Charles Brenner (biochemist)

Last updated
Charles Brenner
Born(1961-10-30)October 30, 1961
NationalityAmerican
Alma mater Wesleyan University (BA)
Stanford University (PhD)
Brandeis University
Known forDiscovery and characterization of nicotinamide riboside as a vitamin
AwardsFellow of the American Association for the Advancement of Science
Scientific career
FieldsEnzymology
Metabolism
Institutions City of Hope National Medical Center
University of Iowa
Dartmouth Medical School
Thomas Jefferson University
Thesis Specificity and Activity of the Kex2 Protease: From Yeast Genetics to Enzyme Kinetics  (1993)
Doctoral advisor Robert S. Fuller
Other academic advisors Gregory A. Petsko
Dagmar Ringe
Notable studentsPeter A. Belenky, Samuel A.J. Trammell
Website brennerlab.net

Charles Brenner (born October 30, 1961) is the inaugural Alfred E Mann Family Foundation Chair of the Department of Diabetes & Cancer Metabolism at the Beckman Research Institute of the City of Hope National Medical Center. Brenner previously held the Roy J. Carver Chair in Biochemistry and was head of biochemistry at the University of Iowa. [1] [2]

Contents

Brenner is a major contributor in the field of nicotinamide adenine dinucleotide (NAD) metabolism and has developed targeted, quantitative methods for NAD metabolomics. [3] Brenner discovered eukaryotic nicotinamide riboside (NR) kinase and nucleosidase pathways to NAD. [4] [5] Brenner's work includes the first human trial of NR, which demonstrated safe oral availability as an NAD+ precursor. [6] [4] He has characterized ways in which NAD is disrupted by diseases and metabolic stress. [2]

Education and career

Brenner graduated from Wesleyan University with a bachelor's degree in biology in 1983. After working for the biotechnology companies Chiron Corporation and DNAX Research Institute, Brenner attended graduate school at Stanford University School of Medicine. At Stanford he worked with Robert S. Fuller, receiving his Ph.D. in Cancer Biology in 1993. Brenner conducted post-doctoral research at Brandeis University with Gregory Petsko and Dagmar Ringe. [7] [8]

Brenner then joined the faculty at Thomas Jefferson University, where he worked from 1996-2003, becoming Director of the Structural Biology & Bioinformatics Program in 2000. He moved to Dartmouth Medical School in 2003, serving as Associate Director for Basic Sciences at Norris Cotton Cancer Center (now named Dartmouth Cancer Center) from 2003-2009. In 2009 he joined the University of Iowa (UI) as Professor and Departmental Executive Officer (DEO) of Biochemistry. In 2010 he became the Roy J. Carver Chair of Biochemistry at UI, holding that position until 2020. [9] [2] [10]

In 2020, Brenner joined City of Hope National Medical Center in Duarte, California as the inaugural Alfred E Mann Family Foundation Chair in Diabetes and Cancer Metabolism. City of Hope created the position and the associated Department of Diabetes & Cancer Metabolism to focus on underlying metabolism and the intersection of metabolic disturbances with diseases such as cancer and diabetes. [2] [1]

Brenner has been funded by agencies including the March of Dimes, [11] the Burroughs Wellcome Fund, [11] the Beckman Foundation, [12] the Lung Cancer Research Foundation, [13] the Bill & Melinda Gates Foundation, [14] the Leukemia & Lymphoma Society, the National Science Foundation. and the National Institutes of Health. [15]

Research contributions

Brenner has made multiple contributions to molecular biology and biochemistry, beginning with purification and characterization of the Kex2 proprotein convertase at Stanford. [16] [17] Significant research projects include the role of Ap3A bindings in the function of the FHIT tumor suppressor gene, [18] characterization and inhibition of DNA methylation, [19] [20] and discovery of new steps in nicotinamide adenine dinucleotide (NAD) metabolism. [21]

Notably, the Brenner laboratory discovered that eukaryotes use nicotinamide riboside (NR) to make NAD+. Bieganowski and Brenner (2004) found that NR is converted to NAD+ through the action of nicotinamide ribose kinases including Nrk1 (yeast and human) and Nrk2 (human). Belenky et al (Cell, 2007) reported another pathway which turns NR into NAM through the action of nucleosidases Urh1/Pnp1/Meu1 and is Nrk1 independent. [4] [22] [6] [23]

