Mitochondrial Chaperones in the Brain: Safeguarding Brain Health and Metabolism?

Anti-Vascular Endothelial Growth Factors Protect Retinal Pigment Epithelium Cells Against Oxidation by Modulating Nitric Oxide Release and Autophagy

Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,154 · see citing works

Mitochondrial formation of reactive oxygen species

Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works

An RNA-Sequencing Transcriptome and Splicing Database of Glia, Neurons, and Vascular Cells of the Cerebral Cortex

Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875 · see citing works

A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine

Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185 · see citing works

Brain energy metabolism: focus on Astrocyte-neuron metabolic cooperation

Bélanger, M., Allaman, I., & Magistretti, P. J. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.016 · Cited by 2,313 · see citing works

Role of Brain Insulin Receptor in Control of Body Weight and Reproduction

Brüning, J. C., Gautam, D., Burks, D. J., Gillette, J., Schubert, M., Orban, P. C., Klein, R., Krone, W., Müller-Wieland, D., & Kahn, C. R. (2000) · Science · doi:10.1126/science.289.5487.2122 · Cited by 2,235 · see citing works

Mitochondrial dysfunction and type 2 diabetes

Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070 · see citing works

Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulatorsPreprint

Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.24.3788 · Cited by 1,898 · see citing works

The Role of Oxidative Stress in Parkinson's Disease

Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845 · see citing works

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818 · see citing works

Molecular Chaperones and Protein Quality Control

Bukau, B., Weissman, J. S., & Horwich, A. L. (2006) · Cell · doi:10.1016/j.cell.2006.04.014 · Cited by 1,556 · see citing works

Novel Signal Transduction Pathway Utilized by Extracellular HSP70

Asea, A., Rehli, M., Kabingu, E., Boch, J. A., Baré, O., Auron, P. E., Stevenson, M. A., & Calderwood, S. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200497200 · Cited by 1,510 · see citing works

Insulin Receptor Signaling in Normal and Insulin-Resistant StatesPreprint

Boucher, J., Kleinridders, A., & Kahn, C. R. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a009191 · Cited by 1,473 · see citing works

The Biology of Proteostasis in Aging and Disease

Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472 · see citing works

Molecular Chaperone Functions in Protein Folding and Proteostasis

Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,468 · see citing works

Oxidative stress, insulin signaling, and diabetes

Rains, J., & Jain, S. K. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.006 · Cited by 1,445 · see citing works

Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.

Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438 · see citing works

Chronic intracerebroventricular infusion of insulin reduces food intake and body weight of baboons

Woods, S. C., Lotter, E. C., McKay, L. D., & Porte, D. (1979) · Nature · doi:10.1038/282503a0 · Cited by 1,114 · see citing works

Metabolic regulation of mitochondrial dynamics

Mishra, P., & Chan, D. C. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201511036 · Cited by 1,096 · see citing works

Mitonuclear protein imbalance as a conserved longevity mechanism

Houtkooper, R. H., Mouchiroud, L., Ryu, D., Moullan, N., Katsyuba, E., Knott, G., Williams, R. W., & Auwerx, J. (2013) · Nature · doi:10.1038/nature12188 · Cited by 1,035 · see citing works

A mitochondrial specific stress response in mammalian cells

Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., & Hoogenraad, N. J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf445 · Cited by 1,026 · see citing works

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

Cheng, M. Y., Hartl, F. U., Martin, J., Pollock, R. A., Kalousek, F., Neuper, W., Hallberg, E. M., Hallberg, R. L., & Horwich, A. L. (1989) · Nature · doi:10.1038/337620a0 · Cited by 953 · see citing works

Mitochondrial Dynamics in Mammalian Health and Disease

Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953 · see citing works

Increased Risk of Type 2 Diabetes in Alzheimer Disease

Janson, J., Laedtke, T., Parisi, J. E., O’Brien, P., Petersen, R. C., & Butler, P. C. (2004) · Diabetes · doi:10.2337/diabetes.53.2.474 · Cited by 950 · see citing works

Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70

Young, J. C., Hoogenraad, N. J., & Hartl, F. U. (2003) · Cell · doi:10.1016/s0092-8674(02)01250-3 · Cited by 915 · see citing works

Hypothalamic insulin signaling is required for inhibition of glucose production

Obici, S., Zhang, B. B., Karkanias, G., & Rossetti, L. (2002) · Nature Medicine · doi:10.1038/nm1202-798 · Cited by 904 · see citing works

