. Clin. Endocrinol. Metab.
89
847-851
2004
Homo sapiens
brenda
Lynch, J.A.; George, A.M.; Eisenhauer, P.B.; Conn, K.; Gao, W.; Carreras, I.; Wells, J.M.; McKee, A.; Ullman, M.D.; Fine, R.E.
Insulin degrading enzyme is localized predominantly at the cell surface of polarized and unpolarized human cerebrovascular endothelial cell cultures
J. Neurosci. Res.
83
1262-1270
2006
Homo sapiens
brenda
Shen, Y.; Joachimiak, A.; Rosner, M.R.; Tang, W.J.
Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
Nature
443
870-874
2006
Homo sapiens
brenda
Gao, W.; Eisenhauer, P.B.; Conn, K.; Lynch, J.A.; Wells, J.M.; Ullman, M.D.; McKee, A.; Thatte, H.S.; Fine, R.E.
Insulin degrading enzyme is expressed in the human cerebrovascular endothelium and in cultured human cerebrovascular endothelial cells
Neurosci. Lett.
371
6-11
2004
Homo sapiens
brenda
Fawcett, J.; Permana, P.A.; Levy, J.L.; Duckworth, W.C.
Regulation of protein degradation by insulin-degrading enzyme: analysis by small interfering RNA-mediated gene silencing
Arch. Biochem. Biophys.
468
128-133
2007
Homo sapiens
brenda
Hersh, L.B.
The insulysin (insulin degrading enzyme) enigma
Cell. Mol. Life Sci.
63
2432-2434
2006
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Hwang, D.Y.; Seo, S.; Kim, Y.; Kim, C.; Shim, S.; Jee, S.; Lee, S.; Sin, J.; Cho, J.; Kang, B.; Jang, I.; Cho, J.
Significant change in insulin production, glucose tolerance and ER stress signaling in transgenic mice coexpressing insulin-siRNA and human IDE
Int. J. Mol. Med.
19
65-73
2007
Homo sapiens
brenda
Jee, S.; Hwang, D.; Seo, S.; Kim, Y.; Kim, C.; Kim, B.; Shim, S.; Lee, S.; Sin, J.; Bae, C.; Lee, B.; Jang, M.; Kim, M.; Yim, S.; Jang, I.; Cho, J.; Chae, K.
Microarray analysis of insulin-regulated gene expression in the liver: the use of transgenic mice co-expressing insulin-siRNA and human IDE as an animal model
Int. J. Mol. Med.
20
829-835
2007
Homo sapiens
brenda
Radulescu, R.T.; Hufnagel, C.; Luppa, P.; Hellebrand, H.; Kuo, W.L.; Rosner, M.R.; Harbeck, N.; Giersig, C.; Meindl, A.; Schmitt, M.; Weirich, G.
Immunohistochemical demonstration of the zinc metalloprotease insulin-degrading enzyme in normal and malignant human breast: correlation with tissue insulin levels
Int. J. Oncol.
30
73-80
2007
Homo sapiens
brenda
Im, H.; Manolopoulou, M.; Malito, E.; Shen, Y.; Zhao, J.; Neant-Fery, M.; Sun, C.Y.; Meredith, S.C.; Sisodia, S.S.; Leissring, M.A.; Tang, W.J.
Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE
J. Biol. Chem.
282
25453-25463
2007
Homo sapiens (P14735), Homo sapiens
brenda
Kim, M.; Hersh, L.B.; Leissring, M.A.; Ingelsson, M.; Matsui, T.; Farris, W.; Lu, A.; Hyman, B.T.; Selkoe, D.J.; Bertram, L.; Tanzi, R.E.
Decreased catalytic activity of the insulin-degrading enzyme in chromosome 10-linked Alzheimer disease families
J. Biol. Chem.
282
7825-7832
2007
Homo sapiens
brenda
Bernstein, H.G.; Lendeckel, U.; Bukowska, A.; Ansorge, S.; Ernst, T.; Stauch, R.; Truebner, K.; Steiner, J.; Dobrowolny, H.; Bogerts, B.
Regional and cellular distribution patterns of insulin-degrading enzyme in the adult human brain and pituitary
J. Chem. Neuroanat.
35
216-224
2008
Homo sapiens
brenda
Grasso, G.; Rizzarelli, E.; Spoto, G.
