Repairing Mitochondrial Dysfunction in Disease

Adipocyte NCoR Knockout Decreases PPARγ Phosphorylation and Enhances PPARγ Activity and Insulin Sensitivity

Li, P., Fan, W., Xu, J., Lu, M. M., Yamamoto, H., Auwerx, J. H., Sears, D. D., Talukdar, S., Oh, D., Chen, A., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.050 · Cited by 264

Increased ceramide in brains with Alzheimer's and other neurodegenerative diseases

Filippov, V., Song, M. A., Zhang, K., Vinters, H. V., Tung, S., Kirsch, W. M., Yang, J., & Duerksen-Hughes, P. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111202 · Cited by 264

The Retinoblastoma-Histone Deacetylase 3 Complex Inhibits PPARγ and Adipocyte Differentiation

Lluis Fajas, A., Egler, V., Reiter, R. J., Hansen, J. B., Kristiansen, K., Debril, M.-B., Miard, S., & Auwerx, J. H. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00360-x · Cited by 258

NAD + repletion improves muscle function in muscular dystrophy and counters global PARylation

Ryu, D., Zhang, H., Ropelle, E. R., Sorrentino, V., Mázala, D. A. G., Mouchiroud, L., Marshall, P. L., Campbell, M. D., Ali, A. S., Knowels, G. M., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf5504 · Cited by 256

Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle

Pirinen, E., Cantó, C., Jo, Y. S., Morato, L., Zhang, H., Menzies, K. J., Williams, E. G., Mouchiroud, L., Moullan, N., Hagberg, C., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.002 · Cited by 254

The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet‐induced obesity

Barbosa, M. T., Soares, S. M., Novak, C. M., Sinclair, D. A., Levine, J. A., Aksoy, P., & Chini, E. N. (2007) · The FASEB Journal · doi:10.1096/fj.07-8290com · Cited by 252

Sirt4 accelerates Ang II-induced pathological cardiac hypertrophy by inhibiting manganese superoxide dismutase activity

Luo, Y., Tang, X., An, X., Xie, X., Chen, X., Zhao, X., Hao, D., Chen, H., & Liu, D. (2016) · European Heart Journal · doi:10.1093/eurheartj/ehw138 · Cited by 250

VCP Is Essential for Mitochondrial Quality Control by PINK1/Parkin and this Function Is Impaired by VCP Mutations

Kim, N. C., Tresse, E., Kolaitis, R., Molliex, A., Thomas, R. E., Alami, N. H., Wang, B., Joshi, A., Smith, R. B., Ritson, G. P., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.029 · Cited by 248

Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes

Cantó, C., Sauve, A. A., & Bai, P. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.004 · Cited by 246

Deacetylase Inhibitors Increase Muscle Cell Size by Promoting Myoblast Recruitment and Fusion through Induction of Follistatin

Iezzi, S., Padova, M. D., Serra, C., Caretti, G., Simone, C., Maklan, E., Minetti, G., Zhao, P., Hoffman, E. P., Puri, P., et al. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00107-8 · Cited by 245

Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA- and ROS-dependent pathway

Liot, G., Bossy, B., Lubitz, S., Kushnareva, Y., Sejbuk, N. E., & Bossy‐Wetzel, E. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.22 · Cited by 244

Multilayered Genetic and Omics Dissection of Mitochondrial Activity in a Mouse Reference Population

Wu, Y., Williams, E. G., Dubuis, S., Mottis, A., Jovaisaite, V., Houten, S. M., Argmann, C. A., Faridi, P., Wolski, W., Kutalik, Z., et al. (2014) · Cell · doi:10.1016/j.cell.2014.07.039 · Cited by 244

Neuroendocrine Coordination of Mitochondrial Stress Signaling and Proteostasis

Berendzen, K. M., Durieux, J., Shao, L.-W., Tian, Y., Kim, H.-E., Wolff, S., Liu, Y., & Dillin, A. G. (2016) · Cell · doi:10.1016/j.cell.2016.08.042 · Cited by 244

P7C3 Neuroprotective Chemicals Function by Activating the Rate-Limiting Enzyme in NAD Salvage

