The DOI matches its Crossref record; 50 of the 52 references it cites were found in a registry or an index.
Subcellular Compartmentation and Differential Catalytic Properties of the Three Human Nicotinamide Mononucleotide Adenylyltransferase Isoforms
Open accessAbstract
Nicotinamide mononucleotide adenylyltransferase (NMNAT) is the central enzyme of the NAD biosynthetic pathway. Three human NMNAT isoforms have recently been identified, but isoform-specific functions are presently unknown, although a tissue-specific role has been suggested. Analyses of the subcellular localization confirmed NMNAT1 to be a nuclear protein, whereas NMNAT2 and -3 were localized to the Golgi complex and the mitochondria, respectively. This differential subcellular localization points to an organelle-specific, nonredundant function of each of the three proteins. Comparison of the kinetic properties showed that particularly NMNAT3 exhibits a high tolerance toward substrate modifications. Moreover, as opposed to preferred NAD+ synthesis by NMNAT1, the other two isoforms could also form NADH directly from the reduced nicotinamide mononucleotide, supporting a hitherto unknown pathway of NAD generation. A variety of physiological intermediates was tested and exerted only minor influence on the catalytic activities of the NMNATs. However, gallotannin was found to be a potent inhibitor, thereby compromising its use as a specific inhibitor of poly-ADP-ribose glycohydrolase. The presence of substrate-specific and independent nuclear, mitochondrial, and Golgi-specific NAD biosynthetic pathways is opposed to the assumption of a general cellular NAD pool. Their existence appears to be consistent with important compartment-specific functions rather than to reflect simple functional redundance.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“This differential subcellular distribution is consistent with previous observations that found NMNAT1 in the nucleus, NMNAT2 in the Golgi complex and neurites and NMNAT3 in the mitochondria (25,26,55,56).”
In the citing paper
“The three mammalian NMNATs include the nuclear NMNAT1, the cytoplasmic NMNAT2, and the mitochondrial NMNAT3, which is also present in the cytosol (Berger et al., 2005).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Berger et al., 2005
Citations
Cites
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
D’Amours, D., Desnoyers, S., D’Silva, I., & Poirier, G. G. (1999) · Biochemical Journal · doi:10.1042/bj3420249 · Cited by 1,819
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,603
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,497
The Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors
Virág, L., & Szabó, C. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.375 · Cited by 1,373
Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration
Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060
Tankyrase, a Poly(ADP-Ribose) Polymerase at Human Telomeres
Smith, S. H., Giriat, I., Schmitt, A., & de Lange, T. (1998) · Science · doi:10.1126/science.282.5393.1484 · Cited by 1,039
Bieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750
Clapper, D. L., Walseth, T. F., Dargie, P. J., & Lee, H. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47970-7 · Cited by 568
Flagged first, then by citations
2 of the 52 references couldn’t be matched to a known paper.
Research works printed but not linked: 3
- Galione, 2000, Sci. STKE. 2000, PE1
- Magni, 1999, Adv. Enzymol. Relat. Areas Mol. Biol., 73, 135
- Barile, 1996, Biochem. Mol. Biol. Int., 38, 297
Cited by
Sorted by citations
Mammalian Sirtuins: Biological Insights and Disease Relevance
Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648
NAD+ metabolism and its roles in cellular processes during ageing
Covarrubias, A. J., Perrone, R., Grozio, A., & Verdin, E. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00313-x · Cited by 1,617
Ying, W. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1672 · Cited by 1,494
Gomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482
Yoshino, J., Mills, K. F., Yoon, M. J., & Imai, S.-I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.014 · Cited by 1,340
NAD + in aging, metabolism, and neurodegeneration
Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319
NAD(H) and NADP(H) Redox Couples and Cellular Energy Metabolism
Xiao, W., Wang, R., Handy, D. E., & Loscalzo, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7216 · Cited by 1,062
NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
Xie, N., Zhang, L., Gao, W. Q., Huang, C., Huber, P., Zhou, X., Li, C. L., Shen, G., & Zou, B. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00311-7 · Cited by 1,147
NAD+ metabolism in health and disease
Belenky, P. A., Bogan, K. L., & Brenner, C. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.006 · Cited by 1,006
Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival
Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., Lamming, D. W., Souza-Pinto, N. C., Bohr, V. A., Rosenzweig, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.035 · Cited by 950
The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways
Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899
Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence
Rajman, L., Chwalek, K., & Sinclair, D. A. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.011 · Cited by 865
NAD+ in Brain Aging and Neurodegenerative Disorders
Lautrup, S., Sinclair, D. A., Mattson, M. P., & Fang, E. F. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.001 · Cited by 790
SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
Nakagawa, T., Lomb, D. J., Haigis, M. C., & Guarente, L. (2009) · Cell · doi:10.1016/j.cell.2009.02.026 · Cited by 787
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Gupte, R., Liu, Z., & Kraus, W. L. (2017) · Genes & Development · doi:10.1101/gad.291518.116 · Cited by 681
“Like the PARPs that they “feed,” the NMNATs exhibit distinct subcellular localizations: NMNAT-1 (nucleus), NMNAT-2 (cytoplasm and golgi), and NMNAT-3 (mitochondria) (Berger et al. 2005).”
BackgroundNuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
Hassa, P. O., Haenni, S. S., Elser, M., & Hottiger, M. O. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-05 · Cited by 719
The power to reduce: pyridine nucleotides—small molecules with a multitude of functions
Pollak, N., Dölle, C., & Ziegler, M. (2007) · Biochemical Journal · doi:10.1042/bj20061638 · Cited by 730
Self-citationThe NAD metabolome — a key determinant of cancer cell biology
Chiarugi, A., Dölle, C., Felici, R., & Ziegler, M. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3340 · Cited by 660
Self-citationNAD+ homeostasis in health and disease
Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627
Wallerian degeneration: an emerging axon death pathway linking injury and disease
Conforti, L., Gilley, J., & Coleman, M. P. (2014) · Nature reviews. Neuroscience · doi:10.1038/nrn3680 · Cited by 630
Paul, O. H. (2007) · Frontiers in bioscience · doi:10.2741/2909 · Cited by 601
The dynamic regulation of NAD metabolism in mitochondria
Stein, L. R., & Imai, S. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.06.005 · Cited by 558
NAD(+) in aging: molecular mechanisms and translational implications
Fang, E. F., Lautrup, S., Hou, Y., Demarest, T. G., Croteau, D. L., Mattson, M. P., & Bohr, V. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.08.001 · Cited by 501
Endogenous Nmnat2 Is an Essential Survival Factor for Maintenance of Healthy Axons
Gilley, J., & Coleman, M. P. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000300 · Cited by 472
Axon degeneration: Molecular mechanisms of a self-destruction pathway
Wang, J. T., Medress, Z. A., & Barres, B. A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201108111 · Cited by 464
Wallerian Degeneration, WldS, and Nmnat
Coleman, M. P., & Freeman, M. R. (2010) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-060909-153248 · Cited by 473
NAD+ metabolism governs the proinflammatory senescence-associated secretome
Nacarelli, T., Lau, L., Fukumoto, T., Zundell, J., Fatkhutdinov, N., Wu, S., Aird, K. M., Iwasaki, O., Kossenkov, A. V., Schultz, D., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0287-4 · Cited by 402
Biosensor reveals multiple sources for mitochondrial NAD +
Cambronne, X. A., Stewart, M. L., Kim, D., Jones-Brunette, A. M., Morgan, R. K., Farrens, D. L., Cohen, M. S., & Goodman, R. H. (2016) · Science · doi:10.1126/science.aad5168 · Cited by 407
Role of NAD+ in regulating cellular and metabolic signaling pathways
Amjad, S., Nisar, S., Bhat, A. A., Shah, A. R., Frenneaux, M. P., Fakhro, K. A., Haris, M., Reddy, R. D., Patay, Z. J., Baur, J. A., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101195 · Cited by 413
Sirtuins mediate mammalian metabolic responses to nutrient availability
Chalkiadaki, A., & Guarente, L. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.225 · Cited by 344
Metabolic Regulation of Histone Post-Translational Modifications
Fan, J., Krautkramer, K. A., Feldman, J. L., & Denu, J. M. (2015) · ACS Chemical Biology · doi:10.1021/cb500846u · Cited by 339
Protein acetylation in metabolism – metabolites and cofactors
Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331
Pathways and Subcellular Compartmentation of NAD Biosynthesis in Human Cells
Nikiforov, A., Dölle, C., Niere, M., & Ziegler, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213298 · Cited by 326
Self-citationNAD+ Repletion Rescues Female Fertility during Reproductive Aging
Bertoldo, M. J., Listijono, D. R., Ho, W.-H. J., Riepsamen, A. H., Goss, D. M., Richani, D., Jin, X. L., Mahbub, S. B., Campbell, J. M., Habibalahi, A., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.01.058 · Cited by 334