AP/MALDI-MS complete characterization of the proteolytic fragments produced by the interaction of insulin degrading enzyme with bovine insulin
J. Mass Spectrom.
42
1590-1598
2007
Homo sapiens
brenda
Vepsaelaeinen, S.; Parkinson, M.; Helisalmi, S.; Mannermaa, A.; Soininen, H.; Tanzi, R.E.; Bertram, L.; Hiltunen, M.
Insulin-degrading enzyme is genetically associated with Alzheimers disease in the Finnish population
J. Med. Genet.
44
606-608
2007
Homo sapiens
brenda
Li, Q.; Krogmann, T.; Ali, M.A.; Tang, W.J.; Cohen, J.I.
The amino terminus of varicella-zoster virus (VZV) glycoprotein E is required for binding to insulin-degrading enzyme, a VZV receptor
J. Virol.
81
8525-8532
2007
Homo sapiens
brenda
Qiu, W.Q.; Folstein, M.F.
Insulin, insulin-degrading enzyme and amyloid beta-peptide in Alzheimers disease: review and hypothesis
Neurobiol. Aging
27
190-198
2006
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Zhao, Z.; Xiang, Z.; Haroutunian, V.; Buxbaum, J.D.; Stetka, B.; Pasinetti, G.M.
Insulin degrading enzyme activity selectively decreases in the hippocampal formation of cases at high risk to develop Alzheimers disease
Neurobiol. Aging
28
824-830
2007
Homo sapiens
brenda
Marlowe, L.; Peila, R.; Benke, K.S.; Hardy, J.; White, L.R.; Launer, L.J.; Myers, A.
Insulin-degrading enzyme haplotypes affect insulin levels but not dementia risk
Neurodegener. Dis.
3
320-326
2006
Homo sapiens
brenda
Malito, E.; Ralat, L.A.; Manolopoulou, M.; Tsay, J.L.; Wadlington, N.L.; Tang, W.J.
Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme
Biochemistry
47
12822-12834
2008
Homo sapiens
brenda
Weirich, G.; Mengele, K.; Yfanti, C.; Gkazepis, A.; Hellmann, D.; Welk, A.; Giersig, C.; Kuo, W.L.; Rosner, M.R.; Tang, W.J.; Schmitt, M.
Immunohistochemical evidence of ubiquitous distribution of the metalloendoprotease insulin-degrading enzyme (IDE; insulysin) in human non-malignant tissues and tumor cell lines
Biol. Chem.
389
1441-1445
2008
Homo sapiens
brenda
Qin, W.; Jia, J.
Down-regulation of insulin-degrading enzyme by presenilin 1 V97L mutant potentially underlies increased levels of amyloid beta 42
Eur. J. Neurosci.
27
2425-2432
2008
Homo sapiens
brenda
Ciaccio, C.; Tundo, G.R.; Grasso, G.; Spoto, G.; Marasco, D.; Ruvo, M.; Gioia, M.; Rizzarelli, E.; Coletta, M.
Somatostatin: a novel substrate and a modulator of insulin-degrading enzyme activity
J. Mol. Biol.
385
1556-1567
2009
Homo sapiens
brenda
Miners, J.S.; Kehoe, P.G.; Love, S.
Immunocapture-based fluorometric assay for the measurement of insulin-degrading enzyme activity in brain tissue homogenates
J. Neurosci. Methods
169
177-181
2008
Homo sapiens
brenda
Zhao, J.; Li, L.; Leissring, M.A.
Insulin-degrading enzyme is exported via an unconventional protein secretion pathway
Mol. Neurodegener.
4
04
2009
Homo sapiens, Mus musculus
brenda
Dorfman, V.B.; Pasquini, L.; Riudavets, M.; Lopez-Costa, J.J.; Villegas, A.; Troncoso, J.C.; Lopera, F.; Castano, E.M.; Morelli, L.
Differential cerebral deposition of IDE and NEP in sporadic and familial Alzheimer's disease
Neurobiol. Aging
31
1743-1757
2010
Homo sapiens
brenda
Du, J.; Zhang, L.; Liu, S.; Zhang, C.; Huang, X.; Li, J.; Zhao, N.; Wang, Z.