NRK1/2 mediated pathway from NR to NAD+ NRK1 and NRK2 mediated biosynthesis pathway from NR to NAD+.png
NRK1/2 mediated pathway from NR to NAD+

Brenner has developed targeted, quantitative analysis of the NAD+ metabolome [3] [24] and made fundamental contributions to NAD metabolism including discovery of nicotinic acid riboside-dependent NAD synthesis, [25] elucidating the mechanism of synthesis of nicotinic acid adenine dinucleotide phosphate, [26] and discovering multiple conditions in which NAD metabolism is dysregulated in disease. [27] [28] [29] [30] [31] [32]

Brenner is active in translating NR technologies to treat and prevent human conditions that disturb the NAD system including cancer [29] diabetic and chemotherapeutic peripheral neuropathy, [33] [34] heart failure, [28] central brain injury, [30] inflammation, [31] mitochondrial myopathy [32] pellagra, and infections [27] such as coronavirus infection [6] [35] Brenner's work included the first human trial of NR in 2016, which demonstrated safe oral availability as an NAD+ precursor. [6] [4] Though Brenner was the first to show that NR increases SIR2 activity, improves gene silencing, and can extend yeast lifespan, [6] [36] his work has not emphasized sirtuins or nonspecific anti-aging claims and instead emphasizes how NR repairs metabolic stresses that dysregulate NAD+ [28] [30] and NADPH. [6] [37]

External videos
Nuvola apps kaboodle.svg “Combating Postpartum Metabolic Stress/Cell Reports, Jan. 22, 2019 (Vol. 22, Issue 4)”.

Examining rodents and their offspring, Brenner has showed that rodent postpartum mothers are under severe metabolic stress to their NAD system. Supplementing rodent mothers with NR increases maternal weight loss, advances juvenile development and provides long lasting neurodevelopmental advantages into adulthood. [38] [39] [14]

Brenner is an author of more than 200 peer-reviewed publications. [40] He was the senior editor of the 2004 book, Oncogenomics: Molecular Approaches to Cancer. [41]

Brenner is both cautious and critical of research that promotes claims of anti-aging and longevity. [42] [43] [44] After writing a favorable review of Steven Austad's book Methuselah's Zoo, [45] he reviewed Lifespan: Why We Age – and Why We Don't Have To by David A. Sinclair, summarizing it as "an influential source of misinformation on longevity, featuring counterfactual claims about longevity genes being conserved between yeast and humans, the existence of supposed activators of these genes, and claimed successful age reversal in mice based on partial reprogramming." [46] Brenner published a major review of sirtuins in 2022 entitled "Sirtuins are not conserved longevity genes". [47]

Educational contributions

External videos
Nuvola apps kaboodle.svg “Charles Brenner: ASBMB Award for Exemplary Contributions to Education Lecture”, May 25, 2016.

In 2012, Brenner and Dagmar Ringe developed pre-medical curriculum recommendations that would be consistent with a revised Medical College Admission Test (MCAT), following a request from the President of the American Society for Biochemistry and Molecular Biology, Suzanne Pfeffer. [48] [49] The recommendations, which include development of inorganic, organic and biochemistry coursework that is more geared toward the chemistry of bioorganic functional groups, have been further refined in academic journals. Brenner's contribution to this area was recognized by the 2016 ASBMB Award for Exemplary Contributions to Education. [50]

Industrial collaborations

Brenner is a former member of the Scientific Advisory Board of Sirtris Pharmaceuticals. [51] He was a co-founder of ProHeathspan prior to its acquisition by ChromaDex, and serves as member of the scientific advisory board and chief scientific advisor to ChromaDex. [7] [52]

Awards

Selected publications

Related Research Articles

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide</span> Chemical compound which is reduced and oxidized

Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen), respectively.

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide phosphate</span> Chemical compound

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP+ is the oxidized form. NADP+ is used by all forms of cellular life.