Protein disaggregation mediated by heat-shock protein Hspl04

Parsell, D. A., Kowal, A. S., Singer, M. A., & Lindquist, S. L. (1994) · Nature · doi:10.1038/372475a0 · Cited by 864 · see citing works

Endocytosed HSP60s Use Toll-like Receptor 2 (TLR2) and TLR4 to Activate the Toll/Interleukin-1 Receptor Signaling Pathway in Innate Immune Cells

Vabulas, R. M., Ahmad-Nejad, P., da Costa, C., Miethke, T., Kirschning, C. J., Häcker, H., & Wagner, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103217200 · Cited by 805 · see citing works

Cerebral metabolic and cognitive decline in persons at genetic risk for Alzheimer’s disease

Small, G. W., Ercoli, L. M., Silverman, D. H. S., Huang, S.-C., Komo, S., Bookheimer, S. Y., Lavretsky, H., Miller, K., Siddarth, P., Rasgon, N. L., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.090106797 · Cited by 790 · see citing works

The mTOR pathway in the control of protein synthesis

Wang, X., & Proud, C. G. (2006) · Physiology · doi:10.1152/physiol.00024.2006 · Cited by 778 · see citing works

Parkinson's Disease Brain Mitochondrial Complex I Has Oxidatively Damaged Subunits and Is Functionally Impaired and Misassembled

Keeney, P., Xie, J., Capaldi, R., & Bennett, J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0984-06.2006 · Cited by 757 · see citing works

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

Fayet, O., Ziegelhoffer, T., & Georgopoulos, C. P. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.3.1379-1385.1989 · Cited by 705 · see citing works

Obesity-Induced CerS6-Dependent C16:0 Ceramide Production Promotes Weight Gain and Glucose Intolerance

Turpin-Nolan, S. M., Nicholls, H. T., Willmes, D. M., Mourier, A., Brodesser, S., Wunderlich, C. M., Mauer, J., Xu, E., Hammerschmidt, P., Brönneke, H. S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.002 · Cited by 693 · see citing works

Insulin Action in Brain Regulates Systemic Metabolism and Brain Function

Kleinridders, A., Ferris, H. A., Cai, W., & Kahn, C. R. (2014) · Diabetes · doi:10.2337/db14-0568 · Cited by 688 · see citing works

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

Ostermann, J., Horwich, A. L., Neupert, W., & Hartl, F. U. (1989) · Nature · doi:10.1038/341125a0 · Cited by 677 · see citing works

Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones

Yoneda, T., Benedetti, C., Urano, F., Clark, S. G., Harding, H. P., & Ron, D. (2004) · Journal of Cell Science · doi:10.1242/jcs.01275 · Cited by 636 · see citing works

Oxidative stress and the etiology of insulin resistance and type 2 diabetes

Henriksen, E. J., Diamond-Stanic, M. K., & Marchionne, E. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.005 · Cited by 600 · see citing works

Somatic Mitochondrial DNA Mutations in Mammalian Aging

Larsson, N. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-093701 · Cited by 543 · see citing works

Mitochondrial Dysfunction and Biogenesis in Neurodegenerative diseases: Pathogenesis and Treatment

Golpich, M., Amini, E., Mohamed, Z., Raymond, A. A., Ibrahim, N. M., & Ahmadiani, A. (2016) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12655 · Cited by 540 · see citing works

Mitostasis in Neurons: Maintaining Mitochondria in an Extended Cellular Architecture

Misgeld, T., & Schwarz, T. L. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.055 · Cited by 536 · see citing works

Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease

Ryan, B. J., Hoek, S., Fon, E. A., & Wade-Martins, R. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.02.003 · Cited by 524 · see citing works

Mitofusin 2 in POMC neurons connects ER stress with leptin resistance and energy imbalance

Schneeberger, M., Dietrich, M. O., Sebastián, D., Imbernón, M., Castaño, C., Garcia, A., Esteban, Y., Gonzalez-Franquesa, A., Rodríguez, I. C., Bortolozzi, A., et al. (2013) · Cell · doi:10.1016/j.cell.2013.09.003 · Cited by 519 · see citing works

Quality control of mitochondria: protection against neurodegeneration and ageing

Tatsuta, T., & Langer, T. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601972 · Cited by 519 · see citing works