PPARgamma transcriptionally regulates the expression of insulin-degrading enzyme in primary neurons
Biochem. Biophys. Res. Commun.
383
485-490
2009
Homo sapiens, Rattus norvegicus
brenda
Radulescu, R.T.; Duckworth, W.C.; Levy, J.L.; Fawcett, J.
Retinoblastoma protein co-purifies with proteasomal insulin-degrading enzyme: implications for cell proliferation control
Biochem. Biophys. Res. Commun.
395
196-199
2010
Homo sapiens
brenda
Bora, R.P.; Prabhakar, R.
Elucidation of interactions of Alzheimer amyloid beta peptides (Abeta40 and Abeta42) with insulin degrading enzyme: a molecular dynamics study
Biochemistry
49
3947-3956
2010
Homo sapiens (P14735)
brenda
Zuo, X.; Jia, J.
Promoter polymorphisms which modulate insulin degrading enzyme expression may increase susceptibility to Alzheimer's disease
Brain Res.
1249
1-8
2009
Homo sapiens
brenda
Wang, R.; Wang, S.; Malter, J.S.; Wang, D.S.
Effects of 4-hydroxy-nonenal and Amyloid-beta on expression and activity of endothelin converting enzyme and insulin degrading enzyme in SH-SY5Y cells
J. Alzheimers Dis.
17
489-501
2009
Homo sapiens
brenda
Amata, O.; Marino, T.; Russo, N.; Toscano, M.
Human insulin-degrading enzyme working mechanism
J. Am. Chem. Soc.
131
14804-14811
2009
Homo sapiens
brenda
Manolopoulou, M.; Guo, Q.; Malito, E.; Schilling, A.B.; Tang, W.J.
Molecular basis of catalytic chamber-assisted unfolding and cleavage of human insulin by human insulin-degrading enzyme
J. Biol. Chem.
284
14177-14188
2009
Homo sapiens
brenda
Ralat, L.A.; Ren, M.; Schilling, A.B.; Tang, W.J.
Protective role of Cys-178 against the inactivation and oligomerization of human insulin-degrading enzyme by oxidation and nitrosylation
J. Biol. Chem.
284
34005-34018
2009
Homo sapiens
brenda
Guo, Q.; Manolopoulou, M.; Bian, Y.; Schilling, A.B.; Tang, W.J.
Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme
J. Mol. Biol.
395
430-443
2010
Homo sapiens
brenda
Bernstein, H.G.; Ernst, T.; Lendeckel, U.; Bukowska, A.; Ansorge, S.; Stauch, R.; Have, S.T.; Steiner, J.; Dobrowolny, H.; Bogerts, B.
Reduced neuronal expression of insulin-degrading enzyme in the dorsolateral prefrontal cortex of patients with haloperidol-treated, chronic schizophrenia
J. Psychiatr. Res.
43
1095-1105
2009
Homo sapiens, Rattus norvegicus
brenda
Lu, X.; Huang, Y.; Liu, Y.; Wu, X.; Shi, X.
Variants in the insulin-degrading enzyme gene are associated with metabolic syndrome in Chinese elders
Metab. Clin. Exp.
58
1465-1469
2009
Homo sapiens
brenda
Cabrol, C.; Huzarska, M.A.; Dinolfo, C.; Rodriguez, M.C.; Reinstatler, L.; Ni, J.; Yeh, L.A.; Cuny, G.D.; Stein, R.L.; Selkoe, D.J.; Leissring, M.A.
Small-molecule activators of insulin-degrading enzyme discovered through high-throughput compound screening
PLoS ONE
4
e5274
2009
Homo sapiens
brenda
Carrasquillo, M.M.; Belbin, O.; Zou, F.; Allen, M.; Ertekin-Taner, N.; Ansari, M.; Wilcox, S.L.; Kashino, M.R.; Ma, L.; Younkin, L.H.; Younkin, S.G.; Younkin, C.S.; Dincman, T.A.; Howard, M.E.; Howell, C.C.; Stanton, C.M.; Watson, C.M.; Crump, M.; Vitart, V.; Hayward, C.; Hastie, N.D.; Rudan, I.; Campbell, H.; , P.
