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Information on EC 3.4.22.1 - cathepsin B and Organism(s) Rattus norvegicus and UniProt Accession P00787
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3.4.22.1 cathepsin BSpecify your search results
Word Map
- 3.4.22.1
- cathepsins
- lysosomal
- proteinases
- papain
- collagen
- metastasis
- pancreatic
- cystatins
-
procathepsin
- upa
-
exopeptidase
- food industry
- myofibrillar
- mansoni
- schistosoma
-
lc3-ii
- calpains
-
permeabilization
- zymogen
-
intralysosomal
- leupeptin
- peptidase
-
hyperamylasemia
- pharmacology
-
papain-like
- diagnostics
- biotechnology
- collagenase
-
antibody-drug
-
autophagy-lysosome
- pepstatin
-
acinar
- ficin
- plasminogen
- caspase-1
- proenzyme
- legumain
-
autophagosomes
- elastase
- caerulein
-
caerulein-induced
- molecular biology
-
dipeptidyl
-
fluorogenic
- inflammasome
- endosomes
-
pro-il-1
-
supramaximal
-
l-like
-
b-mediated
- fasciola
- mu-calpain
- medicine
- trypsinogen
- hepatica
- drug development
-
collagenolytic
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides
Synonyms
cathepsin b, cathepsin-b, cysteine cathepsin, devdase, cat b, cathepsin b1, cathb, smcb1, cath b, cath-b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
APP secretase
-
-
-
-
cathepsin B1
-
-
-
-
cathepsin II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9047-22-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-Arg-Arg-7-amido-4-trifluoromethylcoumarin + H2O
Ac-Arg-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
?
-
a synthetic substrate of caspase-3 and caspase-7
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
cleavage occurs at pH 4.0, but not at pH 7.5
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
20 mM DTT, pH 5.5
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
37°C, pH 6.0, 8 mM DTT, 352 mM KH2PO4, 48 mM Na2HPO4, 4 mM disodium EDTA
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
Proteins + H2O
?
-
-
-
-
?
additional information
?
-
-
enzyme is involved in myoblast-myoblast fusion
-
?
additional information
?
-
-
cathepsin B is expressed in induced cerebral aneurysms and promotes the progression of cerebral aneurysms, which include degradation of extracellular matrix in arterial walls in strong subarachnoid hemorrhage, overview
-
-
?
additional information
?
-
-
cathepsin B secreted by activated microglia is closely associated with the MeHg-induced severe pyknotic changes of the cerebellar granule cells, overview. Cathepsin B is involved in apoptotic processes
-
-
?
additional information
?
-
-
effective inhibition of cathepsin B can decrease the severity of joint inflammation and to reduce the destruction of particular tissues in the rat model of antigen adjuvant-induced arthritis
-
-
?
additional information
?
-
-
under certain conditions, e.g. in hypoxia, cathepsin B participates in cleavage of caspase-3 substrates in brain cells
-
-
?
additional information
?
-
-
cathepsin B is a lysosomal cysteine protease, a unique cysteine member showing dual roles as both endopeptidase and exopeptidase activities due to the presence of the occluding loop in structure
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Proteins + H2O
?
-
-
-
-
?
additional information
?
-
-
enzyme is involved in myoblast-myoblast fusion
-
?
additional information
?
-
-
cathepsin B is expressed in induced cerebral aneurysms and promotes the progression of cerebral aneurysms, which include degradation of extracellular matrix in arterial walls in strong subarachnoid hemorrhage, overview
-
-
?
additional information
?
-
-
cathepsin B secreted by activated microglia is closely associated with the MeHg-induced severe pyknotic changes of the cerebellar granule cells, overview. Cathepsin B is involved in apoptotic processes
-
-
?
additional information
?
-
-
effective inhibition of cathepsin B can decrease the severity of joint inflammation and to reduce the destruction of particular tissues in the rat model of antigen adjuvant-induced arthritis
-
-
?
additional information
?