Keating, S. T., & El‐Osta, A. (2015) · Circulation Research · doi:10.1161/circresaha.116.303936 · Cited by 324
SLC25A51 is a mammalian mitochondrial NAD(+) transporter
Luongo, T. S., Eller, J. M., Lu, M.-J., Niere, M., Raith, F., Perry, C., Bornstein, M. R., Oliphint, P., Wang, L., McReynolds, M. R., et al. (2020) · Nature · doi:10.1038/s41586-020-2741-7 · Cited by 308
Self-citationZhang, T., & Kraus, W. L. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.10.022 · Cited by 314
NAD+ and Vitamin B3: From Metabolism to Therapies
Sauve, A. A. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.120758 · Cited by 307
Pre-B cell colony-enhancing factor (PBEF)/visfatin: a novel mediator of innate immunity
Luk, T., Malam, Z., & Marshall, J. C. (2008) · Journal of Leukocyte Biology · doi:10.1189/jlb.0807581 · Cited by 303
Braidy, N., Berg, J., Clement, J., Khorshidi, F., Poljak, A., Jayasena, T., Grant, R., & Sachdev, P. S. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7269 · Cited by 294
NAD metabolism: Implications in aging and longevity
Yaku, K., Okabe, K., & Nakagawa, T. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.05.006 · Cited by 269
Bacteria Boost Mammalian Host NAD Metabolism by Engaging the Deamidated Biosynthesis Pathway
Shats, I., Williams, J. G., Liu, J., Makarov, M. V., Wu, X., Lih, F. B., Deterding, L. J., Lim, C., Xu, X., Randall, T. A., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.02.001 · Cited by 242
NAD+ and NADH in cellular functions and cell death
Ying, W. (2006) · Frontiers in bioscience · doi:10.2741/2038 · Cited by 255
A rise in NAD precursor nicotinamide mononucleotide (NMN) after injury promotes axon degeneration
Di Stefano, M., Nascimento-Ferreira, I., Orsomando, G., Mori, V, Gilley, J., Brown, R., Janeckova, L., Vargas, M. E., Worrell, L. A., Loreto, A., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.164 · Cited by 246
“In mammals, three NMNAT isoforms, nuclear NMNAT1, cytoplasmic NMNAT2 and mitochondrial NMNAT3, catalyse nicotinamide adenine dinucleotide (NAD) synthesis from nicotinamide mononucleotide (NMN) and adenosine triphosphate (ATP; Figure 1a).(11,12) Several reports indicate Wld protects injured axons by maintaining axonal…”
BackgroundSasaki, Y., Vohra, B. P. S., Lund, F. E., & Milbrandt, J. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5469-08.2009 · Cited by 252
Huang, J.-Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.021 · Cited by 231
Enzymes in the NAD+ Salvage Pathway Regulate SIRT1 Activity at Target Gene Promoters
Zhang, T., Berrocal, J. G., Frizzell, K. M., Gamble, M. J., DuMond, M. E., Krishnakumar, R., Yang, T., Sauve, A. A., & Kraus, W. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016469 · Cited by 234
Microbial NAD Metabolism: Lessons from Comparative Genomics
Gazzaniga, F., Stebbins, R., Chang, S. Z., McPeek, M. A., & Brenner, C. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00042-08 · Cited by 230
Implications of altered NAD metabolism in metabolic disorders
Okabe, K., Yaku, K., Tobe, K., & Nakagawa, T. (2019) · Journal of Biomedical Science · doi:10.1186/s12929-019-0527-8 · Cited by 223
NAD Metabolism in Cancer Therapeutics
Yaku, K., Okabe, K., Hikosaka, K., & Nakagawa, T. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00622 · Cited by 229
Modulating NAD+ metabolism, from bench to bedside
Katsyuba, E., & Auwerx, J. H. (2017) · The EMBO Journal · doi:10.15252/embj.201797135 · Cited by 231
Role of NAD+ and mitochondrial sirtuins in cardiac and renal diseases
