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Information on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase and Organism(s) Mus musculus and UniProt Accession Q9EPA7
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2.7.7.1 nicotinamide-nucleotide adenylyltransferaseIUBMB Comments
Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase.
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Word Map
- 2.7.7.1
- degeneration
-
wallerian
- neurodegenerative
-
neuroprotective
- amaurosis
-
leber
- nampt
-
self-destruct
-
axotomy
- riboside
- nadase
- tiazofurin
-
axonopathies
-
pro-degenerative
- analysis
- drug development
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
nmnat2, nmnat, nmnat1, nmnat3, nicotinamide mononucleotide adenylyltransferase, nmn adenylyltransferase, nicotinamide mononucleotide adenylyltransferase 1, nicotinamide mononucleotide adenylyltransferase 2, namnat, hnmnat-2, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nicotinamide mononucleotide adenylyltransferase
NMNAT1
adenosine triphosphate-nicotinamide mononucleotide transadenylase
-
-
-
-
adenylyltransferase, nicotinamide mononucleotide
-
-
-
-
ATP:NMN adenylyltransferase
-
-
-
-
diphosphopyridine nucleotide pyrophosphorylase
-
-
-
-
NAD+ pyrophosphorylase
-
-
-
-
nicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
NMN adenylyltransferase
-
-
-
-
NMNAT
NMNAT2
NMNAT3
PNAT
-
-
-
-
pyridine nucleotide adenylyltransferase
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide mononucleotide adenylyltransferase
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
NMNAT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:nicotinamide-nucleotide adenylyltransferase
Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase.
CAS REGISTRY NUMBER
COMMENTARY
9032-70-6
-
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
ATP + nicotinic acid mononucleotide
diphosphate + deamido-NAD+
-
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
?
ATP + nicotinic acid mononucleotide
diphosphate + deamido-NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
?
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
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
isoform NMNAT1 is predominantly activated by Zn2+ ions (0.05 mM)
Co2+
isoform NMNAT3 is predominantly activated by Co2+ ions (5 mM)
Mg2+
isoform NMNAT2 is predominantly activated by Mg2+ ions (0.5 mM)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0335
ATP
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.0252
nicotinamide ribonucleotide
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.039
ATP
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.082
ATP
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.08425
ATP
-
wild type enzyme, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.113
ATP
-
mutant enzyme C164S/C165S, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.00295
nicotinamide ribonucleotide
-
mutant enzyme C164S/C165S, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.00691
nicotinamide ribonucleotide
-
wild type enzyme, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.0385
nicotinamide ribonucleotide
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.1176
nicotinamide ribonucleotide
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
ATP
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
15.5
nicotinamide ribonucleotide
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.74
ATP
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
2.33
ATP
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.654
nicotinamide ribonucleotide
-
wild type enzyme, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.75
nicotinamide ribonucleotide
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
2.87
nicotinamide ribonucleotide
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
7.21
nicotinamide ribonucleotide
-
mutant enzyme C164S/C165S, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
450
ATP
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
610
nicotinamide ribonucleotide
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
20
ATP
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
30
ATP
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
10
nicotinamide ribonucleotide
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
70
nicotinamide ribonucleotide
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
isoform Nmat2 is not detected in heart, spleen, lung, kidney, liver and skeletal muscle
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform Nmnat2 is enriched in numerous membrane compartments including synaptic terminals
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
nicotinamide mononucleotide adenylyltransferase 2 (Nmat2) homozygous deletion mutants show an approximate 60% reduction of spinal motoneurons in the lumbar region and a more than 80% reduction in the sensory neurons of the dorsal root ganglion. In the absence of Nmnat2, major target organs and tissues (e.g., muscle) are not functionally innervated resulting in perinatal lethality