<span class="mw-page-title-main">Sirtuin</span> Enzyme

Sirtuins are a family of signaling proteins involved in metabolic regulation. They are ancient in animal evolution and appear to possess a highly conserved structure throughout all kingdoms of life. Chemically, sirtuins are a class of proteins that possess either mono-ADP-ribosyltransferase or deacylase activity, including deacetylase, desuccinylase, demalonylase, demyristoylase and depalmitoylase activity. The name Sir2 comes from the yeast gene 'silent mating-type information regulation 2', the gene responsible for cellular regulation in yeast.

<span class="mw-page-title-main">ADP-ribosylation</span> Addition of one or more ADP-ribose moieties to a protein.

ADP-ribosylation is the addition of one or more ADP-ribose moieties to a protein. It is a reversible post-translational modification that is involved in many cellular processes, including cell signaling, DNA repair, gene regulation and apoptosis. Improper ADP-ribosylation has been implicated in some forms of cancer. It is also the basis for the toxicity of bacterial compounds such as cholera toxin, diphtheria toxin, and others.

NAD<sup>+</sup> kinase Enzyme

NAD+ kinase (EC 2.7.1.23, NADK) is an enzyme that converts nicotinamide adenine dinucleotide (NAD+) into NADP+ through phosphorylating the NAD+ coenzyme. NADP+ is an essential coenzyme that is reduced to NADPH primarily by the pentose phosphate pathway to provide reducing power in biosynthetic processes such as fatty acid biosynthesis and nucleotide synthesis. The structure of the NADK from the archaean Archaeoglobus fulgidus has been determined.

<span class="mw-page-title-main">FHIT</span> Protein-coding gene in the species Homo sapiens

Bis(5'-adenosyl)-triphosphatase also known as fragile histidine triad protein (FHIT) is an enzyme that in humans is encoded by the FHIT gene.

<span class="mw-page-title-main">Nicotinamide phosphoribosyltransferase</span> Protein-coding gene in the species Homo sapiens

Nicotinamide phosphoribosyltransferase, formerly known as pre-B-cell colony-enhancing factor 1 (PBEF1) or visfatin for its extracellular form (eNAMPT), is an enzyme that in humans is encoded by the NAMPT gene. The intracellular form of this protein (iNAMPT) is the rate-limiting enzyme in the nicotinamide adenine dinucleotide (NAD+) salvage pathway that converts nicotinamide to nicotinamide mononucleotide (NMN) which is responsible for most of the NAD+ formation in mammals. iNAMPT can also catalyze the synthesis of NMN from phosphoribosyl pyrophosphate (PRPP) when ATP is present. eNAMPT has been reported to be a cytokine (PBEF) that activates TLR4, that promotes B cell maturation, and that inhibits neutrophil apoptosis.

<span class="mw-page-title-main">Sirtuin 2</span> Protein-coding gene in the species Homo sapiens

NAD-dependent deacetylase sirtuin 2 is an enzyme that in humans is encoded by the SIRT2 gene. SIRT2 is an NAD+ -dependent deacetylase. Studies of this protein have often been divergent, highlighting the dependence of pleiotropic effects of SIRT2 on cellular context. The natural polyphenol resveratrol is known to exert opposite actions on neural cells according to their normal or cancerous status. Similar to other sirtuin family members, SIRT2 displays a ubiquitous distribution. SIRT2 is expressed in a wide range of tissues and organs and has been detected particularly in metabolically relevant tissues, including the brain, muscle, liver, testes, pancreas, kidney, and adipose tissue of mice. Of note, SIRT2 expression is much higher in the brain than all other organs studied, particularly in the cortex, striatum, hippocampus, and spinal cord.

<span class="mw-page-title-main">NMNAT1</span> Protein-coding gene in the species Homo sapiens

Nicotinamide mononucleotide adenylyltransferase 1 (NMNAT1) is an enzyme that in humans is encoded by the nmnat1 gene. It is a member of the nicotinamide-nucleotide adenylyltransferases (NMNATs) which catalyze nicotinamide adenine dinucleotide (NAD) synthesis.