Protein Misfolding Diseases

Hartl, F. U. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044518 · Cited by 519 · see citing works

Disease-causing mutations in Parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy

Lee, J., Nagano, Y., Taylor, J. P., Lim, K. L., & Yao, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001039 · Cited by 517 · see citing works

Role of Protein Aggregation in Mitochondrial Dysfunction and Neurodegeneration in Alzheimer's and Parkinson's Diseases

Hashimoto, M., Rockenstein, E. M., Crews, L. A., & Masliah, E. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:21 · Cited by 498 · see citing works

The mitochondrial UPR – protecting organelle protein homeostasis

Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 490 · see citing works

Insulin resistance in brain alters dopamine turnover and causes behavioral disorders

Kleinridders, A., Cai, W., Cappellucci, L., Ghazarian, A., Collins, W. R., Vienberg, S. G., Pothos, E. N., & Kahn, C. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500877112 · Cited by 486 · see citing works

SirT3 is a nuclear NAD + -dependent histone deacetylase that translocates to the mitochondria upon cellular stressPreprint

Scher, M. B., Vaquero, A., & Reinberg, D. (2007) · Genes & Development · doi:10.1101/gad.1527307 · Cited by 476 · see citing works

Type 2 Diabetes and the Risk of Parkinson's Disease

Hu, G., Jousilahti, P., Bidel, S., Antikainen, R., & Tuomilehto, J. (2007) · Diabetes Care · doi:10.2337/dc06-2011 · Cited by 466 · see citing works

Ageing and diabetes: implications for brain function

Biessels, G. J., van der Heide, L. P., Kamal, A., Bleys, R. L. A. W., & Gispen, W. H. (2002) · European Journal of Pharmacology · doi:10.1016/s0014-2999(02)01486-3 · Cited by 458 · see citing works

Glial Cell Inhibition of Neurons by Release of ATP

Newman, E. A. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-05-01659.2003 · Cited by 427 · see citing works

Different Responses of Astrocytes and Neurons to Nitric Oxide: The Role of Glycolytically Generated ATP in Astrocyte Protection

Almeida, A., Almeida, J., Bolaños, J. P., & Moncada, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261560998 · Cited by 423 · see citing works

The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria

Jin, S. M., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.26122 · Cited by 411 · see citing works

Mitochondria-associated endoplasmic reticulum membrane (MAM) integrity is required for insulin signaling and is implicated in hepatic insulin resistance

Tubbs, E., Theurey, P., Vial, G., Bendridi, N., Bravard, A., Chauvin, M.-A., Ji-Cao, J., Zoulim, F., Bartosch, B., Ovize, M., et al. (2014) · Diabetes · doi:10.2337/db13-1751 · Cited by 411 · cited 1× · see citing works

Neuroprotective Role of the Reaper-Related Serine Protease HtrA2/Omi Revealed by Targeted Deletion in Mice

Martins, L. M., Morrison, A., Klupsch, K., Fedele, V., Moisoi, N., Teismann, P., Abuin, A., Grau, E., Geppert, M., Livi, G. P., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.22.9848-9862.2004 · Cited by 395 · see citing works

Water maze learning and hippocampal synaptic plasticity in streptozotocin-diabetic rats: effects of insulin treatment

Biessels, G. J., Kamal, A., Urban, I. J. A., Spruijt, B. M., Erkelens, D. W., & Gispen, W. H. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00510-1 · Cited by 379 · see citing works

Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice

Jones, J. M., Datta, P., Srinivasula, S. M., Ji, W., Gupta, S., Zhang, Z., Davies, E., Hajnóczky, G., Saunders, T. L., Keuren, M. L. V., et al. (2003) · Nature · doi:10.1038/nature02052 · Cited by 378 · see citing works

Hereditary Spastic Paraplegia SPG13 Is Associated with a Mutation in the Gene Encoding the Mitochondrial Chaperonin Hsp60

Hansen, J. J., Dürr, A., Cournu‐Rebeix, I., Georgopoulos, C. P., Ang, D., Nielsen, M. N., Davoine, C.-S., Brice, A., Fontaine, B., Gregersen, N., et al. (2002) · The American Journal of Human Genetics · doi:10.1086/339935 · Cited by 373 · see citing works

Mitochondrial stress induces chromatin reorganization to promote longevity and UPR(mt)