-
-
under certain conditions, e.g. in hypoxia, cathepsin B participates in cleavage of caspase-3 substrates in brain cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomethylmercuric cation
-
treatment leads to increased cathepsin B mainly in activated microglia which accumulate in the granule cell layer of the cerebellum
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CBZ-Phe-Ser(OBzl)-CHN2
cysteine protease inhibitor 1 (CP-1), effective inhibition at 0.05 mM
E-64c
inhibition of Cathepsin B alone not only reduces hyperthermic injury-induced apoptosis significantly but enhances the beneficial effects of preinduction of HSP-70 in reducing hyperthermic injury-induced apoptosis in H9C2 cells significantly
leupeptin
leupeptin lacks selectivity since it inhibits both serine and cysteine proteases
N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-L-proline
CA-074
2,12-diethyl-11-methylhexadecyl 2-ethyl-11-methylhexadecyl phthalate
-
isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
2-ethyldecyl 2-ethylundecyl phthalate
-
isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
acetyl-Asp-Glu-Val-Asp-CHO
-
complete DEVDase activity inhibition in brain cell supernatant
acetyl-YVAD-chloromethyl ketone
-
caspase inhibitor, inhibition of enzyme contributes to neuroprotective properties of the inhibitor
bis(2-ethyldodecyl) phthalate
-
isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
bis(2-ethylheptyl) phthalate
-
isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
CA-074-Me
-
suppresses microglia conditioned culture medium-induced glioma cell death
CA074Me
-
inhibition affects myotube size and number, fusion-related creatine phosphokinase activity and myosin heavy chain protein, inhibition occurs at each stage of differentiation
cystatin C
-
an endogenous inhibitor of cysteine cathepsins, expression patterns of cathepsin B and cystatin C
-
Gly-Pro-Phe-Pro-Ile
-
amino acids 203-207 of bovine beta-casein, competitive
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
N-ethylmaleimide
-
concentrations above10 mM significantly decrease activity
NC-2300
-
i.e. monosodium (2S,3S)-3-[[(1S)-1-isobutoxymethyl-3-methylbutyl]carbamoyl]oxirane-2-carboxylate, a cysteine cathepsin inhibitor
oxidized glutathione
-
concentrations above10 mM significantly decrease activity
Pro-Phe-Pr-Gly-Pro-Ile
-
amino acids 61-66 of bovine beta-casein, competitive
additional information
inhibitory potency of a series benzyloxycarbonyl-Phe-X-diazomethylketone, in which Phe promotes binding at S2 while the amino acid X probes S1. The S1 region of cathepsin L also has the ability to accommodate large hydrophobic side chains. In this respect cathepsin L differs from cathepsin B. Thus benzyloxycarbonyl-Phe-Tyr(O-l-butyl)-diazomethylketone, inactivates cathepsin L with higher efficiency compared to cathepsin B
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
reduced glutathione
-
the presence of reduced glutathione at concentrations of more than 10 mM significantly increases activity at pH 4.0
dithiothreitol
-
the presence of dithiothreitol at concentrations of more than 10 mM significantly increases activity at pH 4.0
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
2,12-diethyl-11-methylhexadecyl 2-ethyl-11-methylhexadecyl phthalate
Rattus norvegicus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 6.5
-
activity range with substrate acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin, about 90% of maximal activity at pH 3.5, maximal activity at pH 4.0, and about 5-10% of maximal activity at pH 6.5, iactive at pH 7.0
5 - 7
-
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide as substrate, filaggrin is hydrolyzed at pH 4.0, but not at pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
type 1 alveolar epithelial (R3/1) cell
additional information
-
immunohistochemic expression analysis in cerebral arterial walls and aneurysms, overview
-
cathepsin B is expressed in induced cerebral aneurysms and aneurysmal walls, and promotes the progression of cerebral aneurysms
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
cathepsin B activity is detected in exosomes isolated from hydrogen peroxide treated cells
-
-
in oxidative stress cathepsin B may be released from lysosomes into cytoplasm with lowered pH and cleave cytoplasmic proteins, including caspase-3 substrates
additional information
enzymatic activity increases significantly in the injury epicenter at 5 and 7 days post-injury
-
-
the enzyme is released by activated microglia accumulating in the granule cell layer of the lingual and central lobe
-
-
in oxidative stress cathepsin B may be released from lysosomes into cytoplasm with lowered pH and cleave cytoplasmic proteins, including caspase-3 substrates
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
physiological function
-