<span class="mw-page-title-main">NNMT</span> Protein-coding gene in humans

Nicotinamide N-methyltransferase (NNMT) is an enzyme that in humans is encoded by the NNMT gene. NNMT catalyzes the methylation of nicotinamide and similar compounds using the methyl donor S-adenosyl methionine (SAM-e) to produce S-adenosyl-L-homocysteine (SAH) and 1-methylnicotinamide.

<span class="mw-page-title-main">Sirtuin 3</span> Protein-coding gene in the species Homo sapiens

NAD-dependent deacetylase sirtuin-3, mitochondrial also known as SIRT3 is a protein that in humans is encoded by the SIRT3 gene [sirtuin 3 ]. SIRT3 is member of the mammalian sirtuin family of proteins, which are homologs to the yeast Sir2 protein. SIRT3 exhibits NAD+-dependent deacetylase activity.

<span class="mw-page-title-main">NMNAT2</span> Protein-coding gene in the species Homo sapiens

Nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) is an enzyme that in humans is encoded by the NMNAT2 gene.

<span class="mw-page-title-main">ITGB1BP3</span> Protein-coding gene in the species Homo sapiens

Nicotinamide riboside kinase 2 is an enzyme that in humans is encoded by the ITGB1BP3 gene.

<span class="mw-page-title-main">Nicotinamide riboside</span> Chemical compound

Nicotinamide riboside (NR, SR647) is a pyridine-nucleoside and a form of vitamin B3. It functions as a precursor to nicotinamide adenine dinucleotide, or NAD+, through a two-step and a three-step pathway.

<span class="mw-page-title-main">MIR34A</span> Non-coding RNA in the species Homo sapiens

MicroRNA 34a (miR-34a) is a MicroRNA that in humans is encoded by the MIR34A gene.

The Nicotinamide Ribonucleoside (NR) Uptake Permease (PnuC) Family is a family of transmembrane transporters that is part of the TOG superfamily. Close PnuC homologues are found in a wide range of Gram-negative and Gram-positive bacteria, archaea and eukaryotes.

<span class="mw-page-title-main">Nicotinamide mononucleotide</span> Chemical compound

Nicotinamide mononucleotide is a nucleotide derived from ribose, nicotinamide, nicotinamide riboside and niacin. In humans, several enzymes use NMN to generate nicotinamide adenine dinucleotide (NADH). In mice, it has been proposed that NMN is absorbed via the small intestine within 10 minutes of oral uptake and converted to nicotinamide adenine dinucleotide (NAD+) through the Slc12a8 transporter. However, this observation has been challenged, and the matter remains unsettled.

The mitochondrial unfolded protein response (UPRmt) is a cellular stress response related to the mitochondria. The UPRmt results from unfolded or misfolded proteins in mitochondria beyond the capacity of chaperone proteins to handle them. The UPRmt can occur either in the mitochondrial matrix or in the mitochondrial inner membrane. In the UPRmt, the mitochondrion will either upregulate chaperone proteins or invoke proteases to degrade proteins that fail to fold properly. UPRmt causes the sirtuin SIRT3 to activate antioxidant enzymes and mitophagy.

<span class="mw-page-title-main">Mitochondrial theory of ageing</span> Theory of ageing

The mitochondrial theory of ageing has two varieties: free radical and non-free radical. The first is one of the variants of the free radical theory of ageing. It was formulated by J. Miquel and colleagues in 1980 and was developed in the works of Linnane and coworkers (1989). The second was proposed by A. N. Lobachev in 1978.

Nicotinamide mononucleotide adenylyltransferase 3 (NMNAT3) is an enzyme that in humans is encoded by the NMNAT3 gene.