physiological function
malfunction
gain-of-function mutations in the mouse nicotinamide mononucleotide adenylyltransferase type 1, Nmnat1, produce two remarkable phenotypes: protection against traumatic axonal degeneration and reduced hypoxic brain injury, the mechanism involves the mitochondrial unfolded protein response (mitoUPR) factor, penotype, overview
malfunction
NMNAT1 overexpression reduces cell death and apoptosis both in vitro and in vivo. NMNAT1 knockdown exacerbates cell death and apoptosis. NMNAT1 overexpression regulates neuron survival via AMPK activation, as NMNAT1 overexpression enhances AMPKactivity in OGD-treated cortical neurons, and AMPK inhibitor blocks LV-NMNAT1-induced neuroprotection in OGD-treated cortical neurons
physiological function
NMNAT1 is an enzyme in the NAD biosynthetic pathway that generates NAD in the nucleus
physiological function
isozyme nicotinamide mononucleotide adenylyltransferase 1 protects neural cells against ischemic injury in primary cultured neuronal cells and mouse brain with ischemic stroke through AMP-activated protein kinase activation. NMNAT1 overexpression reduces brain infarction size and improves behavioral outcomes in mice with ischemic stroke. Role and mechanism of NMNAT1 in the regulation of neural ischemic injuries by using cultured cortical neurons with oxygen-glucose deprivation of ischemic injury in vitro and mouse transient middle cerebral artery occlusion (MCAO) model of stroke in vivo, overview
physiological function
crossing of htau mice, which express non-mutant human tau isoforms and represent a model of tauopathy relevant to Alzheimer's disease, with Nmnat1 transgenic and knockout mice. In the resulting offspring until the age of 6 months, overexpression of NMNAT1 ameliorates the early deficit in food burrowing characteristic of htau mice. At 6 months of age, htau mice do not show neurodegenerative changes in both the cortex and hippocampus, and these are not induced by downregulating NMNAT1 levels. Modulating NMNAT1 levels produces a corresponding effect on NMNAT enzymatic activity but does not alter NAD levels in htau mice
physiological function
-
nicotinamide mononucleotide adenylyltransferase 2 regulates axon integrity in the mouse embryo
physiological function
-
overexpression of isoform Nmnat2 is toxic to primary neurons resulting in pervasive cell death
physiological function
Golgi fragmentation in cultured dorsal root ganglion neurons results in caspase dependent axon degeneration and neuronal cell death. NMNAT2 depletion in these neurons causes Golgi fragmentation and caspase dependent axon degeneration. NMNAT2 depletion does not cause ATP loss in the axons. Cytosolic Nmnat1 overexpression inhibits the axon degeneration induced by Golgi fragmentation or NMNAT2 depletion
physiological function
NMNAT shows strong interaction with phosphorylated truncated Tau protein. The binding affinity of NMNAT3 to phosphorylated Tau is about one order of magnitude higher than that to Tau.The phosphorylated Ser residues of Tau are the primary binding sites. Substrates (i.e. NMN and ATP) and the chaperone client phosphorylated Tau share the same binding pocket with a partial overlap at the phosphate-binding site
physiological function
NMNAT3 is a target and binding partner of sirtuin SIRT3. SIRT3 physically interacts with and deacetylates NMNAT3, thereby enhancing the enzyme activity of NMNAT3 and contributing to SIRT3-mediated anti-hypertrophic effects. NMNAT3 regulates the activity of SIRT3 via synthesis of mitochondrial NAD+
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). NMNA1_MOUSE
285
0
32355
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
SIRT3 increases NMNAT3 activity by interacting with and deacetylating NMNAT3
palmitoylation
-
isoform Nmnat2 is palmitoylated in vitro (at Cys164 and Cys165) and this modification is required for membrane association
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
WldS(W258A)
the chimeric WldS protein is composed of the N-terminal 70 aa of Ufd2a/Ube4b, an ubiquitin-chain assembly factor, fused to the complete sequence of NMNAT1, the W258A mutation disrupts the NAD-synthesizing activity
C164S/C165S
-
the mutant protein is not palmitoylated (soluble), appears diffuse in the cytoplasm and does not colocalize with GM130. However, the mutant is fully active and shows even higher kcat values compared to the wild type enzyme
E198P/L217R
mutation disrupts the dimer interface, leading to a mixture of dimer and monomer in solution
additional information
additional information
naturally occuring mutant mice, wldS, showing delayed Wallerian degeneration phenotype, suggest that axonal degeneration is an active process, the wldS mutation comprises an 85 kb tandem triplicon, which causes overexpression of the chimeric WldS protein composed of the N-terminal 70 aa of Ufd2a/Ube4b, an ubiquitin-chain assembly factor, fused to the complete sequence of NMNAT1
