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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Nicotinamide nucleotide adenylyltransferase 3

Nmnat3, PNAT-3
This gene encodes a member of the nicotinamide/nicotinic acid mononucleotide adenylyltransferase family. These enzymes use ATP to catalyze the synthesis of nicotinamide adenine dinucleotide or nicotinic acid adenine dinucleotide from nicotinamide mononucleotide or nicotinic acid mononucleotide, respectively. The encoded protein is localized to mitochondria and may also play a neuroprotective role as a molecular chaperone. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jan 2011] (from NCBI)
Top mentioned proteins: Nicotinamide-Nucleotide Adenylyltransferase, NMNAT2, CAN, ACID, HAD
Papers on Nmnat3
Obesity Is Associated With Low NAD(+)/SIRT Pathway Expression in Adipose Tissue of BMI-Discordant Monozygotic Twins.
Pietiläinen et al., Düsseldorf, Germany. In J Clin Endocrinol Metab, Jan 2016
RESULTS: SIRT1, SIRT3, SIRT5, NAMPT, NMNAT2, NMNAT3, and NRK1 expressions were significantly down-regulated and the activity of main cellular NAD(+) consumers, PARPs, trended to be higher in the SAT of heavier co-twins of body mass index-discordant pairs.
Nmnat3 Is Dispensable in Mitochondrial NAD Level Maintenance In Vivo.
Nakagawa et al., Toyama, Japan. In Plos One, Dec 2015
It has been proposed that NAD synthesis enzyme, Nmnat3, was localized in mitochondria, but its physiological relevance to the metabolism in mitochondria was not fully elucidated.
Subcellular Distribution of NAD+ between Cytosol and Mitochondria Determines the Metabolic Profile of Human Cells.
Ziegler et al., Bergen, Norway. In J Biol Chem, Dec 2015
In contrast, human recombinant NMNAT3 localizes to the mitochondrial matrix and is able to catalyze NAD(+) biosynthesis in vitro.
Deficiency of nicotinamide mononucleotide adenylyltransferase 3 (nmnat3) causes hemolytic anemia by altering the glycolytic flow in mature erythrocytes.
Nakagawa et al., Saitama, Japan. In J Biol Chem, 2014
Nicotinamide mononucleotide adenylyltransferase 3 (Nmnat3) is considered a mitochondria-localized NAD synthesis enzyme involved in de novo and salvage pathways.
Axonal protection by Nmnat3 overexpression with involvement of autophagy in optic nerve degeneration.
Takagi et al., Kawasaki, Japan. In Cell Death Dis, 2012
In this study, Nmnat3 immunoreactivity was observed inside axons in the optic nerve.
Insight into molecular and functional properties of NMNAT3 reveals new hints of NAD homeostasis within human mitochondria.
Chiarugi et al., Florence, Italy. In Plos One, 2012
Although NMNAT3 is postulated to be a mitochondrial enzyme contributing to NAD-dependent organelle functioning, information on endogenous proteins is lacking.
CREB-activity and nmnat2 transcription are down-regulated prior to neurodegeneration, while NMNAT2 over-expression is neuroprotective, in a mouse model of human tauopathy.
Lu et al., Houston, United States. In Hum Mol Genet, 2012
We found that over-expressing NMNAT2 or its homolog NMNAT1, but not NMNAT3, in rTg4510 hippocampi from 6 weeks of age using recombinant adeno-associated viral vectors significantly reduced neurodegeneration caused by tau(P301L) over-expression at 5 months of age.
WldS but not Nmnat1 protects dopaminergic neurites from MPP+ neurotoxicity.
O'Malley et al., Saint Louis, United States. In Mol Neurodegener, 2011
RESULTS: Using mutant mice and lentiviral transduction of dopaminergic neurons, the present findings demonstrate that WldS but not Nmnat1, Nmnat3, or cytoplasmically-targeted Nmnat1 protects dopamine axons from the parkinsonian mimetic N-methyl-4-phenylpyridinium (MPP+).
Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation.
Ziegler et al., Bergen, Norway. In J Biol Chem, 2011
When taken up into the organelles, NMN (together with ATP) serves as substrate of NMNAT3 to form NAD. NMNAT3 was conclusively localized to the mitochondrial matrix and is the only known enzyme of NAD synthesis residing within these organelles.
NMNAT expression and its relation to NAD metabolism.
Yalowitz et al., Indianapolis, United States. In Curr Med Chem, 2010
Based on their localization, three different NMNAT's have been recognized, NMNAT-1 (homohexamer) in the nucleus (chromosome 1 p32-35), NMNAT-2 (homodimer) in the cytoplasm (chromosome 1q25) and NMNAT-3 (homotetramer) in the mitochondria.
Homology modeling and deletion mutants of human nicotinamide mononucleotide adenylyltransferase isozyme 2: new insights on structure and function relationship.
Magni et al., Ancona, Italy. In Protein Sci, 2010
Humans possess three NMNAT isozymes (NMNAT1, NMNAT2, and NMNAT3) that differ in size and sequence, gene expression pattern, subcellular localization, oligomeric state and catalytic properties.
Unique expression pattern of human nicotinamide mononucleotide adenylyltransferase isozymes in red blood cells.
Magni et al., Ancona, Italy. In Blood Cells Mol Dis, 2010
Red blood cells represent the first human cell type with a remarkable predominance of NMNAT3 over NMNAT1; NMNAT2 is absent.
Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases.
Ziegler et al., Bergen, Norway. In J Biol Chem, 2010
analysis of isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases
Axon degeneration: Mechanisms and implications of a distinct program from cell death.
Zhai et al., Shanghai, China. In Neurochem Int, 2010
The mitochondrial Nmnat3 and cytoplasm-localized mutants of Wld(S) and Nmnat1 have similar or even stronger effect than Wld(S) to delay axon degeneration, which suggest that increased mitochondrial or local NAD synthesis might contribute to the protective function of Wld(S) and Nmnats.
Endogenous Nmnat2 is an essential survival factor for maintenance of healthy axons.
Coleman et al., Cambridge, United Kingdom. In Plos Biol, 2010
Specific depletion of Nmnat2 is sufficient to induce Wallerian-like degeneration of uninjured axons which endogenous Nmnat1 and Nmnat3 cannot prevent.
Nmnat2 delays axon degeneration in superior cervical ganglia dependent on its NAD synthesis activity.
Zhai et al., Shanghai, China. In Neurochem Int, 2010
Overexpression of Nmnat1 or Nmnat3 can delay axon degeneration, while the role of Nmnat2 in axon degeneration remains largely unknown.
Nicotinamide mononucleotide adenylyltransferase expression in mitochondrial matrix delays Wallerian degeneration.
Araki et al., Kodaira, Japan. In J Neurosci, 2009
results suggest that axonal protection by NMNAT expression in neurons is provided by modifying mitochondrial functionNMNAT activity does lead to axonal protection phenotype in vivo
Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis.
Magni et al., Ancona, Italy. In Biochemistry, 2007
NMN binds before ATP with the mitochondrial isozyme NMNAT3. Only NMNAT3 utilizes ITP efficiently in place of ATP, and NMNH conversion to NADH by NMNAT1 and NMNAT3 occurs at similar rates.
Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms.
Ziegler et al., Berlin, Germany. In J Biol Chem, 2005
NMNAT1 is a nuclear protein, whereas NMNAT2 and -3 are localized to the Golgi complex and the mitochondria
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