References

  1. 1 2 "Leading Biochemist Charles Brenner, PhD, Joins City of Hope as Chair of First Department Focused on Diabetes and Cancer Metabolism". OncLive. MJH Life Sciences. Aug 27, 2020. Retrieved 3 February 2023.
  2. 1 2 3 4 "Brenner stepping down as chair of Department of Biochemistry | Department of Biochemistry and Molecular Biology". University of Iowa. July 8, 2020. Retrieved 2 February 2023.
  3. 1 2 "Awards for Regev and Gierasch; new job for Brenner". ASBMB Today. July 20, 2020.
  4. 1 2 3 4 Katsyuba, E; Romani, M; Hofer, D; Auwerx, J (January 2020). "NAD(+) homeostasis in health and disease". Nature Metabolism. 2 (1): 9–31. doi:10.1038/s42255-019-0161-5. ISSN   2522-5812. PMID   32694684. S2CID   214277961 . Retrieved 6 February 2023.
  5. ↑ Cercillieux, A; Ciarlo, E; Canto, C (2022-08-02). "Balancing NAD+ deficits with nicotinamide riboside: therapeutic possibilities and limitations". Cellular and Molecular Life Sciences. 79 (8): 463. doi:10.1007/s00018-022-04499-5. ISSN   1420-9071. PMC   9345839 . PMID   35918544.
  6. 1 2 3 4 5 6 Mehmel, M; Jovanović, N; Spitz, U (31 May 2020). "Nicotinamide Riboside-The Current State of Research and Therapeutic Uses". Nutrients. 12 (6): 1616. doi: 10.3390/nu12061616 . PMC   7352172 . PMID   32486488.
  7. 1 2 "ChromaDex To Host Key Opinion Leader Webinar on the Transforming Benefits of Nicotinamide Riboside (NR)". BusinessWire. July 7, 2022. Retrieved 3 February 2023.
  8. ↑ "Vital Signs: Investigator Insight". Dartmouth Medicine Magazine. Vol. 28, no. 4. 2004. Retrieved 2 February 2023.
  9. ↑ "Brenner Named Head of Biochemistry at UI Carver College of Medicine". News-releases.uiowa.edu. May 5, 2009. Archived from the original on July 20, 2011. Retrieved December 9, 2010.
  10. ↑ "CV". Brenner Lab. Retrieved 3 February 2023.
  11. 1 2 3 4 "Curriculum Vitae | Charles Brenner Laboratory". University of Iowa. Retrieved 2 February 2023.
  12. 1 2 "Charles Brenner". Arnold and Mabel Beckman Foundation. Archived from the original on 2 August 2018. Retrieved 1 August 2018.
  13. ↑ "2008 - Dartmouth Medical School - Charles Brenner, PhD". Lung Cancer Research Foundation. Retrieved 6 February 2023.
  14. 1 2 "Humanitarian Grant Awarded for Preclinical Study on the Impact of NAD Precursor Vitamins on Milk Bioactive Production and Brain Development in Rodents". GlobeNewswire News Room. 7 October 2019. Retrieved 6 February 2023.
  15. ↑ "@author Charles Brenner". Grantome. Retrieved 6 February 2023.
  16. ↑ Nakayama, K (1 November 1997). "Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins". The Biochemical Journal. 327 (3): 625–35. doi:10.1042/bj3270625. PMC   1218878 . PMID   9599222 . Retrieved 6 February 2023.
  17. ↑ Sreenivas, S; Krishnaiah, SM; Govindappa, N; Basavaraju, Y; Kanojia, K; Mallikarjun, N; Natarajan, J; Chatterjee, A; Sastry, KN (January 2015). "Enhancement in production of recombinant two-chain Insulin Glargine by over-expression of Kex2 protease in Pichia pastoris" (PDF). Applied Microbiology and Biotechnology. 99 (1): 327–36. doi:10.1007/s00253-014-6052-5. PMID   25239036. S2CID   253777642.