Concordant association of insulin degrading enzyme gene (IDE) variants with IDE mRNA, Abeta, and Alzheimers disease
PLoS ONE
5
e8764
2010
Homo sapiens
brenda
Zhang, W.J.; Luo, X.; Guo, Z.Y.
In vitro degradation of insulin-like peptide 3 by insulin-degrading enzyme
Protein J.
29
93-98
2010
Homo sapiens
brenda
Hulse, R.E.; Ralat, L.A.; Wei-Jen, T.
Structure, function, and regulation of insulin-degrading enzyme
Vitam. Horm.
80
635-648
2009
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Song, E.; Rodgers, D.; Hersh, L.
Mixed dimers of insulin-degrading enzyme reveal a cis activation mechanism
J. Biol. Chem.
286
13853-13858
2011
Homo sapiens
brenda
Ralat, L.A.; Guo, Q.; Ren, M.; Funke, T.; Dickey, D.M.; Potter, L.R.; Tang, W.J.
Insulin-degrading enzyme modulates the natriuretic peptide-mediated signaling response
J. Biol. Chem.
286
4670-4679
2011
Homo sapiens
brenda
Bora, R.; Ozbil, M.; Prabhakar, R.
Elucidation of insulin degrading enzyme catalyzed site specific hydrolytic cleavage of amyloid beta peptide: A comparative density functional theory study
J. Biol. Inorg. Chem.
15
485-495
2010
Homo sapiens
brenda
Ralat, L.A.; Kalas, V.; Zheng, Z.; Goldman, R.D.; Sosnick, T.R.; Tang, W.J.
Ubiquitin is a novel substrate for human insulin-degrading enzyme
J. Mol. Biol.
406
454-466
2011
Homo sapiens
brenda
Kummer, M.P.; Huelsmann, C.; Hermes, M.; Axt, D.; Heneka, M.T.
Nitric Oxide Decreases the Enzymatic Activity of Insulin Degrading Enzyme in APP/PS1 Mice
J. Neuroimmune Pharmacol.
7
165-172
2012
Homo sapiens, Mus musculus
brenda
Grasso, G.; Satriano, C.; Milardi, D.
A neglected modulator of insulin-degrading enzyme activity and conformation: The pH
Biophys. Chem.
203-204
33-40
2015
Homo sapiens (P14735)
brenda
Charton, J.; Gauriot, M.; Totobenazara, J.; Hennuyer, N.; Dumont, J.; Bosc, D.; Marechal, X.; Elbakali, J.; Herledan, A.; Wen, X.; Ronco, C.; Gras-Masse, H.; Heninot, A.; Pottiez, V.; Landry, V.; Staels, B.; Liang, W.; Leroux, F.; Tang, W.; Deprez, B.; De
Structure-activity relationships of imidazole-derived 2-[N -carbamoylmethyl-alkylamino]acetic acids, dual binders of human insulin-degrading enzyme
Eur. J. Med. Chem.
90
547-567
2014
Homo sapiens (P14735), Homo sapiens
brenda
Tundo, G.; Sbardella, D.; Ciaccio, C.; Bianculli, A.; Orlandi, A.; Desimio, M.; Arcuri, G.; Coletta, M.; Marini, S.
Insulin-degrading enzyme (IDE): A novel heat shock-like protein
J. Biol. Chem.
288
2281-2289
2013
Homo sapiens (P14735), Homo sapiens
brenda
Abdul-Hay, S.O.; Sahara, T.; McBride, M.; Kang, D.; Leissring, M.A.
Identification of BACE2 as an avid beta-amyloid-degrading protease
Mol. Neurodegener.
7
46
2012
Homo sapiens (Q9Y5Z0)
brenda
McCord, L.; Liang, W.; Dowdell, E.; Kalas, V.; Hoey, R.; Koide, A.; Koide, S.; Tang, W.
Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme
Proc. Natl. Acad. Sci. USA
110
13827-13832
2013
Homo sapiens (P14735), Homo sapiens
brenda
Krasinski, C.A.; Ivancic, V.A.; Zheng, Q.; Spratt, D.E.; Lazo, N.D.