Tian, Y., Garcia, G., Bian, Q., Steffen, K. K., Joe, L., Wolff, S., Meyer, B. J., & Dillin, A. (2016) · Cell · doi:10.1016/j.cell.2016.04.011 · Cited by 370 · see citing works

Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence

Höhn, A., Weber, D., Jung, T., Ott, C., Hugo, M., Kochlik, B., Kehm, R., König, J., Grune, T., & Castro, J. P. (2016) · Redox Biology · doi:10.1016/j.redox.2016.12.001 · Cited by 368 · see citing works

Hippocampal hypometabolism predicts cognitive decline from normal aging

Mosconi, L., De Santi, S., Li, J., Tsui, W. H., Li, Y., Boppana, M., Laska, E., Rusinek, H., & de Leon, M. J. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.12.008 · Cited by 360 · see citing works

Regulation of the Cellular Heat Shock Response in Caenorhabditis elegans by Thermosensory Neurons

Prahlad, V., Cornelius, T., & Morimoto, R. I. (2008) · Science · doi:10.1126/science.1156093 · Cited by 359 · see citing works

Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome.

Martinus, R., Garth, G. P., Webster, T., Cartwright, P., Naylor, D. J., Høj, P., & Hoogenraad, N. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0098h.x · Cited by 340 · see citing works

Role for neuronal insulin resistance in neurodegenerative diseases

Schubert, M., Gautam, D., Surjo, D., Ueki, K., Baudler, S., Schubert, D., Kondo, T., Alber, J., Galldiks, N., Kustermann, E., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308724101 · Cited by 339 · see citing works

Type 2 diabetes as a protein misfolding disease

Mukherjee, A., Morales‐Scheihing, D., Butler, P. C., & Soto, C. A. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.04.005 · Cited by 338 · see citing works

Chaperoning extended life

Tatar, M., Khazaeli, A. A., & Curtsinger, J. W. (1997) · Nature · doi:10.1038/36237 · Cited by 332 · see citing works

European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)

Egea, J., Fabregat, I., Frapart, Y., Ghezzi, P., Görlach, A., Kietzmann, T., Kubaichuk, K. I., Knaus, U. G., López, M. G., González, G. O., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.05.007 · Cited by 311 · see citing works

Mitochondrial Dysfunction in SOD1G93A-Bearing Astrocytes Promotes Motor Neuron Degeneration: Prevention by Mitochondrial-Targeted Antioxidants

Cassina, P., Cassina, A., Pehar, M., Castellanos, R., Gandelman, M., de León, A., Robinson, K. M., Mason, R. P., Beckman, J. S., Barbeito, L., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5308-07.2008 · Cited by 310 · see citing works

Mitochondrial dynamics controlled by mitofusins regulate Agrp neuronal activity and diet-induced obesity

Dietrich, M. O., Liu, Z.-W., & Horvath, T. L. (2013) · Cell · doi:10.1016/j.cell.2013.09.004 · Cited by 306 · see citing works

Maintenance and propagation of a deleterious mitochondrial genome by the mitochondrial unfolded protein response

Lin, Y., Schulz, A. M., Pellegrino, M. W., Lu, Y., Shaham, S., & Haynes, C. M. (2016) · Nature · doi:10.1038/nature17989 · Cited by 302 · see citing works

Mitochondria in Huntington's disease

Damiano, M. G., Galvan, L., Déglon, N., & Brouillet, E. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.012 · Cited by 282 · see citing works

Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis

Yoshida, S., Tsutsumi, S., Mühlebach, G., Sourbier, C., Lee, M.-J., Lee, S., Vartholomaiou, E., Tatokoro, M., Beebe, K. E., Miyajima, N., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220659110 · Cited by 281 · see citing works

SGLT2-inhibitor and DPP-4 inhibitor improve brain function via attenuating mitochondrial dysfunction, insulin resistance, inflammation, and apoptosis in HFD-induced obese rats

Sa-nguanmoo, P., Tanajak, P., Kerdphoo, S., Jaiwongkam, T., Pratchayasakul, W., Chattipakorn, N., & Chattipakorn, S. C. (2017) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2017.08.005 · Cited by 274 · see citing works