  18. ↑ Herzog, D; Jansen, J; Mißun, M; Diederichs, K; Stengel, F; Marx, A (18 May 2022). "Chemical Proteomics of the Tumor Suppressor Fhit Covalently Bound to the Cofactor Ap(3)A Elucidates Its Inhibitory Action on Translation". Journal of the American Chemical Society. 144 (19): 8613–8623. doi:10.1021/jacs.2c00815. ISSN   0002-7863. PMC   9121386 . PMID   35522782. S2CID   248554359.
  19. ↑ Syeda, F; Fagan, RL; Wean, M; Avvakumov, GV; Walker, JR; Xue, S; Dhe-Paganon S; Brenner, C (2011). "The Replication Focus Targeting Sequence (RFTS) Domain is a DNA-Competitive Inhibitor of Dnmt1". J. Biol. Chem. 286 (17): 15344–15351. doi: 10.1074/jbc.M110.209882 . PMC   3083197 . PMID   21389349.
  20. ↑ Wu, B-K; Brenner, C (2014). "Suppression of TET1-Dependent DNA Demethylation Is Essential for KRAS-Mediated Transformation". Cell Reports. 9 (5): 1827–1840. doi:10.1016/j.celrep.2014.10.063. PMC   4268240 . PMID   25466250.
  21. ↑ Elhassan, YS; Philp, AA; Lavery, GG (1 July 2017). "Targeting NAD+ in Metabolic Disease: New Insights Into an Old Molecule". Journal of the Endocrine Society. 1 (7): 816–835. doi:10.1210/js.2017-00092. PMC   5686634 . PMID   29264533.
  22. ↑ Fletcher RS, Lavery GG (2018). "The emergence of the nicotinamide riboside kinases in the regulation of NAD+ metabolism". Journal of Molecular Endocrinology . 61 (1): R107–R121. doi:10.1530/JME-18-0085. PMC   6145238 . PMID   30307159.
  23. ↑ James Theoga Raj, C; Lin, SJ (October 2019). "Cross-talk in NAD(+) metabolism: insights from Saccharomyces cerevisiae". Current Genetics. 65 (5): 1113–1119. doi:10.1007/s00294-019-00972-0. PMC   6744962 . PMID   30993413.
  24. ↑ Trammell, SAJ; Brenner, C (2013). "Targeted, LCMS-based Metabolomics for Quantitative Measurement of NAD(+) Metabolites". Comput Struct Biotechnol J. 4 (5): e201301012. doi:10.5936/csbj.201301012. PMC   3962138 . PMID   24688693.
  25. ↑ Tempel, W; Rabeh, WM; Bogan, KL; Belenky, P; Wojcik, M; Seidle, HF; Nedyalkova, L; Yang, T; Sauve, AA; Park, HW; Brenner, C (2 October 2007). "Nicotinamide riboside kinase structures reveal new pathways to NAD+". PLOS Biology. 5 (10): e263. doi: 10.1371/journal.pbio.0050263 . ISSN   1545-7885. PMC   1994991 . PMID   17914902.
  26. ↑ Nam, TS; Park, DR; Rah, SY; Woo, TG; Chung, HT; Brenner, C; Kim, UH (September 2020). "Interleukin-8 drives CD38 to form NAADP from NADP(+) and NAAD in the endolysosomes to mobilize Ca(2+) and effect cell migration". FASEB Journal. 34 (9): 12565–12576. doi: 10.1096/fj.202001249R . ISSN   1530-6860. PMID   32717131.
  27. 1 2 Navas, LE; Carnero, A (1 January 2021). "NAD(+) metabolism, stemness, the immune response, and cancer". Signal Transduction and Targeted Therapy. 6 (1): 2. doi:10.1038/s41392-020-00354-w. ISSN   2059-3635. PMC   7775471 . PMID   33384409. S2CID   229935354.
  28. 1 2 3 Diguet, N; Trammell, SAJ; Tannous, C; Deloux, R; Piquereau, J; Mougenot, N; Gouge, A; Gressette, M; Manoury, B; Blanc, J; Breton, M; Decaux, JF; Lavery, GG; Baczkó, I; Zoll, J; Garnier, A; Li, Z; Brenner, C; Mericskay, M (22 May 2018). "Nicotinamide Riboside Preserves Cardiac Function in a Mouse Model of Dilated Cardiomyopathy". Circulation. 137 (21): 2256–2273. doi:10.1161/CIRCULATIONAHA.116.026099. ISSN   1524-4539. PMC   6954688 . PMID   29217642.
