Regulation of pgc-1α, a nodal regulator of mitochondrial biogenesis

Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1

Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139 · see citing works

A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis

Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works

AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works

Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works

Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres

Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · see citing works

AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α

Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491 · see citing works

ATP-citrate lyase links cellular metabolism to histone acetylation

Wellen, K. E., Hatzivassiliou, G., Sachdeva, U. M., Bui, T. V., Cross, J. R., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1164097 · Cited by 2,298 · see citing works

The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · see citing works

Nuclear Receptors and Lipid Physiology: Opening the X-Files

Chawla, A., Repa, J. J., Evans, R. M., & Mangelsdorf, D. J. (2001) · Science · doi:10.1126/science.294.5548.1866 · Cited by 2,085 · see citing works

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 1,918 · see citing works

Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1

Yoon, J. C., Puigserver, P., Chen, G., Donovan, J., Wu, Z., Rhee, J., Adelmant, G., Stafford, J., Kahn, C. R., Granner, D. K., et al. (2001) · Nature · doi:10.1038/35093050 · Cited by 1,821 · see citing works

PGC-1α, SIRT1 and AMPK, an energy sensing network that controls energy expenditure

Cantó, C., & Auwerx, J. (2009) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e328328d0a4 · Cited by 1,624 · see citing works

Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction

Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487 · see citing works

CREB regulates hepatic gluconeogenesis through the coactivator PGC-1

Herzig, S., Long, F., Jhala, U. S., Hedrick, S., Quinn, R., Bauer, A., Rudolph, D., Schutz, G., Yoon, C., Puigserver, P., et al. (2001) · Nature · doi:10.1038/35093131 · Cited by 1,440 · see citing works

Sir2 mediates longevity in the fly through a pathway related to calorie restriction

Rogina, B., & Helfand, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404184101 · Cited by 1,361 · see citing works

Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α

Gerhart‐Hines, Z., Rodgers, J. T., Bare, O., Lerin, C., Kim, S., Mostoslavsky, R., Alt, F. W., Wu, Z., & Puigserver, P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601633 · Cited by 1,294 · see citing works

Mitochondrial biogenesis in mammals: the role of endogenous nitric oxide

Nisoli, E., Clementi, E., Paolucci, C., Cozzi, V., Tonello, C., Sciorati, C., Bracale, R., Valerio, A., Francolini, M., Moncada, S., et al. (2003) · Science · doi:10.1126/science.1079368 · Cited by 1,243 · see citing works

The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor α in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes

Vega, R. B., Huss, J. M., & Kelly, D. P. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1868-1876.2000 · Cited by 1,195 · see citing works

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 · see citing works

Glucose Restriction Inhibits Skeletal Myoblast Differentiation by Activating SIRT1 through AMPK-Mediated Regulation of Nampt

Fulco, M., Cen, Y., Zhao, P., Hoffman, E. P., McBurney, M. W., Sauve, A. A., & Sartorelli, V. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.02.004 · Cited by 821 · see citing works

Cytokine Stimulation of Energy Expenditure through p38 MAP Kinase Activation of PPARγ Coactivator-1

Puigserver, P., Rhee, J., Lin, J., Wu, Z., Yoon, J. C., Zhang, C.-Y., Krauss, S., Mootha, V. K., Lowell, B. B., & Spiegelman, B. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00390-2 · Cited by 732 · see citing works

An autoregulatory loop controls peroxisome proliferator-activated receptor γ coactivator 1α expression in muscle

Handschin, C., Rhee, J., Lin, J., Tarr, P. T., & Spiegelman, B. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1232352100 · Cited by 729 · see citing works

Exercise Stimulates Pgc-1α Transcription in Skeletal Muscle through Activation of the p38 MAPK Pathway

Akimoto, T., Pohnert, S. C., Li, P., Zhang, M., Gumbs, C., Rosenberg, P. B., Williams, R. S., & Yan, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408862200 · Cited by 714 · see citing works

Regulation of mitochondrial biogenesis in skeletal muscle by CaMK

Wu, H., Kanatous, S. B., Thurmond, F. A., Gallardo, T., Isotani, E., Bassel-Duby, R., & Williams, R. S. (2002) · Science · doi:10.1126/science.1071163 · Cited by 684 · see citing works

Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1

Michael, L. F., Wu, Z., Cheatham, R. B., Puigserver, P., Adelmant, G., Lehman, J. J., Kelly, D. P., & Spiegelman, B. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061035098 · Cited by 663 · see citing works