Central insulin action regulates peripheral glucose and fat metabolism in mice

Koch, L., Wunderlich, F. T., Seibler, J., Könner, A. C., Hampel, B., Irlenbusch, S., Brabant, G. E., Kahn, C. R., Schwenk, F., & Brüning, J. C. (2008) · Journal of Clinical Investigation · doi:10.1172/jci31073 · Cited by 270 · see citing works

Diabetes Mellitus and the Risk of Alzheimer’s Disease: A Nationwide Population-Based Study

Huang, C., Chung, C., Leu, H., Lin, L., Chiu, C.-C., Hsu, C., Chiang, C.-H., Huang, P., Chen, T., Lin, S., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087095 · Cited by 266 · see citing works

Mitochondrial involvement in brain function and dysfunction: relevance to aging, neurodegenerative disorders and longevity

Calabrese, V., Scapagnini, G., Giuffrida Stella, A. M., Bates, T. E., & Clark, J. B. (2001) · Neurochemical Research · doi:10.1023/a:1010955807739 · Cited by 263 · see citing works

Quality Control of Mitochondrial ProteostasisPreprint

Baker, M. J., Tatsuta, T., & Langer, T. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007559 · Cited by 260 · see citing works

Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding

Rowley, N., Prip‐Buus, C., Westermann, B., et al. (1994) · Cell · doi:10.1016/0092-8674(94)90317-4 · Cited by 249 · see citing works

Oxidative Stress and Insulin Resistance

Park, K., Gross, M., Lee, D., Holvoet, P., Himes, J. H., Shikany, J. M., & Jacobs, D. R. (2009) · Diabetes Care · doi:10.2337/dc09-0259 · Cited by 246 · see citing works

The Relationship Between Diabetes Mellitus and Parkinson'S Disease

Sandyk, R. (1993) · International Journal of Neuroscience · doi:10.3109/00207459309003322 · Cited by 244 · see citing works

Protein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus

Ashraf, G., Greig, N., Khan, T., Hassan, I., Tabrez, S., Shakil, S., Sheikh, I., Zaidi, S., Akram, M., Jabir, N., et al. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140917095514 · Cited by 236 · see citing works

Brain mitochondrial dysfunction in aging

Boveris, A., & Navarro, A. (2008) · IUBMB Life · doi:10.1002/iub.46 · Cited by 235 · see citing works

Inflammatory response of microglial BV‐2 cells includes a glycolytic shift and is modulated by mitochondrial glucose‐regulated protein 75/mortalin

Voloboueva, L. A., Emery, J. F., Sun, X., & Giffard, R. G. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.067 · Cited by 230 · see citing works

Extended longevity of Caenorhabditis elegans by knocking in extra copies of hsp70F, a homolog of mot‐2 (mortalin)/mthsp70/Grp75

Yokoyama, K., Fukumoto, K., Murakami, T., Harada, S.-I., Hosono, R., Wadhwa, R., Mitsui, Y., & Ohkuma, S. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02470-5 · Cited by 229 · see citing works

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 227 · see citing works

Loss of Mitochondrial Fission Depletes Axonal Mitochondria in Midbrain Dopamine Neurons

Berthet, A., Margolis, E. B., Zhang, J., Hsieh, I., Zhang, J., Hnasko, T. S., Ahmad, J., Edwards, R. H., Sesaki, H., Huang, E. J., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0930-14.2014 · Cited by 226 · see citing works

Shared dysregulated pathways lead to Parkinson's disease and diabetes

Santiago, J. A., & Potashkin, J. A. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.01.002 · Cited by 226 · see citing works

Mitochondrial Hsp60 Chaperonopathy Causes an Autosomal-Recessive Neurodegenerative Disorder Linked to Brain Hypomyelination and Leukodystrophy

Magen, D., Georgopoulos, C. P., Bross, P., Ang, D., Segev, Y., Goldsher, D., Nemirovski, A., Shahar, E. M., Ravid, S., LUDER, A. S., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.05.016 · Cited by 212 · see citing works

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 208 · see citing works

Diabetes and the Risk of Developing Parkinson’s Disease in Denmark

Schernhammer, E. S., Hansen, J., Rugbjerg, K., Wermuth, L., & Ritz, B. R. (2011) · Diabetes Care · doi:10.2337/dc10-1333 · Cited by 198 · see citing works