  29. 1 2 Fons, NR; Sundaram, RK; Breuer, GA; Peng, S; McLean, RL; Kalathil, AN; Schmidt, MS; Carvalho, DM; Mackay, A; Jones, C; Carcaboso, ÁM; Nazarian, J; Berens, ME; Brenner, C; Bindra, RS (22 August 2019). "PPM1D mutations silence NAPRT gene expression and confer NAMPT inhibitor sensitivity in glioma". Nature Communications. 10 (1): 3790. Bibcode:2019NatCo..10.3790F. doi:10.1038/s41467-019-11732-6. ISSN   2041-1723. PMC   6706443 . PMID   31439867.
  30. 1 2 3 Vaur, P; Brugg, B; Mericskay, M; Li, Z; Schmidt, M S.; Vivien, D; Orset, C; Jacotot, E; Brenner, C (December 2017). "Nicotinamide riboside, a form of vitamin B3, protects against excitotoxicity-induced axonal degeneration". FASEB Journal. 31 (12): 5440–5452. doi:10.1096/fj.201700221RR. ISSN   1530-6860. PMID   28842432.
  31. 1 2 Covarrubias, AJ; Kale, A; Perrone, R; Lopez-Dominguez, JA; Pisco, AO; Kasler, HG; Schmidt, MS; Heckenbach, I; Kwok, R; Wiley, CD; Wong, HS; Gibbs, E; Iyer, SS; Basisty, N; Wu, Q; Kim, IJ; Silva, E; Vitangcol, K; Shin, KO; Lee, YM; Riley, R; Ben-Sahra, I; Ott, M; Schilling, B; Scheibye-Knudsen, M; Ishihara, K; Quake, SR; Newman, J; Brenner, C; Campisi, J; Verdin, E (November 2020). "Senescent cells promote tissue NAD(+) decline during ageing via the activation of CD38(+) macrophages". Nature Metabolism. 2 (11): 1265–1283. doi:10.1038/s42255-020-00305-3. ISSN   2522-5812. PMC   7908681 . PMID   33199924.
  32. 1 2 Pirinen, E; Auranen, M; Khan, NA; Brilhante, V; Urho, N; Pessia, A; Hakkarainen, A; Kuula, J; Heinonen, U; Schmidt, MS; Haimilahti, K; Piirilä, P; Lundbom, N; Taskinen, MR; Brenner, C; Velagapudi, V; Pietiläinen, KH; Suomalainen, A (2 June 2020). "Niacin Cures Systemic NAD(+) Deficiency and Improves Muscle Performance in Adult-Onset Mitochondrial Myopathy". Cell Metabolism. 31 (6): 1078–1090.e5. doi:10.1016/j.cmet.2020.04.008. hdl: 10138/330502 . ISSN   1550-4131. PMID   32386566. S2CID   218585981.
  33. ↑ Lautrup, S; Sinclair, DA; Mattson, MP; Fang, EF (1 October 2019). "NAD(+) in Brain Aging and Neurodegenerative Disorders". Cell Metabolism. 30 (4): 630–655. doi:10.1016/j.cmet.2019.09.001. ISSN   1550-4131. PMC   6787556 . PMID   31577933. S2CID   203653485 . Retrieved 6 February 2023.
  34. ↑ "Manipulating biosynthesis pathways may hold promise for preventing chemotherapy-induced pain | Carver College of Medicine". Carver College of Medicine, The University of Iowa. October 8, 2018. Retrieved 6 February 2023.
  35. ↑ Vitali, L; Merlini, A; Galvagno, F; Proment, A; Sangiolo, D (19 October 2022). "Biological and Exploitable Crossroads for the Immune Response in Cancer and COVID-19". Biomedicines. 10 (10): 2628. doi: 10.3390/biomedicines10102628 . ISSN   2227-9059. PMC   9599827 . PMID   36289890.
  36. ↑ Belenky, P; Racette, FG; Bogan, KL; McClure, JM; Smith, JS; Brenner, C (4 May 2007). "Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+". Cell. 129 (3): 473–84. doi: 10.1016/j.cell.2007.03.024 . PMID   17482543. S2CID   4661723.
  37. ↑ Trammell, SAJ; Weidemann, BJ; Chadda, A; Yorek, MS; Holmes, A; Coppey, LJ; Obrosov, A; Kardon, RH; Yorek, MA; Brenner, C (2016). "Nicotinamide Riboside Opposes Type 2 Diabetes and Neuropathy in Mice". Scientific Reports. 6: 26933. Bibcode:2016NatSR...626933T. doi:10.1038/srep26933. PMC   4882590 . PMID   27230286.