Wang, G., Han, T., Nijhawan, D., Theodoropoulos, P., Naidoo, J., Yadavalli, S., Mirzaei, H., Pieper, A. A., Ready, J. M., & McKnight, S. L. (2014) · Cell · doi:10.1016/j.cell.2014.07.040 · Cited by 243

Rapamycin ameliorates age-dependent obesity associated with increased mTOR signaling in hypothalamic POMC neurons

Yang, S.-B., Tien, A.-C., Boddupalli, G., Xu, A. W., Jan, Y. N., & Jan, L. Y. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.043 · Cited by 242

A Randomized, Controlled Trial of Doxycycline and Rifampin for Patients with Alzheimer's Disease

Loeb, M. B., Molloy, D. W., Smieja, M., Standish, T., Goldsmith, C. H., Mahony, J. B., Smith, S. R., BORRIE, M. J., Decoteau, E., Davidson, W., et al. (2004) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.2004.52109.x · Cited by 241

The mitochondrial protein BNIP3L is the substrate of PARK2 and mediates mitophagy in PINK1/PARK2 pathway

Gao, F., Dong, C., Si, J., Hu, Q., Qin, Z., Fang, M., & Wang, G. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv017 · Cited by 239

Suppression of oxidative metabolism and mitochondrial biogenesis by the transcriptional corepressor RIP140 in mouse adipocytes

Powelka, A. M. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26040 · Cited by 236

Reversal of Hypertriglyceridemia, Fatty Liver Disease, and Insulin Resistance by a Liver-Targeted Mitochondrial Uncoupler

Perry, R. J., Kim, T.-H., Zhang, X., Lee, H., Pesta, D. H., Popov, V., Zhang, D., Rahimi, Y., Jurczak, M. J., Cline, G. W., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.10.004 · Cited by 230

PARP-1 involvement in neurodegeneration: A focus on Alzheimer’s and Parkinson’s diseases

Martire, S., Mosca, L., & D’Erme, M. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.04.001 · Cited by 228

AMPK Activation Stimulates Autophagy and Ameliorates Muscular Dystrophy in the mdx Mouse Diaphragm

Pauly, M., Daussin, F., Burelle, Y., Li, T., Godin, R., Fauconnier, J., Koechlin-Ramonatxo, C., Hugon, G., Lacampagne, A., Coisy-Quivy, M., et al. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.04.004 · Cited by 225

TRPV1 Pain Receptors Regulate Longevity and Metabolism by Neuropeptide Signaling

Riera, C. E., Huising, M. O., Follett, P., Leblanc, M., Halloran, J. J., Andel, R. V., Filho, C. D. D. M., Merkwirth, C., & Dillin, A. G. (2014) · Cell · doi:10.1016/j.cell.2014.03.051 · Cited by 223

Mitochondrial fragmentation and superoxide anion production in coronary endothelial cells from a mouse model of type 1 diabetes

Makino, A., Scott, B. T., & Dillmann, W. H. (2010) · Diabetologia · doi:10.1007/s00125-010-1770-4 · Cited by 223

Tissue-Specific Loss of DARS2 Activates Stress Responses Independently of Respiratory Chain Deficiency in the Heart

Doğan, Ş. A., Pujol, C., Maiti, P., Kukat, A., Wang, S., Hermans, S., Senft, K., Wibom, R., Rugarli, E. I., & Trifunović, A. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.02.004 · Cited by 222

Lipid Biosynthesis Coordinates a Mitochondrial-to-Cytosolic Stress Response

Kim, H.-E., Grant, A. R., Simic, M., Kohnz, R. A., Nomura, D. K., Durieux, J., Riera, C. E., Sanchez, M., Kapernick, E. A., Wolff, S., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.027 · Cited by 222

A Role for Peroxisome Proliferator-Activated Receptor γ Coactivator-1 in the Control of Mitochondrial Dynamics During Postnatal Cardiac Growth