Computed Tomography and Positron Emission Transaxial Tomography Evaluations of Normal Aging and Alzheimer's Disease

de Leon, M. J., Ferris, S. H., GEORGE, A. E., Reisberg, ‌., Christman, D. R., Kricheff, I. I., & Wolf, A. P. (1983) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.1983.57 · Cited by 197 · see citing works

Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex I assemblyPreprint

Vogel, R. O., Janssen, R. J. R. J., van den Brand, M. A. M., Dieteren, C. E. J., Verkaart, S., Koopman, W. J. H., Willems, P. H. G. M., Pluk, W., van den Heuvel, L. P. W. J., Smeitink, J. A. M., et al. (2007) · Genes & Development · doi:10.1101/gad.408407 · Cited by 195 · see citing works

Mitochondrial protein quality control during biogenesis and aging

Baker, B. M., & Haynes, C. M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.01.004 · Cited by 192 · see citing works

SIRT3 Functions in the Nucleus in the Control of Stress-Related Gene Expression

Iwahara, T., Bonasio, R., Narendra, V. K., & Reinberg, D. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00822-12 · Cited by 192 · see citing works

TRAP-1, the mitochondrial Hsp90

Altieri, D. C., Stein, G. S., Lian, J. B., & Languino, L. R. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.08.007 · Cited by 187 · see citing works

Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response

Moisoi, N., Klupsch, K., Fedele, V., East, P., Sharma, S., Renton, A. E., Plun‐Favreau, H., Edwards, R., Teismann, P., Esposti, M. D., et al. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.166 · Cited by 175 · see citing works

Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease

Quintanilla, R. A., & Johnson, G. V. W. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.07.010 · Cited by 173 · see citing works

Hypothalamic and pituitary c-Jun N-terminal kinase 1 signaling coordinately regulates glucose metabolism

Belgardt, B., Mauer, J., Wunderlich, F. T., Ernst, M. B., Pál, M., Spohn, G., Brönneke, H. S., Brodesser, S., Hampel, B., Schauss, A. C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001796107 · Cited by 168 · see citing works

An Update on the Oxygen Stress–Mitochondrial Mutation Theory of Aging: Genetic and Evolutionary Implications

Miquel, J. (1998) · Experimental Gerontology · doi:10.1016/s0531-5565(97)00060-0 · Cited by 167 · see citing works

Loss of prohibitin membrane scaffolds impairs mitochondrial architecture and leads to tau hyperphosphorylation and neurodegeneration

Merkwirth, C., Martinelli, P., Korwitz, A., Morbin, M., Brönneke, H. S., Jordan, S. D., Rugarli, E. I., & Langer, T. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1003021 · Cited by 162 · see citing works

Brain mitochondrial dysfunction in aging, neurodegeneration and Parkinson's disease

Navarro, A. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00034 · Cited by 158 · see citing works

Mitochondrial dysfunction in glial cells: Implications for neuronal homeostasis and survival

Rose, J., Brian, C., Woods, J., Pappa, A., Panayiotidis, M. I., Powers, R., & Franco, R. (2017) · Toxicology · doi:10.1016/j.tox.2017.06.011 · Cited by 155 · see citing works

Metabolic Alterations Induced by Sucrose Intake and Alzheimer’s Disease Promote Similar Brain Mitochondrial Abnormalities

Carvalho, C., Cardoso, S., Correia, S. C., Santos, R. X., Santos, M. S., Baldeiras, I., Oliveira, C. R., & Moreira, P. I. (2012) · Diabetes · doi:10.2337/db11-1186 · Cited by 152 · see citing works

Mitochondrial contribution to lipofuscin formation

König, J., Ott, C., Hugo, M., Jung, T., Bulteau, A., Grune, T., & Höhn, A. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.017 · Cited by 151 · see citing works

A Computational Model of Motor Neuron Degeneration

Masson, G. L., Przedborski, S., & Abbott, L. F. (2014) · Neuron · doi:10.1016/j.neuron.2014.07.001 · Cited by 149 · see citing works

Hsp90 Inhibition Decreases Mitochondrial Protein Turnover

Margineantu, D. H., Emerson, C. B., Diaz, D., & Hockenbery, D. M. (2007) · PLoS ONE · doi:10.1371/journal.pone.0001066 · Cited by 147 · see citing works

Time course of high-fat diet-induced reductions in adipose tissue mitochondrial proteins: potential mechanisms and the relationship to glucose intolerance