additional information
naturally occuring mutant mice, wldS, showing delayed Wallerian degeneration phenotype, suggest that axonal degeneration is an active process, the wldS mutation comprises an 85 kb tandem triplicon, which causes overexpression of the chimeric WldS protein composed of the N-terminal 70 aa of Ufd2a/Ube4b, an ubiquitin-chain assembly factor, fused to the complete sequence of NMNAT1
additional information
-
naturally occuring mutant mice, wldS, showing delayed Wallerian degeneration phenotype, suggest that axonal degeneration is an active process, the wldS mutation comprises an 85 kb tandem triplicon, which causes overexpression of the chimeric WldS protein composed of the N-terminal 70 aa of Ufd2a/Ube4b, an ubiquitin-chain assembly factor, fused to the complete sequence of NMNAT1
additional information
NMNAT1 overexpression reduces brain infarction size and improves behavioral outcomes in mice with ischemic stroke
additional information
-
NMNAT1 overexpression reduces brain infarction size and improves behavioral outcomes in mice with ischemic stroke
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, at pH 7.5 in buffer containing both glycerol and TCEP, 6 months, about 20% loss of activity
4°C, at pH 7.5 in buffer containing both glycerol and TCEP, 6 months, about 55% loss of activity
-20°C, at pH 7.5 in buffer containing both glycerol and TCEP, 6 months, about 55% loss of activity
-20°C, at pH 7.5 in buffer containing both glycerol and TCEP, 6 months, about 60% loss of activity
4°C, at pH 7.5 in buffer containing both glycerol and TCEP, 6 months, about 60% loss of activity
4°C, at pH 7.5 in buffer containing both glycerol and TCEP, 6 months, about 90% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Nmnat1, recombinant expression of mouse Nmnat1 non-nuclear-localized gain-of-function mutant gene (m-nonN-Nmnat1) in Caenorhabditis elegans. The transgenic enzyme provides protection from both hypoxia-induced animal death and taxol-induced axonal pathology and significantly lengthens the nematode's lifespan. Loss of function in two genes, haf-1 and dve-1, encoding mitochondrial unfolded protein response (mitoUPR) factors are identified as suppressors. M-nonN-Nmnat1 induces a transcriptional reporter of the mitoUPR gene hsp-6 and provides protection from the mitochondrial proteostasis toxin ethidium bromide. M-nonN-Nmnat1 is also protective against axonal degeneration in Caenorhabditis elegans induced by the chemotherapy drug taxol. Taxol markedly reduces basal expression of a mitoUPR reporter, the expression is restored by m-nonN-Nmnat1
transgenic mice overexpressing NMNAT1 and the mutant WldS(W258A) are generated
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform Nmnat2 protein levels increase dramatically upon differentiation of SH-SY5Y cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the mitochondrial localization of NMNAT activity plays an important role in NMNAT expression-mediated axonal protection
additional information
additional information
The expression of Nmnat1 itself is sufficient to protect axons in an in vitro Wallerian degeneration assay, suggesting that increased NAD production is crucial for axonal protection.
additional information
The expression of Nmnat1 itself is sufficient to protect axons in an in vitro Wallerian degeneration assay, suggesting that increased NAD production is crucial for axonal protection.
additional information
The expression of Nmnat1 itself is sufficient to protect axons in an in vitro Wallerian degeneration assay, suggesting that increased NAD production is crucial for axonal protection.
additional information
The expression of Nmnat1 itself is sufficient to protect axons in an in vitro Wallerian degeneration assay, suggesting that increased NAD production is crucial for axonal protection.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boulton, S.; Kyle, S.; Durkacz, B.W.
Low nicotinamide mononucleotide adenylyltransferase activity in a tiazofurin-resistant cell line: effects on NAD metabolism and DNA repair
Br. J. Cancer
76
845-851
1997
Mus musculus, Mus musculus L1210
Yalowitz, J.A.; Jayaram, H.N.
Modulation of cytotoxicity of benzamide riboside by expression of NMN adenylyltransferase
Curr. Med. Chem.
9
749-758
2002
Saccharomyces cerevisiae, Homo sapiens, Mammalia, Mus musculus
Conforti, L.; Fang, G.; Beirowski, B.; Wang, M.S.; Sorci, L.; Asress, S.; Adalbert, R.; Silva, A.; Bridge, K.; Huang, X.P.; Magni, G.; Glass, J.D.; Coleman, M.P.
NAD(+) and axon degeneration revisited: Nmnat1 cannot substitute for Wld(S) to delay Wallerian degeneration
Cell Death Differ.
14
116-127
2007
Mus musculus
Sasaki, Y.; Araki, T.; Milbrandt, J.
Stimulation of nicotinamide adenine dinucleotide biosynthetic pathways delays axonal degeneration after axotomy
J. Neurosci.
26
8484-8491
2006
Mus musculus (Q99JR6), Mus musculus (Q9EPA7)
Watanabe, M.; Tsukiyama, T.; Hatakeyama, S.