Martin, O. J., Lai, L., Soundarapandian, M. M., Leone, T. C., Antonio Zorzano, A., Keller, M. P., Attie, A., Muoio, D. M., & Kelly, D. P. (2013) · Circulation Research · doi:10.1161/circresaha.114.302562 · Cited by 218

A small natural molecule promotes mitochondrial fusion through inhibition of the deubiquitinase USP30

Yue, W., Chen, Z., Liu, H., Chen, Y., Chen, M., Feng, D., Yan, C., Wu, H., Du, L., Wang, Y., et al. (2014) · Cell Research · doi:10.1038/cr.2014.20 · Cited by 218

Metabolic networks of longevity

Houtkooper, R. H., Williams, R. W., & Auwerx, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.029 · Cited by 217

Nicotinamide mononucleotide protects against β-amyloid oligomer-induced cognitive impairment and neuronal death

Wang, X., Hu, X., Yang, Y., Takata, T., & Sakurai, T. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.060 · Cited by 217

The Chop Gene Contains an Element for the Positive Regulation of the Mitochondrial Unfolded Protein Response

Horibe, T., & Hoogenraad, N. J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000835 · Cited by 215

Chemical Inducers of Autophagy That Enhance the Clearance of Mutant Proteins in Neurodegenerative Diseases

Renna, M., Jiménez-Sánchez, M., Sarkar, S., & Rubinsztein, D. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.072181 · Cited by 215

A PGC1α-mediated transcriptional axis suppresses melanoma metastasis

Luo, C., Lim, J.-H., Lee, Y., Granter, S. R., Thomas, A., Vázquez, F., Widlund, H. R., & Puigserver, P. (2016) · Nature · doi:10.1038/nature19347 · Cited by 213

Estrogen receptor mediates a distinct mitochondrial unfolded protein response

Papa, L., & Germain, D. (2011) · Journal of Cell Science · doi:10.1242/jcs.078220 · Cited by 212

Iron-starvation-induced mitophagy mediates lifespan extension upon mitochondrial stress in C.elegans

Schiavi, A., Maglioni, S., Palikaras, K., Shaik, A., Strappazzon, F., Brinkmann, V., Torgovnick, A., Castelein, N., De Henau, S., Braeckman, B. P., et al. (2015) · Current Biology · doi:10.1016/j.cub.2015.05.059 · Cited by 209

Shared Mechanisms of Neurodegeneration in Alzheimer’s Disease and Parkinson’s Disease

Xie, A., Gao, J., Xu, L., & Meng, D.-M. (2014) · BioMed Research International · doi:10.1155/2014/648740 · Cited by 204

Induction of Mitochondrial Biogenesis Is a Maladaptive Mechanism in Mitochondrial Cardiomyopathies

Sebastiani, M., Giordano, C., Nediani, C., Travaglini, C., Borchi, E., Zani, M., Feccia, M. A., Mancini, M., Petrozza, V., Cossarizza, A., et al. (2007) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2007.06.035 · Cited by 200

Regulation of PPARγ coactivator 1α (PGC-1α) signaling by an estrogen-related receptor α (ERRα) ligand

Willy, P. J., Murray, I., Qian, J., Busch, B. B., Stevens, W. C., Martin, R., Mohan, R., Zhou, S., Ordentlich, P., Wei, P. Y., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401420101 · Cited by 200

Rb and p107 regulate preadipocyte differentiation into white versus brown fat through repression of PGC-1α

Scimè, A., Grenier, G., Huh, M. S., Gillespie, M. A., Bevilacqua, L., Harper, M.-E., & Rudnicki, M. A. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.002 · Cited by 199

Effect of nicotinamide mononucleotide on brain mitochondrial respiratory deficits in an Alzheimer’s disease-relevant murine model

Long, A., Owens, K., Schlappal, A. E., Kristián, T., Fishman, P. S., & Schuh, R. A. (2015) · BMC Neurology · doi:10.1186/s12883-015-0272-x · Cited by 199

PPARδ Promotes Running Endurance by Preserving Glucose

Fan, W., Waizenegger, W., Lin, C. S., Sorrentino, V., He, M.-X., Wall, C. E., Li, H., Liddle, C., Yu, R. T., Atkins, A. R., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.04.006 · Cited by 198