Nuclear Receptors and the Control of Metabolism

Francis, G. A., Fayard, E., Picard, F., & Auwerx, J. H. (2003) · Annual Review of Physiology · doi:10.1146/annurev.physiol.65.092101.142528 · Cited by 632 · see citing works

p38 Mitogen-Activated Protein Kinase Is the Central Regulator of Cyclic AMP-Dependent Transcription of the Brown Fat Uncoupling Protein 1 Gene

Cao, W., Daniel, K. W., Robidoux, J., Puigserver, P., Medvedev, A. V., Bai, X., Floering, L. M., Spiegelman, B. M., & Collins, S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.3057-3067.2004 · Cited by 605 · see citing works

Non-CpG methylation of the PGC-1α promoter through DNMT3B controls mitochondrial density.

Barrès, R., Osler, M. E., Yan, J., Rune, A., Fritz, T., Caidahl, K., Krook, A., & Zierath, J. R. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.07.011 · Cited by 602 · see citing works

Activation of PPARγ Coactivator-1 Through Transcription Factor Docking

Puigserver, P., Adelmant, G., Wu, Z., Fan, M., Xu, J., O’Malley, B. W., & Spiegelman, B. M. (1999) · Science · doi:10.1126/science.286.5443.1368 · Cited by 596 · see citing works

Regulation of hepatic fasting response by PPARγ coactivator-1α (PGC-1): Requirement for hepatocyte nuclear factor 4α in gluconeogenesis

Rhee, J., Inoue, Y., Yoon, J. C., Puigserver, P., Fan, M., Gonzalez, F. J., & Spiegelman, B. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0730870100 · Cited by 564 · see citing works

Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1

Rodgers, J. T., & Puigserver, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702509104 · Cited by 549 · see citing works

Mitochondrial biogenesis by NO yields functionally active mitochondria in mammals

Nisoli, E., Falcone, S., Tonello, C., Cozzi, V., Palomba, L., Fiorani, M., Pisconti, A., Brunelli, S., Cardile, A., Francolini, M., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405432101 · Cited by 495 · see citing works

Akt/PKB regulates hepatic metabolism by directly inhibiting PGC-1α transcription coactivator

Li, X., Monks, B., Ge, Q., & Birnbaum, M. J. (2007) · Nature · doi:10.1038/nature05861 · Cited by 487 · see citing works

Peroxisome Proliferator-activated Receptor Coactivator-1α (PGC-1α) Coactivates the Cardiac-enriched Nuclear Receptors Estrogen-related Receptor-α and -γ

Huss, J. M., Kopp, R. P., & Kelly, D. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206324200 · Cited by 480 · see citing works

Regulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complex

Kajimura, S., Seale, P., Tomaru, T., Erdjument-Bromage, H., Cooper, M. P., Ruas, J. L., Chin, S., Tempst, P., Lazar, M. A., & Spiegelman, B. M. (2008) · Genes & Development · doi:10.1101/gad.1666108 · Cited by 468 · see citing works

GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1α

Lerin, C., Rodgers, J. T., Kalume, D. E., Kim, S.-H., Pandey, A., & Puigserver, P. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.013 · Cited by 443 · see citing works

Regulation of the MEF2 Family of Transcription Factors by p38

Zhao, M. F., New, L., Kravchenko, V. V., Kato, Y., Gram, H., Padova, F. D., Olson, E. N., Ulevitch, R. J., & Han, J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.21 · Cited by 438 · see citing works

Biological control through regulated transcriptional coactivators

Spiegelman, B. M., & Heinrich, R. (2004) · Cell · doi:10.1016/j.cell.2004.09.037 · Cited by 377 · see citing works

Suppression of mitochondrial respiration through recruitment of p160 myb binding protein to PGC-1α: modulation by p38 MAPK

Fan, M., Rhee, J., St-Pierre, J., Handschin, C., Puigserver, P., Lin, J., Jäeger, S., Erdjument-Bromage, H., Tempst, P., & Spiegelman, B. M. (2004) · Genes & Development · doi:10.1101/gad.1152204 · Cited by 309 · see citing works

Multiple environmental and genetic factors influence skeletal muscle PGC-1α and PGC-1β gene expression in twins