Atg7-induced CTSB overexpression contributes to an NLRP3-dependent proinflammatory response and subsequently impairs glucose-stimulated insulin secretion independently of apoptosis
additional information
the substrate peptide bond cleaved by cathepsin B (EC 3.4.22.1) and cathepsin L (EC 3.4.22.15) is determined not by the amino acid contributing the carboxyl group to this bond as in the case of serine proteases but rather by the presence of a neighboring amino acid with a large hydrophobic side chain, active center differences between cathepsins L and B in the S1 binding region, overview
physiological function
cathepsin B is involved in hyperthermic injury-induced cardiomyocyte apoptosis in H9C2 cells and HSP-70 protects these cells from hyperthermic injury-induced cardiomyocyte apoptosis through cathepsin B pathways
physiological function
exosomal cathepsin B regulates the receptor for advanced glycation end-products (RAGE) in type 1 alveolar cells under conditions of oxidative stress
malfunction
-
Microglia induce apoptosis of glioma cells via the release of NO and cathepsin B protease. Cathepsin B causes a decrease in cell survival. Cathepsin B plays a critical role in cytotoxicity in the central nervous system
malfunction
-
blocking CTSB expression using CTSB siRNA suppresses inflammatory response but does not affect apoptosis markedly
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CATB_RAT
339
0
37470
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E245Q
-
reduced Kcat for benzyloxycarbonyl-Phe-Arg-p-nitroanilide and benzyloxycarbonyl-Arg-Arg-p-nitroanilide
R202A
-
no significant effect on kinetic contstants with benzyloxycarbonyl-Phe-Arg-p-nitroanilide or benzyloxycarbonyl-Arg-Arg-p-nitroanilide
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from brain cell supernatant by ammonium sulfate fractionation and gel filtration
-
S-Sepharose Fast Flow column chromatography and Sephadex G-25 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression analysis by quantitative RT-PCR, expression patterns of cathepsin B and endogenous inhibitor cystatin C
-
intestine-specific expression of GFP-tagged mature cathepsin B driven by the A33-antigen promoter, that contains positive cis-regulatory elements, including caudal-related homeobox binding sites, in CHO-K1 cells, evaluation of the expression system, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
enzyme is involved in neuronal cell death, particularly following ischemia
medicine
-
cathepsin B inhibitors are expected to be useful for the treatment of inflammatory joint disease, invasion of cancer, and other diseases related to cathepsin B disorder
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Towatari, T.; Kawabata, Y.; Katunuma, N.
Crystallization and properties of cathepsin B from rat liver
Eur. J. Biochem.
102
279-289
1979
Rattus norvegicus
Lenney, J.F.; Tolan, J.R.; Sugai, W.J.; Lee, A.G.
Thermostable endogenous inhibitors of cathepsins B and H
Eur. J. Biochem.
101
153-161
1979
Rattus norvegicus
Szego, C.M.; Seeler, B.J.; Smith, R.E.
Lysosomal cathepsin B1: Partial characterization in rat preputial gland and recompartmentation in response to estradiol-17beta
Eur. J. Biochem.
69
463-474
1976
Rattus norvegicus
-
Kawada, A.; Hara, K.; Morimoto, K.; Hiruma, M.; Ishibashi, A.
Rat epidermal cathepsin B: purification and characterization of proteolytic properties toward filaggrin and synthetic substrates
Int. J. Biochem. Cell Biol.
27
175-183
1995
Rattus norvegicus
San Segundo, B.; Chan, S.J.; Steiner, D.F.
Identification of cDNA clones encoding a precursor of rat liver cathepsin B
Proc. Natl. Acad. Sci. USA
82
2320-2324
1985
Rattus norvegicus
Jia, Z.; Hasnain, S.; Hirama, T.; Lee, X.; Mort, J.S.; To, R.
Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design [published erratum appears in J Biol Chem 1995 Nov 24;270(47):28494
J. Biol. Chem.
270
5527-5533
1995
Rattus norvegicus
Lee, X.; Ahmed, F.R.; Hirama, T.; Huber, C.P.; Rose, D.R.; To, R.; Hasnain, S.
Crystallization of recombinant rat cathepsin B
J. Biol. Chem.
265
5950-5951
1990
Rattus norvegicus
Hasnain, S.; Hirama, T.; Huber, C.P.; Mason, P.; Mort, J.S.
Characterization of cathepsin B specificity by site-directed mutagenesis. Importance of Glu245 in the S2-P2 specificity for arginine and its role in transition state stabilization
J. Biol. Chem.
268
235-240
1993
Rattus norvegicus
Taniguchi, T.; Mizuochi, T.; Towatari, T.; Katunuma, N.; Kobata, A.
Structural studies on the carbohydrate moieties of rat liver cathepsins B and H
J. Biochem.
97
973-976
1985
Rattus norvegicus
Jane, D.T.; Morvay, L.C.; Allen, F.; Sloane, B.F.; Dufresne, M.J.
Selective inhibition of cathepsin B with cell-permeable CA074me negatively affects L6 rat myoblast differentiation
Biochem. Cell Biol.
80
457-465
2002
Rattus norvegicus
Gray, J.; Haran, M.M.; Schneider, K.; Vesce, S.; Ray, A.M.; Owen, D.; White, I.R.; Cutler, P.; Davis, J.B.