Thiazolidinedione safety

Kung, J., & Henry, R. R. (2012) · Expert Opinion on Drug Safety · doi:10.1517/14740338.2012.691963 · Cited by 198

The Transcriptional Corepressor RIP140 Regulates Oxidative Metabolism in Skeletal Muscle

Seth, A., Steel, J. H., Nichol, D., Pocock, V., Kumaran, M. K., Fritah, A., Mobberley, M. A., Ryder, T. A., Rowlerson, A. M., Scott, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.004 · Cited by 196

Amyloid-β Peptide Induces Mitochondrial Dysfunction by Inhibition of Preprotein Maturation

Mossmann, D., Vögtle, F. ‐., Taşkin, A. A., Teixeira, P. F., Ring, J., Burkhart, J. M., Burger, N., Pinho, C. M., Tadić, J., Loreth, D., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.07.024 · Cited by 196

Mitochondrial iron metabolism and its role in neurodegeneration

Horowitz, M. P., & Greenamyre, J. T. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100354 · Cited by 195

Estrogen-related Receptor γ Is a Key Regulator of Muscle Mitochondrial Activity and Oxidative Capacity

Rangwala, S. M., Wang, X., Calvo, J. A., Lindsley, L., Zhang, Y., Deyneko, G., Beaulieu, V., Gao, J., Turner, G. M., & Markovits, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125401 · Cited by 195

The nuclear receptor co-repressor Nrip1 (RIP140) is essential for female fertility

White, R., Leonardsson, G., Rosewell, I. R., Jacobs, M. A., Milligan, S. R., & Parker, M. G. (2000) · Nature Medicine · doi:10.1038/82183 · Cited by 193

Exercise and PGC-1α-Independent Synchronization of Type I Muscle Metabolism and Vasculature by ERRγ

Narkar, V. A., Fan, W., Downes, M., Yu, R. T., Jonker, J. W., Alaynick, W. A., Banayo, E., Karunasiri, M. S., Lorca, S., & Evans, R. M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.019 · Cited by 192

Exercise Mimetics: Impact on Health and Performance

Fan, W., & Evans, R. M. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.10.022 · Cited by 188

A Systems Approach for Decoding Mitochondrial Retrograde Signaling Pathways

Chae, S., Ahn, B. Y., Byun, K., Cho, Y. M., Yu, M., Lee, B., Hwang, D., & Park, K. S. (2013) · Science Signaling · doi:10.1126/scisignal.2003266 · Cited by 185

Resveratrol and Alzheimer’s Disease: Mechanistic Insights

Ahmed, T., Javed, S., Javed, S., Tariq, A., Šamec, D., Tejada, S., Nabavi, S. F., Braidy, N., & Nabavi, S. M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9839-9 · Cited by 183

Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane

Nakamura, N., & Hirose, S. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-11-1103 · Cited by 181

Mechanism of increases in l -kynurenine and quinolinic acid in renal insufficiency

Saito, K., Fujigaki, S., Heyes, M. P., Shibata, K., Takemura, M., Fujii, H., Wada, H., Noma, A., & Seishima, M. (2000) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2000.279.3.f565 · Cited by 181

Tissue-Specific Remodeling of the Mitochondrial Proteome in Type 1 Diabetic Akita Mice

Bugger, H., Chen, D., Riehle, C., Soto, J., Theobald, H. A., Hu, X. X., Ganesan, B., Weimer, B. C., & Abel, E. D. (2009) · Diabetes · doi:10.2337/db09-0259 · Cited by 180

The journey of resveratrol from yeast to human

Timmers, S., Auwerx, J. H., & Schrauwen, P. (2012) · Aging · doi:10.18632/aging.100445 · Cited by 180

Novel Therapies Targeting Inner Mitochondrial Membrane—From Discovery to Clinical Development

Szeto, H. H., & Schiller, P. W. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0476-8 · Cited by 175

Role of mitochondrial homeostasis and dynamics in Alzheimer's disease

Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175

Chronic AMPK activation evokes the slow, oxidative myogenic program and triggers beneficial adaptations in mdx mouse skeletal muscle