Ling, C., Poulsen, P., Carlsson, E., Ridderstråle, M., Almgren, P., Wojtaszewski, J. F. P., Beck‐Nielsen, H., Groop, L., & Vaag, A. A. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200421889 · Cited by 300 · see citing works

Multiple environmental and genetic factors influence skeletal muscle PGC-1α and PGC-1β gene expression in twins

Ling, C., Poulsen, P., Carlsson, E., Ridderstråle, M., Almgren, P., Wojtaszewski, J., Beck-Nielsen, H., Groop, L., & Vaag, A. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21889 · Cited by 300 · see citing works

Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1α transcription and mitochondrial biogenesis in muscle cells

Wu, Z., Huang, X., Feng, Y., Handschin, C., Feng, Y., Gullicksen, P. S., Bare, O., Labow, M., Spiegelman, B., & Stevenson, S. C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606714103 · Cited by 291 · see citing works

Tissue-specific regulation of metabolic pathways through the transcriptional coactivator PGC1-α

Puigserver, P. (2005) · International Journal of Obesity · doi:10.1038/sj.ijo.0802905 · Cited by 290 · see citing works

Dynamic regulation of PGC‐1α localization and turnover implicates mitochondrial adaptation in calorie restriction and the stress response

Anderson, R. M., Barger, J. L., Edwards, M. G., Braun, K. H., O’Connor, C. E., Prolla, T. A., & Weindruch, R. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2007.00357.x · Cited by 283 · see citing works

Effects of α‐AMPK knockout on exercise‐induced gene activation in mouse skeletal muscle

Jørgensen, S. B., Wojtaszewski, J. F. P., Viollet, B., Andreelli, F., Birk, J. B., Hellsten, Y., Schjerling, P., Vaulont, S., Neufer, P. D., Richter, E. A., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-3144fje · Cited by 274 · see citing works

Activation of nuclear receptor coactivator PGC-1α by arginine methylationPreprint

Teyssier, C., Ma, H., Emter, R., Kralli, A., & Stallcup, M. R. (2005) · Genes & Development · doi:10.1101/gad.1295005 · Cited by 260 · see citing works

Effects of chronic AICAR treatment on fiber composition, enzyme activity, UCP3, and PGC-1 in rat muscles

Suwa, M., Nakano, H., & Kumagai, S. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00349.2003 · Cited by 250 · see citing works

A PGC-1α-O-GlcNAc Transferase Complex Regulates FoxO Transcription Factor Activity in Response to Glucose

Housley, M. P., Udeshi, N. D., Rodgers, J. T., Shabanowitz, J., Puigserver, P., Hunt, D. F., & Hart, G. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808890200 · Cited by 216 · see citing works

Characterization of two genes required for the position‐effect control of yeast mating‐type genes.

Shore, D., Squire, M., & Nasmyth, K. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02214.x · Cited by 206 · see citing works

The genetic ablation of SRC-3 protects against obesity and improves insulin sensitivity by reducing the acetylation of PGC-1α

Coste, A., Louet, J.-F., Lagouge, M., Lerin, C., Antal, M. C., Meziane, H., Schoonjans, K., Puigserver, P., O'Malley, B. W., & Auwerx, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808207105 · Cited by 205 · see citing works

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 · see citing works

SCFCdc4 acts antagonistically to the PGC-1α transcriptional coactivator by targeting it for ubiquitin-mediated proteolysisPreprint

Olson, B. L., Hock, M. B., Ekholm‐Reed, S., Wohlschlegel, J. A., Dev, K. K., Kralli, A., & Reed, S. I. (2008) · Genes & Development · doi:10.1101/gad.1624208 · Cited by 185 · see citing works

A Functional Interaction between RIP140 and PGC-1α Regulates the Expression of the Lipid Droplet Protein CIDEA

Hallberg, M., Morganstein, D. L., Kiskinis, E., Shah, K., Kralli, A., Dilworth, S. M., White, R., Parker, M. G., & Christian, M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00504-08 · Cited by 164 · see citing works

Nitric oxide regulates mitochondrial oxidative stress protection via the transcriptional coactivator PGC‐1α

Borniquel, S., Valle, I., Cadenas, S., Lamas, S., & Monsalve, M. (2006) · The FASEB Journal · doi:10.1096/fj.05-5189fje · Cited by 147 · see citing works

p38 Mitogen-activated Protein Kinase Plays a Stimulatory Role in Hepatic Gluconeogenesis