Hershberger, K. A., Martin, A. S., & Hirschey, M. D. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.5 · Cited by 220
NAMPT and NAPRT: Two Metabolic Enzymes With Key Roles in Inflammation
Audrito, V., Messana, V. G., & Deaglio, S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00358 · Cited by 215
Axonal Degeneration Is Mediated by the Mitochondrial Permeability Transition Pore
Barrientos, S. A., Martínez, N. W., Yoo, S., Jara, J. S., Zamorano, S., Hetz, C. A., Twiss, J. L., Álvarez, J., & Court, F. A. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4065-10.2011 · Cited by 214
The Highwire Ubiquitin Ligase Promotes Axonal Degeneration by Tuning Levels of Nmnat Protein
Xiong, X., Hao, Y., Sun, K., Li, J., Li, X., Mishra, B., Soppina, P., Wu, C., Hume, R. I., & Collins, C. A. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001440 · Cited by 202
NMNAT1 mutations cause Leber congenital amaurosis
Falk, M. J., Zhang, Q., Nakamaru‐Ogiso, E., Kannabiran, C., Fonseca-Kelly, Z., Chakarova, C. F., Audo, I. S., Mackay, D. S., Zeitz, C., Borman, A. D., et al. (2012) · Nature Genetics · doi:10.1038/ng.2361 · Cited by 201
Emerging therapeutic roles for NAD+ metabolism in mitochondrial and age‐related disorders
Srivastava, S. (2016) · Clinical and Translational Medicine · doi:10.1186/s40169-016-0104-7 · Cited by 200
Sonne, S. B., Almstrup, K., Dalgaard, M., Juncker, A. S., Edsgärd, D., Ruban, L., Harrison, N. J., Schwager, C., Abdollahi, A., Huber, P. E., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4554 · Cited by 201
The role of NAD biosynthesis in plant development and stress responses
Hashida, S.-N., Takahashi, H., & Uchimiya, H. (2009) · Annals of Botany · doi:10.1093/aob/mcp019 · Cited by 195
A conserved NAD + binding pocket that regulates protein-protein interactions during aging
Li, J., Bonkowski, M. S., Moniot, S., Zhang, D., Hubbard, B. P., Ling, A. J. Y., Rajman, L. A., Qin, B., Lou, Z., Gorbunova, V. A., et al. (2017) · Science · doi:10.1126/science.aad8242 · Cited by 188
PARPs in lipid metabolism and related diseases
Szántó, M., Gupte, R., Kraus, W. L., Pacher, P., & Bai, P. (2021) · Progress in Lipid Research · doi:10.1016/j.plipres.2021.101117 · Cited by 181
The neuroimmunology of degeneration and regeneration in the peripheral nervous system
Oranburg, T. D., Lindborg, J. A., Niemi, J. P., & Zigmond, R. E. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.09.027 · Cited by 180
Boosting NAD+ with a small molecule that activates NAMPT
Gardell, S. J., Hopf, M., Khan, A., Dispagna, M., Hampton Sessions, E., Falter, R., Kapoor, N., Brooks, J., Culver, J., Petucci, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11078-z · Cited by 169
Extracellular NAD and ATP: Partners in immune cell modulation
Haag, F., Adriouch, S., Braß, A., Jung, C., Möller, S., Scheuplein, F., Bannas, P., Séman, M., & Koch‐Nolte, F. (2007) · Purinergic Signalling · doi:10.1007/s11302-006-9038-7 · Cited by 169
Metabolic Profiling of Alternative NAD Biosynthetic Routes in Mouse Tissues
Mori, V., Amici, A., Mazzola, F., Stefano, M. D., Conforti, L., Magni, G., Ruggieri, S., Raffaelli, N., & Orsomando, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113939 · Cited by 158
Yahata, N., Yuasa, S., & Araki, T. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4304-08.2009 · Cited by 154
“Previous reports suggest that NMNAT3 is located mainly, but not exclusively, in mitochondria when it is transiently overexpressed in cultured cells (Zhang et al., 2003; Berger et al., 2005); however, we found that NMNAT3 was located almost exclusively in mitochondria of NMNAT3-Tg mice.”