  38. ↑ Ear, PH; Chadda, A; Gumusoglu, SB; Schmidt, MS; Vogeler, S; Malicoat, J; Kadel, J; Moore, MM; Migaud, ME; Stevens, HE; Brenner, C (22 January 2019). "Maternal Nicotinamide Riboside Enhances Postpartum Weight Loss, Juvenile Offspring Development, and Neurogenesis of Adult Offspring". Cell Reports. 26 (4): 969–983.e4. doi: 10.1016/j.celrep.2019.01.007 . ISSN   2211-1247. PMID   30673618.
  39. ↑ "Supplement makes (mouse) moms' milk better; pups benefit for life". medicalxpress.com. Retrieved 2019-01-26..
  40. ↑ "Charles Brenner". scholar.google.com. Retrieved 3 February 2023.
  41. ↑ Brenner, Charles; Duggan, David, eds. (2004). Oncogenomics: Molecular approaches to cancer. Hoboken, N.J.: Wiley-Liss. ISBN   0-471-22592-4.
  42. ↑ Ritchie, Stuart (24 January 2023). "Why you shouldn't get too excited at claims scientists have reversed ageing... yet". inews.co.uk. Retrieved 3 February 2023.
  43. ↑ Colbert, Chris (13 May 2022). "Unpacking Longevity: The Myths of Anti-Aging". Private Medical. Retrieved 2 February 2023.
  44. ↑ Garth, Eleanor (2 November 2022). "Charles Brenner: longevity is not a simple engineering problem". Longevity.Technology - Latest News, Opinions, Analysis and Research. Retrieved 3 February 2023.
  45. ↑ Brenner, C (12 August 2022). "Longevity lessons Methuselah's Zoo: What Nature Can Teach Us About Living Longer, Healthier Lives Steven N. Austad MIT Press, 2022. 320 pp". Science. 377 (6607): 718. doi:10.1126/science.add9130. ISSN   0036-8075. PMID   35951694. S2CID   251516708.
  46. ↑ Brenner, C (January 2023). "A science-based review of the world's best-selling book on aging". Archives of Gerontology and Geriatrics. 104: 104825. doi:10.1016/j.archger.2022.104825. ISSN   0167-4943. PMC   9669175 . PMID   36183524.
  47. ↑ Brenner, C (2022-09-22). "Sirtuins are not conserved longevity genes". Life Metabolism (2): 122–133. doi: 10.1093/lifemeta/loac025 . ISSN   2755-0230. PMC   10081735 . PMID   37035412.
  48. ↑ Brenner, Charles; Ringe, Dagmar (2012). "Response to the New MCAT: ASBMB Premedical Curriculum Recommendations" (PDF). ASBMB Today. No. March. pp. 12–14.
  49. ↑ Chemical Sciences, Roundtable; Board on Chemical Sciences and Technology; Division on Earth and Life Studies; National Research Council (24 March 2014). "Chapter 1: Introduction and Overview". Undergraduate Chemistry Education: A Workshop Summary. Washington, D.C.: National Academies Press. p. 1. doi:10.17226/18555. ISBN   978-0-309-29589-5. PMID   24830064.
  50. 1 2 Sengupta, Samarpita (March 1, 2016). "Brenner recognized for devotion to 'cutting-edge education' and serving the biomedical community". ASBMB Today. Retrieved 2 February 2023.
  51. ↑ "Sirtris Pharmaceuticals, Inc. offering of common stock, Filed Pursuant to Rule 424(b)(4) Registration No.: 333-140979". www.sec.gov. May 22, 2007. Retrieved 2 February 2023.
  52. ↑ "Charles Brenner Ph.D." Bloomberg. Retrieved 1 August 2018.
  53. ↑ "ChromaDex Chief Scientific Advisor Dr. Charles Brenner Receives 2020 National Scientific Achievement Award from the American Society for Nutrition". BusinessWire. May 21, 2020.
  54. ↑ "AAAS Members Elected as Fellows". American Association for the Advancement of Science (AAAS). 30 November 2012. Retrieved 2 February 2023.
  55. ↑ "William E. M. Lands Lectureship | Biological Chemistry | Michigan Medicine". Biological Chemistry. 22 March 2018. Retrieved 2 February 2023.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.