Cao, W., Collins, Q. F., Becker, T. C., Robidoux, J., Lupo, E. G., Xiong, Y., Daniel, K. W., Floering, L. M., & Collins, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506223200 · Cited by 146 · see citing works

Cdc2-like Kinase 2 Is an Insulin-Regulated Suppressor of Hepatic Gluconeogenesis

Rodgers, J. T., Haas, W., Gygi, S. P., & Puigserver, P. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2009.11.006 · Cited by 132 · see citing works

GCN5-mediated Transcriptional Control of the Metabolic Coactivator PGC-1β through Lysine Acetylation

Kelly, T. J., Lerín, C., Haas, W., Gygi, S. P., & Puigserver, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.015164 · Cited by 130 · see citing works

p38 Mitogen-activated Protein Kinase Mediates Free Fatty Acid-induced Gluconeogenesis in Hepatocytes

Collins, Q. F., Xiong, Y., Lupo, E. G., Liu, H., & Cao, W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602177200 · Cited by 122 · see citing works

Real-time imaging of peroxisome proliferator-activated receptor-γ coactivator-1α promoter activity in skeletal muscles of living mice

Akimoto, T., Sorg, B. S., & Yan, Z. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00425.2003 · Cited by 117 · see citing works

Intramolecular Control of Protein Stability, Subnuclear Compartmentalization, and Coactivator Function of Peroxisome Proliferator-activated Receptor γ Coactivator 1α

Sano, M., Tokudome, S., Shimizu, N., Yoshikawa, N., Ogawa, C., Shirakawa, K., Endo, J., Katayama, T., Yuasa, S., Ieda, M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703634200 · Cited by 114 · see citing works

Role of the β3-Adrenergic Receptor and/or a Putative β4-Adrenergic Receptor on the Expression of Uncoupling Proteins and Peroxisome Proliferator-Activated Receptor-γ Coactivator-1

Boss, O., Bachman, E. S., Vidal‐Puig, A., Zhang, C., Peroni, O. D., & Lowell, B. B. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1145 · Cited by 100 · see citing works

Regulation of NT-PGC-1α Subcellular Localization and Function by Protein Kinase A-dependent Modulation of Nuclear Export by CRM1

Chang, J. S., Huypens, P., Zhang, Y., Black, C. M., Kralli, A., & Gettys, T. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083121 · Cited by 84 · see citing works

Rapid in vivo PGC-1 mRNA upregulation in brown adipose tissue of Wistar rats by a β3-adrenergic agonist and lack of effect of leptin

Gómez‐Ambrosi, J., Frühbeck, G., & Martínez, J. A. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(01)00451-8 · Cited by 43 · see citing works

The Hallmarks of Aging

López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works

Sirtuins as regulators of metabolism and healthspan

Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works

Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging

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 · see citing works

NAD ⁺ in aging, metabolism, and neurodegeneration

Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319 · see citing works

Oncogene ablation-resistant pancreatic cancer cells depend on mitochondrial function

Viale, A., Pettazzoni, P., Lyssiotis, C. A., Ying, H., Sánchez, N., Marchesini, M., Carugo, A., Green, T., Seth, S., Giuliani, V., et al. (2014) · Nature · doi:10.1038/nature13611 · Cited by 1,259 · see citing works

Microglia polarization from M1 to M2 in neurodegenerative diseases

Guo, S., Wang, H., & Yin, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.815347 · Cited by 920 · see citing works

The Tumor Microenvironment Represses T Cell Mitochondrial Biogenesis to Drive Intratumoral T Cell Metabolic Insufficiency and Dysfunction

Scharping, N. E., Menk, A. V., Moreci, R. S., Whetstone, R. D., Dadey, R. E., Watkins, S. C., Ferris, R. L., & Delgoffe, G. M. (2016) · Immunity · doi:10.1016/j.immuni.2016.07.009 · Cited by 848 · see citing works

Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds

Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834 · see citing works

Transcriptional integration of mitochondrial biogenesis

Scarpulla, R. C., Vega, R. B., & Kelly, D. P. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.06.006 · Cited by 798 · see citing works

Mitonuclear communication in homeostasis and stress

Quirós, P. M., Mottis, A., & Auwerx, J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.23 · Cited by 787 · see citing works

Irisin Stimulates Browning of White Adipocytes Through Mitogen-Activated Protein Kinase p38 MAP Kinase and ERK MAP Kinase Signaling