Sutherland, L. N., Capozzi, L. C., Turchinsky, N. J., Bell, R. C., & Wright, D. C. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90408.2008 · Cited by 147 · see citing works

Neuronal circuitry regulates the response of Caenorhabditis elegans to misfolded proteins

Prahlad, V., & Morimoto, R. I. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106557108 · Cited by 143 · see citing works

The Mitochondrial Chaperone Protein TRAP1 Mitigates α-Synuclein Toxicity

Butler, E. K., Voigt, A., Lutz, A. K., Toegel, J. P., Gerhardt, E., Karsten, P., Falkenburger, B. H., Reinartz, A., Winklhofer, K. F., & Schulz, J. B. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002488 · Cited by 142 · see citing works

Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria.

Höhfeld, J., & Hartl, F. U. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.2.305 · Cited by 140 · see citing works

The small Tim proteins and the twin Cx3C motif

Koehler, C. M. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.11.003 · Cited by 139 · see citing works

High frequency of mitochondrial complex I mutations in Parkinson’s disease and aging

Smigrodzki, R. M., Parks, J. K., & Parker, W. D. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.020 · Cited by 138 · see citing works

Mammalian Copper Chaperone Cox17p Has an Essential Role in Activation of Cytochrome c Oxidase and Embryonic Development

Takahashi, Y., Kako, K., Kashiwabara, S., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.21.7614-7621.2002 · Cited by 135 · see citing works

CLPB Mutations Cause 3-Methylglutaconic Aciduria, Progressive Brain Atrophy, Intellectual Disability, Congenital Neutropenia, Cataracts, Movement Disorder

Wortmann, S. B., Ziętkiewicz, S., Kousi, M., Szklarczyk, R., Haack, T. B., Gersting, S. W., Muntau, A. C., Raković, A., Renkema, G. H., Rodenburg, R. J., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.12.013 · Cited by 131 · see citing works

Leptin regulation of Hsp60 impacts hypothalamic insulin signaling

Kleinridders, A., Lauritzen, H. P. M. M., Ussar, S., Christensen, J. H., Mori, M. A., Bross, P., & Kahn, C. R. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67615 · Cited by 130 · see citing works

Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson’s disease

Costa, A. C., Loh, S. H. Y., & Martins, L. M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2012.205 · Cited by 129 · see citing works

Human ERAL1 is a mitochondrial RNA chaperone involved in the assembly of the 28S small mitochondrial ribosomal subunit

Dennerlein, S., Rozanska, A. L., Wydro, M. M., Chrzanowska‐Lightowlers, Z. M., & Lightowlers, R. N. (2010) · Biochemical Journal · doi:10.1042/bj20100757 · Cited by 128 · see citing works

Differential Effects of Mitochondrial Heat Shock Protein 60 and Related Molecular Chaperones to Prevent Intracellular β-Amyloid-induced Inhibition of Complex IV and Limit Apoptosis

Veereshwarayya, V., Kumar, P., Rosen, K. M., Mestril, R., & Querfurth, H. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602533200 · Cited by 125 · see citing works

Activation of the mitochondrial unfolded protein response promotes longevity and dopamine neuron survival in Parkinson’s disease models

Cooper, J. F., Machiela, E., Dues, D. J., Spielbauer, K. K., Senchuk, M. M., & Raamsdonk, J. M. V. (2017) · Scientific Reports · doi:10.1038/s41598-017-16637-2 · Cited by 125 · see citing works

Increased Oxidative Stress and Mitochondrial Dysfunction in Zucker Diabetic Rat Liver and Brain

Raza, H., John, A., & Howarth, F. C. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373947 · Cited by 123 · see citing works

Familial longevity is marked by enhanced insulin sensitivity

Wijsman, C. A., Rozing, M. P., Streefland, T. C. M., le Cessie, S., Mooijaart, S. P., Slagboom, P. E., Westendorp, R. G. J., Pijl, H., van Heemst, D., & On behalf of the Leiden Longevity Study group (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00650.x · Cited by 120 · see citing works

Somatic mitochondrial DNA mutations in cortex and substantia nigra in aging and Parkinson’s disease

Simon, D. K., Lin, M. T., Zheng, L., Liu, G.-J., Ahn, C. H., Kim, L. M., Mauck, W. M., Twu, F., Beal, M. F., & Johns, D. R. (2004) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00037-x · Cited by 118 · see citing works