Ljubicic, V., Miura, P., Burt, M., Boudreault, L., Khogali, S. E. O., Lunde, J. A., Renaud, J.-M., & Jasmin, B. J. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr265 · Cited by 171

ADP ribosyl cyclase activity of a novel bone marrow stromal cell surface molecule, BST‐1

Hirata, Y., Kimura, N., Sato, K., Ohsugi, Y., Takasawa, S., Okamoto, H., Ishikawa, J., Kaisho, T., Ishihara, K., & Hirano, T. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01279-2 · Cited by 168

PARP inhibition protects against alcoholic and non-alcoholic steatohepatitis

Mukhopadhyay, P., Horváth, B., Rajesh, M., Varga, Z. V., Gariani, K., Ryu, D., Cao, Z., Holovac, E., Park, O., Zhou, Z., et al. (2016) · Journal of Hepatology · doi:10.1016/j.jhep.2016.10.023 · Cited by 168

Inhibiting poly ADP-ribosylation increases fatty acid oxidation and protects against fatty liver disease

Gariani, K., Ryu, D., Menzies, K. J., Yi, H.-S., Stein, S., Zhang, H., Perino, A., Lemos, V., Katsyuba, E., Jha, P., et al. (2017) · Journal of Hepatology · doi:10.1016/j.jhep.2016.08.024 · Cited by 167

Mitochondrial fission is required for cardiomyocyte hypertrophy via a Ca2+-calcineurin signalling pathway

Pennanen, C., Parra, V., López‐Crisosto, C., Morales, P. E., del Campo, A., Gutiérrez, T., Rivera-Mejías, P., Kuzmicic, J., Chiong, M., Antonio Zorzano, A., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.139394 · Cited by 166

Clioquinol promotes the degradation of metal-dependent amyloid-β (Aβ) oligomers to restore endocytosis and ameliorate Aβ toxicity

Matlack, K. E. S., Tardiff, D. F., Narayan, P. S., Hamamichi, S., Caldwell, K. A., Caldwell, G. A., & Lindquist, S. L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402228111 · Cited by 166

A Small Molecule Promotes Mitochondrial Fusion in Mammalian Cells

Wang, D., Wang, J., Bonamy, G. M. C., Meeusen, S., Brusch, R. G., Turk, C. N., Yang, P., & Schultz, P. G. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201204589 · Cited by 165

Circadian Amplitude Regulation via FBXW7-Targeted REV-ERBα Degradation

Zhao, X., Hirota, T., Han, X., Cho, H., Chong, L.-W., Lamia, K. A., Liu, S., Atkins, A. R., Banayo, E., Liddle, C., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.012 · Cited by 162

Neuropeptide signals cell non-autonomous mitochondrial unfolded protein response

Shao, L.-W., Niu, R., & Liu, Y. (2016) · Cell Research · doi:10.1038/cr.2016.118 · Cited by 161

TGR5 and Immunometabolism: Insights from Physiology and Pharmacology

Perino, A., & Schoonjans, K. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.002 · Cited by 157

Exploiting the mitochondrial unfolded protein response for cancer therapy in mice and human cells

Siegelin, M. D., Dohi, T., Raskett, C. M., Orlowski, G. M., Powers, C. M., Gilbert, C. A., Ross, A. H., Plescia, J., & Altieri, D. C. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44855 · Cited by 157

Mitochondrial iron homeostasis and its dysfunctions in neurodegenerative disorders

Mena, N. P., Urrutia, P. J., Lourido, F., Carrasco, C. M., & Núñez, M. T. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.02.001 · Cited by 154

Transgenic Mouse Model of Ventricular Preexcitation and Atrioventricular Reentrant Tachycardia Induced by an AMP-Activated Protein Kinase Loss-of-Function Mutation Responsible for Wolff-Parkinson-White Syndrome

Sidhu, J. S., Rajawat, Y. S., Rami, T. G., Gollob, M. H., Wang, Z., Yuan, R., Marian, A. J., DeMayo, F. J., Weilbaecher, D., Taffet, G. E., et al. (2004) · Circulation · doi:10.1161/01.cir.0000151291.32974.d5 · Cited by 145

