N4256

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显示 1-14 共 14 条结果关于 "N4256" 范围论文

The SARM1 toll/interleukin-1 receptor domain possesses intrinsic NAD+ cleavage activity that promotes pathological axonal degeneration

Essuman K, et al.

Neuron, 93(6), 1334-1343 (2017)

Protocol for the Analysis of Yeast and Human Mitochondrial Respiratory Chain Complexes and Supercomplexes by Blue Native Electrophoresis.

Alba Timón-Gómez et al.

STAR protocols, 1(2) (2020-10-01)

By using negatively charged Coomassie brilliant blue G-250 dye to induce a charge shift on proteins, blue native polyacrylamide gel electrophoresis (BN-PAGE) allows resolution of enzymatically active multiprotein complexes extracted from cellular or subcellular lysates while retaining their native conformation.

Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements.

Ralf Jauch et al.

The Journal of biological chemistry, 280(15), 15131-15140 (2005-02-09)

Nicotinamide adenine dinucleotide synthetases (NADS) catalyze the amidation of nicotinic acid adenine dinucleotide (NAAD) to yield the enzyme cofactor nicotinamide adenine dinucleotide (NAD). Here we describe the crystal structures of the ammonia-dependent homodimeric NADS from Escherichia coli alone and in

Nicotinamide Riboside Augments the Aged Human Skeletal Muscle NAD+ Metabolome and Induces Transcriptomic and Anti-inflammatory Signatures.

Yasir S Elhassan et al.

Cell reports, 28(7), 1717-1728 (2019-08-15)

Nicotinamide adenine dinucleotide (NAD+) is modulated by conditions of metabolic stress and has been reported to decline with aging in preclinical models, but human data are sparse. Nicotinamide riboside (NR) supplementation ameliorates metabolic dysfunction in rodents. We aimed to establish

Bacteria Boost Mammalian Host NAD Metabolism by Engaging the Deamidated Biosynthesis Pathway.

Igor Shats et al.

Cell metabolism, 31(3), 564-579 (2020-03-05)

Nicotinamide adenine dinucleotide (NAD), a cofactor for hundreds of metabolic reactions in all cell types, plays an essential role in metabolism, DNA repair, and aging. However, how NAD metabolism is impacted by the environment remains unclear. Here, we report an

Mechanism of sirtuin inhibition by nicotinamide: altering the NAD+ co-substrate specificity of a Sir2 enzyme

Avalos JL, et al.

Molecular Cell, 17(6), 855-868 (2005)

A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme NPP5.

Alexei Gorelik et al.

The FEBS journal, 284(21), 3718-3726 (2017-09-13)

The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) family of proteins mediates purinergic signaling by degrading extracellular nucleotides and also participates in phospholipid metabolism. NPP5 (ENPP5) is the least characterized member of this group and its specific role is unknown. This enzyme does not

Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD.

Hong Zhang et al.

Structure (London, England : 1993), 10(1), 69-79 (2002-02-14)

Nicotinamide/Nicotinate mononucleotide (NMN/NaMN) adenylyltransferase is an indispensable enzyme in both de novo biosynthesis and salvage of NAD+ and NADP+. In prokaryotes, it is absolutely required for cell survival, thus representing an attractive target for the development of new broad-spectrum antibacteria

Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme.

José L Avalos et al.

Molecular cell, 17(6), 855-868 (2005-03-23)

Sir2 enzymes form a unique class of NAD(+)-dependent deacetylases required for diverse biological processes, including transcriptional silencing, regulation of apoptosis, fat mobilization, and lifespan regulation. Sir2 activity is regulated by nicotinamide, a noncompetitive inhibitor that promotes a base-exchange reaction at

Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis.

Shanyun Lu et al.

Acta crystallographica. Section F, Structural biology and crystallization communications, 64(Pt 10), 893-898 (2008-10-22)

Nicotinic acid mononucleotide adenylyltransferase (NaMNAT; EC 2.7.7.18) is the penultimate enzyme in the biosynthesis of NAD(+) and catalyzes the adenylation of nicotinic acid mononucleotide (NaMN) by ATP to form nicotinic acid adenine dinucleotide (NaAD). This enzyme is regarded as a

Mycobacterial nicotinate mononucleotide adenylyltransferase structure, mechanism, and implications for drug discovery

Rodionova IA, et al.

Test, 290(12), 7693-7706 (2015)

Simultaneous measurement of NAD metabolome in aged mice tissue using liquid chromatography tandem-mass spectrometry.

Keisuke Yaku et al.

Biomedical chromatography : BMC, 32(6), e4205-e4205 (2018-02-10)

Nicotinamide adenine dinucleotide (NAD) is a major co-factor that mediates multiple biological processes including redox reaction and gene expression. Recently, NAD metabolism has received considerable attention because administration of NAD precursors exhibited beneficial effects against aging-related metabolic disorders in animals.

Stimulation of nicotinamide adenine dinucleotide biosynthetic pathways delays axonal degeneration after axotomy

Sasaki Y, et al.

The Journal of Neuroscience, 26(33), 8484-8491 (2006)

Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry.

Anthony A Sauve et al.

Biochemistry, 42(31), 9249-9256 (2003-08-06)

Life span regulation and inhibition of gene silencing in yeast have been linked to nicotinamide effects on Sir2 enzymes. The Sir2 enzymes are NAD(+)-dependent protein deacetylases that influence gene expression by forming deacetylated proteins, nicotinamide and 2'-O-acetyl-ADPR. Nicotinamide is a

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