Zhang, Y., Li, R., Meng, Y., Li, S., Donelan, W., Zhao, Y., Qi, L., Zhang, M., Wang, X., Cui, T., et al. (2014) · Diabetes · doi:10.2337/db13-1106 · Cited by 733 · see citing works

PGC1α Expression Defines a Subset of Human Melanoma Tumors with Increased Mitochondrial Capacity and Resistance to Oxidative Stress

Vazquez, F., Lim, J.-H., Chim, H., Bhalla, K., Girnun, G., Pierce, K., Clish, C. B., Granter, S. R., Widlund, H. R., Spiegelman, B. M., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2012.11.020 · Cited by 715 · see citing works

MYC/PGC-1α Balance Determines the Metabolic Phenotype and Plasticity of Pancreatic Cancer Stem Cells

Sancho, P., Burgos-Ramos, E., Tavera, A., Bou Kheir, T., Jagust, P., Schoenhals, M., Barneda, D., Sellers, K., Campos-Olivas, R., Graña, O., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.08.015 · Cited by 722 · see citing works

Pharmacological approaches to restore mitochondrial function

Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works

Mitochondrial dysfunction in ataxia-telangiectasia

Valentin-Vega, Y. A., MacLean, K. H., Tait-Mulder, J., Milasta, S., Steeves, M., Dorsey, F. C., Cleveland, J. L., Green, D. R., & Kastan, M. B. (2012) · Blood · doi:10.1182/blood-2011-08-373639 · Cited by 365 · see citing works

Mechanisms and regulation of protein synthesis in mitochondria

Kummer, E., & Ban, N. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00332-2 · Cited by 349 · see citing works

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 · see citing works

O-GlcNAc Transferase/Host Cell Factor C1 Complex Regulates Gluconeogenesis by Modulating PGC-1α Stability

Ruan, H.-B., Han, X., Li, M.-D., Singh, J. P., Qian, K., Azarhoush, S., Zhao, L., Bennett, A. M., Samuel, V. T., Wu, J., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.006 · Cited by 296 · see citing works

Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice

Quirós, P. M., Ramsay, A. J., Sala, D., Fernández‐Vizarra, E., Rodríguez, F., Peinado, J. R., Fernández‐García, M. S., Vega, J. A., Enríquez, J. A., Zorzano, A., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.70 · Cited by 269 · see citing works

AMPK promotes mitochondrial biogenesis and function by phosphorylating the epigenetic factors DNMT1, RBBP7, and HAT1

Marin, T. L., Gongol, B., Zhang, F., Martin, M., Johnson, D. A., Xiao, H., Wang, Y., Subramaniam, S., Chien, S., & Shyy, J. Y.-J. (2017) · Science Signaling · doi:10.1126/scisignal.aaf7478 · Cited by 257 · see citing works

The neuroprotective effects of glucagon-like peptide 1 in Alzheimer’s and Parkinson’s disease: An in-depth review

Reich, N., & Hölscher, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.970925 · Cited by 248 · see citing works

Inhibition of prostaglandin-degrading enzyme 15-PGDH rejuvenates aged muscle mass and strength

Palla, A. R., Ravichandran, M., Wang, Y. X., Alexandrova, L., Yang, A. V., Kraft, P., Holbrook, C. A., Schürch, C. M., Ho, A. T. V., & Blau, H. M. (2021) · Science · doi:10.1126/science.abc8059 · Cited by 232 · see citing works

Metabolic adaptation in obesity and type ii diabetes: myokines, adipokines and hepatokines

Oh, K.-J., Lee, D., Kim, W., Han, B., Lee, S., & Bae, K.-H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms18010008 · Cited by 210 · see citing works

Vitamin C and E supplementation prevents some of the cellular adaptations to endurance-training in humans

Morrison, D., Hughes, J., Della Gatta, P. A., Mason, S., Lamon, S., Russell, A. P., & Wadley, G. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.412 · Cited by 171 · see citing works

Mitochondrial dynamics, transport, and quality control: A bottleneck for retinal ganglion cell viability in optic neuropathies

Ito, Y. A., & Di Polo, A. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.08.014 · Cited by 142 · see citing works

Turn up the power - pharmacological activation of mitochondrial biogenesis in mouse models

Komen, J. C., & Thorburn, D. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12413 · Cited by 149 · see citing works

Intensified mitophagy in skeletal muscle with aging is downregulated by PGC-1alpha overexpression in vivo