Joint mouse–human phenome-wide association to test gene function and disease risk

Wang, X., Pandey, A. K., Mulligan, M. K., Williams, E. G., Mozhui, K., Li, Z., Jovaisaite, V., Quarles, L. D., Xiao, Z., Huang, J., et al. (2016) · Nature Communications · doi:10.1038/ncomms10464 · Cited by 145

Identification of Diaryl Ether-Based Ligands for Estrogen-Related Receptor α as Potential Antidiabetic Agents

Patch, R. J., Searle, L. L., Kim, A. J., De, D., Zhu, X., Askari, H. B., O’Neill, J. C., Abad, M. C., Rentzeperis, D., Liu, J., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101063h · Cited by 141

Pharmacokinetics and tolerability of SRT 2104, a first‐in‐class small molecule activator of SIRT 1, after single and repeated oral administration in man

Hoffmann, E. C., Wald, J., Lavu, S., Roberts, J., Beaumont, C., Haddad, J., Elliott, P. J., Westphal, C. H., & Jacobson, E. W. (2012) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2012.04340.x · Cited by 139

MARF and Opa1 Control Mitochondrial and Cardiac Function in Drosophila

Dorn, G. W., Clark, C. F., Eschenbacher, W. H., Kang, M., Engelhard, J. T., Warner, S. J., Matkovich, S. J., & Jowdy, C. C. (2010) · Circulation Research · doi:10.1161/circresaha.110.236745 · Cited by 139

Evidence for Mitochondrial UPR Gene Activation in Familial and Sporadic Alzheimer's Disease

Beck, J. S., Mufson, E. J., & Counts, S. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666151221145445 · Cited by 139

Discovery, synthesis, and biological evaluation of thiazoloquin(az)olin(on)es as potent CD38 inhibitors

Haffner, C. D., Becherer, J. D., Boros, E. E., Cadilla, R., Carpenter, T., Cowan, D., Deaton, D. N., Guo, Y., Harrington, W., Henke, B. R., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm502009h · Cited by 137

Nicotinamide improves glucose metabolism and affects the hepatic NAD-sirtuin pathway in a rodent model of obesity and type 2 diabetes

Yang, S. J., Choi, J. M., Kim, L., Park, S. E., Rhee, E., Lee, W., Oh, K. W., Park, S. W., & Park, C.-Y. (2013) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2013.09.004 · Cited by 135

A pilot randomized, placebo controlled, double blind phase I trial of the novel SIRT1 activator SRT2104 in elderly volunteers

Libri, V., Brown, A. P., Gambarota, G., Haddad, J., Shields, G. S., Dawes, H., Pinato, D. J., Hoffman, E., Elliot, P. J., Vlasuk, G. P., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051395 · Cited by 135

Astrocyte‐Derived Nitric Oxide Causes Both Reversible and Irreversible Damage to the Neuronal Mitochondrial Respiratory Chain

Stewart, V. C., Sharpe, M. A., Clark, J. B., & Heales, S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750694.x · Cited by 133

Mechanism of Action of Compound-13: An α1-Selective Small Molecule Activator of AMPK

Hunter, R. W., Foretz, M., Bultot, L., Fullerton, M. D., Deák, M., Ross, F. A., Hawley, S. A., Shpiro, N., Viollet, B., Barron, D., et al. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.05.014 · Cited by 132

The mitochondrial unfolded protein response–synchronizing genomes

Jovaisaite, V., & Auwerx, J. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.12.003 · Cited by 131

Nicotinamide enhances mitochondria quality through autophagy activation in human cells

Kang, H. T., & Hwang, E. S. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00487.x · Cited by 128

Long-Term Follow-Up of Bezafibrate Treatment in Patients With the Myopathic Form of Carnitine Palmitoyltransferase 2 Deficiency

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Mitochondrial SSBP1 protects cells from proteotoxic stresses by potentiating stress-induced HSF1 transcriptional activity

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