BackgroundInfluentialOxidative stress induces autophagy in response to multiple noxious stimuli in retinal ganglion cells
Lin, W., & Kuang, H. (2014) · Autophagy · doi:10.4161/auto.36076 · Cited by 154
The role of NAD+ metabolism and its modulation of mitochondria in aging and disease
Yusri, K., Jose, S., Vermeulen, K. S., Tan, T. C. M., & Sorrentino, V. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-025-00067-0 · Cited by 194
Nicotinamide adenine dinucleotide is transported into mammalian mitochondria
Davila, A., Liu, L., Chellappa, K., Redpath, P., Nakamaru-Ogiso, E., Paolella, L. M., Zhang, Z., Migaud, M. E., Rabinowitz, J. D., & Baur, J. A. (2018) · eLife · doi:10.7554/elife.33246 · Cited by 142
Perrault, I., Hanein, S., Zanlonghi, X., Serre, V., Nicouleau, M., Defoort‐Dhellemmes, S., Delphin, N., Fares‐Taie, L., Gerber, S., Xerri, O., et al. (2012) · Nature Genetics · doi:10.1038/ng.2357 · Cited by 150
New Facets in the Regulation of Gene Expression by ADP-Ribosylation and Poly(ADP-ribose) Polymerases
Ryu, K. W., Kim, D.-S., & Kraus, W. L. (2015) · Chemical Reviews · doi:10.1021/cr5004248 · Cited by 151
Transgenic Mice Expressing the Nmnat1 Protein Manifest Robust Delay in Axonal Degeneration In Vivo
Sasaki, Y., Vohra, B. P. S., Baloh, R. H., & Milbrandt, J. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.1429-09.2009 · Cited by 152
Transfer of metabolites across the peroxisomal membrane
Antonenkov, V. D., & Hiltunen, J. K. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.011 · Cited by 150
Valenti, D., Rasmo, D. D., Signorile, A., Rossi, L., Lidia de, B. A. R. I., Scala, I., Granese, B., Papa, S., & Vacca, R. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.12.011 · Cited by 146
NAD+ salvage pathway in cancer metabolism and therapy
Kennedy, B. E., Sharif, T., Martell, E., Dai, C., Kim, Y., Lee, P. W. K., & Gujar, S. A. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.10.027 · Cited by 149
Nicotinamide Mononucleotide: Exploration of Diverse Therapeutic Applications of a Potential Molecule
Poddar, S. K., Sifat, A. E., Haque, S., Nahid, N. A., Chowdhury, S., & Mehedi, I. (2019) · Biomolecules · doi:10.3390/biom9010034 · Cited by 134
Conforti, L., Fang, G., Beirowski, B., Wang, M. S., Sorci, L., Asress, S., Adalbert, R., Silva, A., Bridge, K., Huang, X. P., et al. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401944 · Cited by 137
Cambronne, X. A., & Kraus, W. L. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.05.010 · Cited by 137
Preclinical and clinical evidence of NAD+ precursors in health, disease, and ageing
Reiten, O. K., Wilvang, M. A., Mitchell, S. J., Hu, Z., & Fang, E. F. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111567 · Cited by 136
Nmnat delays axonal degeneration caused by mitochondrial and oxidative stress
Press, C., & Milbrandt, J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.0525-08.2008 · Cited by 137
“adenine dinucleotide (NAD ) (Araki et al., 2004; Berger et al., 2005), although recent studies in Drosophila neurodegeneration have suggested that additional Nmnat activities may also be important for synaptic protection (Zhai et al.”
BackgroundThe NMN/NaMN adenylyltransferase (NMNAT) protein family
Lau, C. (2009) · Frontiers in bioscience · doi:10.2741/3252 · Cited by 134
Self-citationGujar, A. D., Le, S. B., Mao, D. D., Dadey, D. Y. A., Turski, A., Sasaki, Y., Aum, D. J., Luo, J. R., Dahiya, S. M., Yuan, L., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610921114 · Cited by 134
Giroud‐Gerbetant, J., Joffraud, M., Giner, M. P., Cercillieux, A., Bártová, S., Makarov, M. V., Perez, R. Z., Sánchez-García, J. L., Houtkooper, R. H., Migaud, M. E., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.09.013 · Cited by 132
NMNAT2:HSP90 Complex Mediates Proteostasis in Proteinopathies
Ali, Y., Allen, H. M., Yu, L., Li‐Kroeger, D., Bakhshizadehmahmoudi, D., Hatcher, A., Aubin, C., Xu, J., Bjorklund, N. L., Taglialatela, G., et al. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002472 · Cited by 131
Milde, S., Gilley, J., & Coleman, M. P. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001539 · Cited by 128