Yeo, D., Kang, C., Gomez-Cabrera, M. C., Vina, J., & Ji, L. L. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.456 · Cited by 137 · see citing works

Beta-Aminoisobutyric Acid as a Novel Regulator of Carbohydrate and Lipid Metabolism

Tanianskii, D. A., Jarzebska, N., Birkenfeld, A. L., O’Sullivan, J. F., & Rodionov, R. N. (2019) · Nutrients · doi:10.3390/nu11030524 · Cited by 121 · see citing works

PGC-1α protects RPE cells of the aging retina against oxidative stress-induced degeneration through the regulation of senescence and mitochondrial quality control. The significance for AMD pathogenesis

Kaarniranta, K., Kajdanek, J., Morawiec, J., Pawlowska, E., & Blasiak, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082317 · Cited by 112 · see citing works

Natural Products as a Potential Modulator of Microglial Polarization in Neurodegenerative Diseases

Jin, X., Liu, M.-Y., Zhang, D.-F., Zhong, X., Du, K., Qian, P., Gao, H., & Wei, M.-J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104253 · Cited by 109 · see citing works

Targeting the acetylation signaling pathway in cancer therapy

Dang, F., & Wei, W. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.03.001 · Cited by 109 · see citing works

Nuclear respiratory factor 1 and endurance exercise promote human telomere transcription

Diman, A., Boros, J., Poulain, F., Rodriguez, J., Purnelle, M., Episkopou, H., Bertrand, L., Francaux, M., Deldicque, L., & Decottignies, A. (2016) · Science Advances · doi:10.1126/sciadv.1600031 · Cited by 101 · see citing works

Aerobic and resistance exercise training reverses age‐dependent decline in NAD⁺salvage capacity in human skeletal muscle

de Guia, R. M., Agerholm, M., Nielsen, T. S., Consitt, L. A., Søgaard, D., Helge, J. W., Larsen, S., Brandauer, J., Houmard, J. A., & Treebak, J. T. (2019) · Physiological Reports · doi:10.14814/phy2.14139 · Cited by 99 · see citing works

Prmt7 Deficiency Causes Reduced Skeletal Muscle Oxidative Metabolism and Age-Related Obesity

Jeong, H.-J., Lee, H.-J., Vuong, T. A., Choi, K.-S., Choi, D., Koo, S.-H., Cho, S. C., Cho, H., & Kang, J.-S. (2016) · Diabetes · doi:10.2337/db15-1500 · Cited by 101 · see citing works

Coordination of mitochondrial biogenesis by PGC-1α in human skeletal muscle: A re-evaluation

Islam, H., Edgett, B. A., & Gurd, B. J. (2018) · Metabolism · doi:10.1016/j.metabol.2017.11.001 · Cited by 99 · see citing works

Mitochondrial dynamics in cancer-induced cachexia

van der Ende, M., Grefte, S., Plas, R., Meijerink, J., Witkamp, R. F., Keijer, J., & van Norren, K. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.07.008 · Cited by 87 · see citing works

A perspective on the determination of mitochondrial biogenesis

Miller, B. F., & Hamilton, K. L. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00578.2011 · Cited by 86 · see citing works

Nutraceutical Activation of Sirt1: A Review

DiNicolantonio, J. J., McCarty, M. F., & O'Keefe, J. H. (2022) · Open Heart · doi:10.1136/openhrt-2022-002171 · Cited by 65 · see citing works

Musclin, A Myokine Induced by Aerobic Exercise, Retards Muscle Atrophy During Cancer Cachexia in Mice

Re Cecconi, A. D., Forti, M., Chiappa, M., Zhu, Z., Zingman, L. V., Cervo, L., Beltrame, L., Marchini, S., & Piccirillo, R. (2019) · Cancers · doi:10.3390/cancers11101541 · Cited by 66 · see citing works

Resistance training increases muscle NAD(+) and NADH concentrations as well as NAMPT protein levels and global sirtuin activity in middle-aged, overweight, untrained individuals

Lamb, D. A., Moore, J. H., Mesquita, P. H. C., Smith, M. A., Vann, C. G., Osburn, S. C., Fox, C. D., Lopez, H. L., Ziegenfuss, T. N., Huggins, K. W., et al. (2020) · Aging · doi:10.18632/aging.103218 · Cited by 62 · see citing works

Novel Insights into the Anti-Aging Role of Mitophagy

(2018) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2018.05.005 · Cited by 56 · see citing works