Resveratrol sustains insulin-degrading enzyme activity toward Abeta42
ACS Omega
3
13275-13282
2018
Homo sapiens (P14735)
brenda
Sharma, S.K.; Chorell, E.; Wittung-Stafshede, P.
Insulin-degrading enzyme is activated by the C-terminus of alpha-synuclein
Biochem. Biophys. Res. Commun.
466
192-195
2015
Homo sapiens (P14735)
brenda
Kurochkin, I.V.; Guarnera, E.; Wong, J.H.; Eisenhaber, F.; Berezovsky, I.N.
Toward allosterically increased catalytic activity of insulin-degrading enzyme against amyloid peptides
Biochemistry
56
228-239
2017
Homo sapiens (P14735), Homo sapiens
brenda
Stefanidis, L.; Fusco, N.D.; Cooper, S.E.; Smith-Carpenter, J.E.; Alper, B.J.
Molecular determinants of substrate specificity in human insulin-degrading enzyme
Biochemistry
57
4903-4914
2018
Homo sapiens (P14735), Homo sapiens
brenda
Hubin, E.; Cioffi, F.; Rozenski, J.; van Nuland, N.A.; Broersen, K.
Characterization of insulin-degrading enzyme-mediated cleavage of Abeta in distinct aggregation states
Biochim. Biophys. Acta
1860
1281-1290
2016
Homo sapiens (P14735), Homo sapiens
brenda
Ivancic, V.A.; Krasinski, C.A.; Zheng, Q.; Meservier, R.J.; Spratt, D.E.; Lazo, N.D.
Enzyme kinetics from circular dichroism of insulin reveals mechanistic insights into the regulation of insulin-degrading enzyme
Biosci. Rep.
38
BSR20181416
2018
Homo sapiens (P14735)
brenda
Grasso, G.; Lanza, V.; Malgieri, G.; Fattorusso, R.; Pietropaolo, A.; Rizzarelli, E.; Milardi, D.
The insulin degrading enzyme activates ubiquitin and promotes the formation of K48 and K63 diubiquitin
Chem. Commun. (Camb.)
51
15724-15727
2015
Homo sapiens (P14735)
brenda
Zhang, H.; Liu, D.; Huang, H.; Zhao, Y.; Zhou, H.
Characteristics of insulin-degrading enzyme in Alzheimers Disease a meta-analysis
Curr. Alzheimer Res.
15
610-617
2018
Homo sapiens (P14735), Homo sapiens
brenda
Tundo, G.R.; Di Muzio, E.; Ciaccio, C.; Sbardella, D.; Di Pierro, D.; Polticelli, F.; Coletta, M.; Marini, S.
Multiple allosteric sites are involved in the modulation of insulin-degrading-enzyme activity by somatostatin
FEBS J.
283
3755-3770
2016
Homo sapiens (P14735)
brenda
Durham, T.B.; Toth, J.L.; Klimkowski, V.J.; Cao, J.X.; Siesky, A.M.; Alexander-Chacko, J.; Wu, G.Y.; Dixon, J.T.; McGee, J.E.; Wang, Y.; Guo, S.Y.; Cavitt, R.N.; Schindler, J.; Thibodeaux, S.J.; Calvert, N.A.; Coghlan, M.J.; Sindelar, D.K.; Christe, M.; Kiselyov, V.V.; Michael, M.D.; Sloop, K.W.
Dual exosite-binding inhibitors of insulin-degrading enzyme challenge its role as the primary mediator of insulin clearance in vivo
J. Biol. Chem.
290
20044-20059
2015
Homo sapiens (P14735), Mus musculus (Q9JHR7)
brenda
Maianti, J.P.; Tan, G.A.; Vetere, A.; Welsh, A.J.; Wagner, B.K.; Seeliger, M.A.; Liu, D.R.
Substrate-selective inhibitors that reprogram the activity of insulin-degrading enzyme
Nat. Chem. Biol.
15
565-574
2019
Homo sapiens (P14735)
brenda
Smith-Carpenter, J.E.; Alper, B.J.
Functional requirement for human pitrilysin metallopeptidase 1 arginine 183, mutated in amyloidogenic neuropathy
Protein Sci.
27
861-873
2018
Homo sapiens (Q5JRX3), Homo sapiens
brenda