Evidence that inhibition of cathepsin-B contributes to the neuroprotective properties of caspase inhibitor Tyr-Val-Ala-Asp-chloromethyl ketone
J. Biol. Chem.
276
32750-32755
2001
Mus musculus, Rattus norvegicus
Lee, H.S.; Lee, K.J.
Cathepsin B inhibitory peptides derived from beta-casein
Peptides
21
807-809
2000
Rattus norvegicus
Jane, D.T.; Morvay, L.; Dasilva, L.; Cavallo-Medved, D.; Sloane, B.F.; Dufresne, M.J.
Cathepsin B localizes to plasma membrane caveolae of differentiating myoblasts and is secreted in an active form at physiological pH
Biol. Chem.
387
223-234
2006
Rattus norvegicus (P00787)
Ellis, R.C.; O'Steen, W.A.; Hayes, R.L.; Nick, H.S.; Wang, K.K.; Anderson, D.K.
Cellular localization and enzymatic activity of cathepsin B after spinal cord injury in the rat
Exp. Neurol.
193
19-28
2005
Rattus norvegicus (P00787)
Anagli, J.; Abounit, K.; Stemmer, P.; Han, Y.; Allred, L.; Weinsheimer, S.; Movsisyan, A.; Seyfried, D.
Effects of cathepsins B and L inhibition on postischemic protein alterations in the brain
Biochem. Biophys. Res. Commun.
366
86-91
2008
Rattus norvegicus (P00787)
Yakovlev, A.A.; Gorokhovatsky, A.Y.; Onufriev, M.V.; Beletsky, I.P.; Gulyaeva, N.V.
Brain cathepsin B cleaves a caspase substrate
Biochemistry (Moscow)
73
332-336
2008
Rattus norvegicus
Wang, Y.; Gu, Z.L.; Cao, Y.; Liang, Z.Q.; Han, R.; Bennett, M.C.; Qin, Z.H.
Lysosomal enzyme cathepsin B is involved in kainic acid-induced excitotoxicity in rat striatum
Brain Res.
1071
245-249
2006
Rattus norvegicus
Mayer, K.; Iolyeva, M.E.; Meyer-Grahle, U.; Brix, K.
Intestine-specific expression of green fluorescent protein-tagged cathepsin B: proof-of-principle experiments
Biol. Chem.
389
1085-1096
2008
Rattus norvegicus
Li, Y.; Qian, Z.J.; Kim, S.K.
Cathepsin B inhibitory activities of three new phthalate derivatives isolated from seahorse, Hippocampus Kuda Bleeker
Bioorg. Med. Chem. Lett.
18
6130-6134
2008
Rattus norvegicus
Sakamoto, M.; Miyamoto, K.; Wu, Z.; Nakanishi, H.
Possible involvement of cathepsin B released by microglia in methylmercury-induced cerebellar pathological changes in the adult rat
Neurosci. Lett.
442
292-296
2008
Rattus norvegicus
Aoki, T.; Kataoka, H.; Ishibashi, R.; Nozaki, K.; Hashimoto, N.
Cathepsin B, K, and S are expressed in cerebral aneurysms and promote the progression of cerebral aneurysms
Stroke
39
2603-2610
2008
Homo sapiens, Rattus norvegicus
Hwang, S.Y.; Yoo, B.C.; Jung, J.W.; Oh, E.S.; Hwang, J.S.; Shin, J.A.; Kim, S.Y.; Cha, S.H.; Han, I.O.
Induction of glioma apoptosis by microglia-secreted molecules: The role of nitric oxide and cathepsin B
Biochim. Biophys. Acta
1793
1656-1668
2009
Homo sapiens, Rattus norvegicus
Hsu, S.F.; Hsu, C.C.; Cheng, B.C.; Lin, C.H.
Cathepsin B is involved in the heat shock induced cardiomyocytes apoptosis as well as the anti-apoptosis effect of HSP-70
Apoptosis
19
1571-1580
2014
Rattus norvegicus (P00787)
Li, S.; Du, L.; Zhang, L.; Hu, Y.; Xia, W.; Wu, J.; Zhu, J.; Chen, L.; Zhu, F.; Li, C.; Yang, S.
Cathepsin B contributes to autophagy-related 7 (Atg7)-induced nod-like receptor 3 (NLRP3)-dependent proinflammatory response and aggravates lipotoxicity in rat insulinoma cell line
J. Biol. Chem.
288
30094-30104
2013
Rattus norvegicus
Kirschke, H.; Wikstrom, P.; Shaw, E.
Active center differences between cathepsins L and B the S, binding region
FEBS Lett.
228
128-130
1988
Rattus norvegicus (P00787)
-
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