From mitochondria to sarcopenia: role of 17β-estradiol and testosterone

Tian, X., Lou, S., & Shi, R. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1156583 · Cited by 54 · see citing works

Myricanol mitigates lipid accumulation in 3T3-L1 adipocytes and high fat diet-fed zebrafish via activating AMP-activated protein kinase

Shen, S., Liao, Q., Feng, Y., Liu, J., Pan, R., Lee, S. M.-Y., & Lin, L. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2018.07.117 · Cited by 51 · see citing works

Combined activation of the energy and cellular-defense pathways may explain the potent anti-senescence activity of methylene blue

Atamna, H., Atamna, W., Al-Eyd, G., Shanower, G., & Dhahbi, J. M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.004 · Cited by 40 · see citing works

Disruptions to the limb muscle core molecular clock coincide with changes in mitochondrial quality control following androgen depletion

Rossetti, M. L., Esser, K. A., Lee, C., Tomko, R. J., Eroshkin, A. M., & Gordon, B. S. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00177.2019 · Cited by 37 · see citing works

Butyrate Ameliorates Mitochondrial Respiratory Capacity of The Motor-Neuron-like Cell Line NSC34-G93A, a Cellular Model for ALS

Li, X., Dong, L., Li, A., Yi, J., Brotto, M., & Zhou, J. (2022) · Biomolecules · doi:10.3390/biom12020333 · Cited by 33 · see citing works

Gper and erα mediate estradiol enhancement of mitochondrial function in inflamed adipocytes through a pka dependent mechanism

Bauzá-Thorbrügge, M., Rodríguez-Cuenca, S., Vidal-Puig, A., Galmés-Pascual, B. M., Sbert-Roig, M., Gianotti, M., Lladó, I., & Proenza, A. M. (2019) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2018.09.013 · Cited by 30 · see citing works

Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds

Jun, L., Tao, Y.-X., Geetha, T., & Babu, J. R. (2024) · Current Nutrition Reports · doi:10.1007/s13668-024-00555-7 · Cited by 27 · see citing works

Cellular Models of Aging and Senescence

Kim, B., Lee, D. I., Basisty, N., & Dai, D.-F. (2025) · Cells · doi:10.3390/cells14161278 · Cited by 16 · see citing works

Study on the comorbid mechanisms of sarcopenia and late-life depression

Wu, J., Tang, J., Huang, D., Wang, Y., Zhou, E., Ru, Q., Xu, G., Chen, L., & Wu, Y. (2025) · Behavioural Brain Research · doi:10.1016/j.bbr.2025.115538 · Cited by 12 · see citing works

Research progress in peroxisome proliferator-activated receptor γ coactivator-1α

Tao, H. (2012) · International Journal of Pathology and Clinical Medicine

Expression of PGC1α in glioblastoma multiforme patients

Cho, S. Y., Kim, S., Yi, M., et al. (2017) · Oncology Letters · doi:10.3892/ol.2017.5972 · Cited by 10 · see citing works

Age associated low mitochondrial biogenesis may be explained by lack of response of PGC-1α to exercise training

Derbré, F., Gómez‐Cabrera, M. C., Nascimento, A. L. R., Sanchis‐Gomar, F., Martinez-Bello, V. E., Tresguerres, J. A. F., Fuentes, T., Gratas‐Delamarche, A., Monsalve, M., & Viña, J. (2011) · AGE · doi:10.1007/s11357-011-9264-y · Cited by 129 · see citing works

Mitochondrial Biogenesis Inhibitors for Anticancer Therapy: A Review of Recent Patents

Wang, J., Wen, X., Liu, J., & Sun, H. (2016) · Recent Patents on Anti-Cancer Drug Discovery · doi:10.2174/1574892811666160418123628 · Cited by 4 · see citing works

Cardiac-specific induction of the transcriptional coactivator peroxisome proliferator-activated receptor γ coactivator-1α promotes mitochondrial biogenesis and reversible cardiomyopathy in a developmental stage-dependent manner.

Russell, L. K., Mansfield, C. M., Lehman, J. J., Kovacs, A., Courtois, M., Saffitz, J. E., Medeiros, D. M., Valencik, M. L., McDonald, J. A., & Kelly, D. P. (2004) · Circulation Research · doi:10.1161/01.res.0000117088.36577.eb · Cited by 402 · see citing works