Protection of vincristine-induced neuropathy by WldS expression and the independence of the activity of Nmnat1
Neurosci. Lett.
411
228-232
2007
Mus musculus
Jia, H.; Yan, T.; Feng, Y.; Zeng, C.; Shi, X.; Zhai, Q.
Identification of a critical site in Wld(s): essential for Nmnat enzyme activity and axon-protective function
Neurosci. Lett.
413
46-51
2007
Mus musculus
Yahata, N.; Yuasa, S.; Araki, T.
Nicotinamide mononucleotide adenylyltransferase expression in mitochondrial matrix delays Wallerian degeneration
J. Neurosci.
29
6276-6284
2009
Mus musculus (Q99JR6), Mus musculus (Q9EPA7), Mus musculus
Mayer, P.R.; Huang, N.; Dewey, C.M.; Dries, D.R.; Zhang, H.; Yu, G.
Expression, localization, and biochemical characterization of nicotinamide mononucleotide adenylyltransferase 2
J. Biol. Chem.
285
40387-40396
2010
Mus musculus, Homo sapiens (Q9BZQ4)
Raches, D.W.; Xiao, S.; Kusumanchi, P.; Yalowitz, J.; Sanghani, P.; Long, E.C.; Antony, A.C.; Jayaram, H.N.
Cloning, expression and characterization of mouse (Mus musculus) nicotinamide 5-mononucleotide adenylyltransferase-2
Med. Chem.
7
718-726
2011
Mus musculus
Hicks, A.N.; Lorenzetti, D.; Gilley, J.; Lu, B.; Andersson, K.E.; Miligan, C.; Overbeek, P.A.; Oppenheim, R.; Bishop, C.E.
Nicotinamide mononucleotide adenylyltransferase 2 (Nmnat2) regulates axon integrity in the mouse embryo
PLoS ONE
7
e47869
2012
Mus musculus
Orsomando, G.; Cialabrini, L.; Amici, A.; Mazzola, F.; Ruggieri, S.; Conforti, L.; Janeckova, L.; Coleman, M.P.; Magni, G.
Simultaneous single-sample determination of NMNAT isozyme activities in mouse tissues
PLoS ONE
7
e53271
2012
Mus musculus (Q5HZI3), Mus musculus (Q99JR6), Mus musculus (Q9EPA7), Mus musculus
Mao, X.R.; Kaufman, D.M.; Crowder, C.M.
Nicotinamide mononucleotide adenylyltransferase promotes hypoxic survival by activating the mitochondrial unfolded protein response
Cell Death Dis.
7
e2113
2016
Mus musculus (Q9EPA7), Mus musculus
Liang, J.; Wang, P.; Wei, J.; Bao, C.; Han, D.
Nicotinamide mononucleotide adenylyltransferase 1 protects neural cells against ischemic injury in primary cultured neuronal cells and mouse brain with ischemic stroke through AMP-activated protein kinase activation
Neurochem. Res.
40
1102-1110
2015
Mus musculus (Q9EPA7), Mus musculus
Rossi, F.; Geiszler, P.C.; Meng, W.; Barron, M.R.; Prior, M.; Herd-Smith, A.; Loreto, A.; Lopez, M.Y.; Faas, H.; Pardon, M.C.; Conforti, L.
NAD-biosynthetic enzyme NMNAT1 reduces early behavioral impairment in the htau mouse model of tauopathy
Behav. Brain Res.
339
140-152
2018
Mus musculus (Q9EPA7), Mus musculus
Ma, X.; Zhu, Y.; Lu, J.; Xie, J.; Li, C.; Shin, W.; Qiang, J.; Liu, J.; Dou, S.; Xiao, Y.; Wang, C.; Jia, C.; Long, H.; Yang, J.; Fang, Y.; Jiang, L.; Zhang, Y.; Zhang, S.; Zhai, R.; Liu, C.; Li, D.
Nicotinamide mononucleotide adenylyl transferase uses its NAD+ substrate-binding site to chaperone phosphorylated TAU
eLife
9
e51859
2020
Mus musculus (Q99JR6), Drosophila melanogaster (Q9VC03)
Yue, Z.; Ma, Y.; You, J.; Li, Z.; Ding, Y.; He, P.; Lu, X.; Jiang, J.; Chen, S.; Liu, P.
NMNAT3 is involved in the protective effect of SIRT3 in Ang II-induced cardiac hypertrophy
Exp. Cell Res.
347
261-273
2016
Mus musculus (Q99JR6)
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