Epistasis-driven identification of SLC25A51 as a regulator of human mitochondrial NAD import
Girardi, E., Agrimi, G., Goldmann, U., Fiume, G., Lindinger, S., Sedlyarov, V., Srndic, I., Gürtl, B., Agerer, B., Kartnig, F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19871-x · Cited by 123
Pharmacological Effects of Exogenous NAD on Mitochondrial Bioenergetics, DNA Repair, and Apoptosis
Pittelli, M. G., Felici, R., Pitozzi, V., Giovannelli, L., Bigagli, E., Cialdai, F., Romano, G., Moroni, F., & Chiarugi, A. (2011) · Molecular Pharmacology · doi:10.1124/mol.111.073916 · Cited by 125
Rescue of Peripheral and CNS Axon Defects in Mice Lacking NMNAT2
Gilley, J., Adalbert, R., Yu, G., & Coleman, M. P. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1534-13.2013 · Cited by 129
Axonal degeneration as a therapeutic target in the CNS
Lingor, P., Koch, J. C., Tönges, L., & Bähr, M. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1362-3 · Cited by 119
Targeting NMNAT1 to Axons and Synapses Transforms Its Neuroprotective PotencyIn Vivo
Babetto, E., Beirowski, B., Janečková, L., Brown, R., Gilley, J., Thomson, D., Ribchester, R. R., & Coleman, M. P. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1189-10.2010 · Cited by 124
NAD+ and NADH in brain functions, brain diseases and brain aging
Ying, W. (2006) · Frontiers in bioscience · doi:10.2741/2194 · Cited by 124
Non-metabolic functions of glycolytic enzymes in tumorigenesis
Yu, X., & Li, S. (2016) · Oncogene · doi:10.1038/onc.2016.410 · Cited by 114
Nampt/PBEF/Visfatin: A regulator of mammalian health and longevity?
Yang, H., Lavu, S., & Sinclair, D. A. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.06.003 · Cited by 113
The chemistry of the vitamin B3 metabolome
Makarov, M. V., Trammell, S. A. J., & Migaud, M. E. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180420 · Cited by 115
Interplay between compartmentalized NAD + synthesis and consumption: a focus on the PARP familyPreprint
Cohen, M. S. (2020) · Genes & Development · doi:10.1101/gad.335109.119 · Cited by 111
Axonal protection by Nmnat3 overexpression with involvement of autophagy in optic nerve degeneration
Kitaoka, Y., Munemasa, Y., Kojima, K., Hirano, A., Ueno, S., & Takagi, H. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.391 · Cited by 108
NAD + Biosynthesis and Signaling in Plants
Gakière, B., Hao, J., de Bont, L., Pétriacq, P., Nunes-Nesi, A., & Fernie, A. R. (2018) · Critical Reviews in Plant Sciences · doi:10.1080/07352689.2018.1505591 · Cited by 108
Braidy, N., Grant, R., Adams, S., & Guillemin, G. J. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07487.x · Cited by 110
Ljungberg, M. C., Ali, Y. O., Zhu, J., Wu, C.-S., Oka, K., Zhai, R. G., & Lu, H.-C. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr492 · Cited by 107
Metadata
- Authors
- Berger, F., Lau, C., Dahlmann, M., & Ziegler, M.
- Affiliations
- Freie Universität Berlin (DE)
- University of Bergen (NO)
- Corresponding author
- Ziegler, Mathias
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-10
- Volume
- 280
- Issue
- 43
- Pages
- 36334-36341
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2068128334
- Cited by
- 508
- References
- 52
- Citations by year
- 2026: 14 · 2025: 30 · 2024: 36 · 2023: 23 · 2022: 29 · 2021: 40 · 2020: 39 · 2019: 35 · 2018: 39 · 2017: 21 · 2016: 22 · 2015: 23 · 2014: 16 · 2013: 23 · 2012: 20
- FWCI
- 4.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- nicotinamide mononucleotide adenylyltransferase, NAD biosynthesis, subcellular compartmentalization, Golgi apparatus, mitochondria, nuclear localization, enzyme kinetics, substrate tolerance, NADH production, gallotannins, functional redundancy
- MeSH terms
- Adenosine Triphosphate, Catalysis, Cell Line, Cell Nucleus, Cloning, Molecular, Glycoside Hydrolases, Golgi Apparatus, HeLa Cells, Humans, Kinetics, Nicotinamide-Nucleotide Adenylyltransferase, Poly(ADP-ribose) Polymerases, Protein Conformation, Substrate Specificity, Time Factors, Tissue Distribution, DNA, Complementary, Protein Isoforms, Catalytic Domain, Hydrolyzable Tannins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