Absence of BiP Co-chaperone DNAJC3 Causes Diabetes Mellitus and Multisystemic Neurodegeneration

Synofzik, M., Haack, T. B., Kopajtich, R., Gorza, M., Rapaport, D., Greiner, M., Schönfeld, C., Freiberg, C., Schorr, S., Holl, R. W., et al. (2014) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.10.013 · Cited by 118 · see citing works

Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis

Kardon, J. R., Yien, Y. Y., Huston, N. C., Branco, D. S., Hildick-Smith, G. J., Rhee, K. Y., Paw, B. H., & Baker, T. A. (2015) · Cell · doi:10.1016/j.cell.2015.04.017 · Cited by 116 · see citing works

Mitochondrial stress: A bridge between mitochondrial dysfunction and metabolic diseases?

Hu, F., & Liu, F. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.008 · Cited by 112 · see citing works

TRAP1 rescues PINK1 loss-of-function phenotypes

Zhang, L., Karsten, P., Hamm, S., Pogson, J. H., Müller-Rischart, A. K., Exner, N., Haass, C., Whitworth, A. J., Winklhofer, K. F., Schulz, J. B., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt132 · Cited by 109 · see citing works

Cellular Regulation of Amyloid Formation in Aging and Disease

Stroo, E., Koopman, M., Nollen, E. A. A., & Mata‐Cabana, A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00064 · Cited by 108 · see citing works

Dysregulation of autophagy and mitochondrial function in Parkinson’s disease

Wang, B., Abraham, N. A., Gao, G., & Yang, Q. (2016) · Translational Neurodegeneration · doi:10.1186/s40035-016-0065-1 · Cited by 106 · see citing works

Crosstalk between Lysosomes and Mitochondria in Parkinson's Disease

Plotegher, N., & Duchen, M. R. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00110 · Cited by 106 · see citing works

Insulin Receptor Signaling in POMC, but Not AgRP, Neurons Controls Adipose Tissue Insulin Action

Shin, A. C., Filatova, N., Lindtner, C., Chi, T., Degann, S., Oberlin, D. J., & Buettner, C. (2017) · Diabetes · doi:10.2337/db16-1238 · Cited by 105 · see citing works

Hsp90 Functions in the Targeting and Outer Membrane Translocation Steps of Tom70-mediated Mitochondrial Import

Fan, A. C. Y., Bhangoo, M. K., & Young, J. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605250200 · Cited by 103 · see citing works

Loss of mitochondrial protease ClpP protects mice from diet‐induced obesity and insulin resistance

Bhaskaran, S., Pharaoh, G. A., Ranjit, R., Murphy, A., Matsuzaki, S., Nair, B. C., Forbes, B., Gispert, S., Auburger, G. W. J., Humphries, K. M., et al. (2018) · EMBO Reports · doi:10.15252/embr.201745009 · Cited by 103 · see citing works

Mitochondrial proteolytic stress induced by loss of mortalin function is rescued by Parkin and PINK1

Burbulla, L. F., Fitzgerald, J. C., Stegen, K., Westermeier, J., Thost, A.-K., Kato, H., Mokranjac, D., Sauerwald, J., Martins, L. M., Woitalla, D., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.103 · Cited by 97 · see citing works

The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria.

Schmitt, M., Neupert, W., & Langer, T. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.6.1375 · Cited by 96 · see citing works

ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1 leads to mitochondrial dysfunction and growth retardation

Uchiumi, T., Ohgaki, K., Yagi, M., Aoki, Y., Sakai, A., Matsumoto, S., & Kang, D. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq305 · Cited by 96 · see citing works

Brain Insulin-Like Growth Factor and Neurotrophin Resistance in Parkinson's Disease and Dementia with Lewy Bodies: Potential Role of Manganese Neurotoxicity

Tong, M., Dong, M., & de la Monte, S. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0995 · Cited by 95 · see citing works

Dysregulation of parkin in the substantia nigra of db/db and high-fat diet mice

Khang, R., Park, C., & Shin, J.-H. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.03.017 · Cited by 93 · see citing works

The impact of dietary energy intake on cognitive aging

Mattson, M. P. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/neuro.24.005.2010 · Cited by 91 · see citing works

Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis

Uhrigshardt, H., Singh, A., Kovtunovych, G., Ghosh, M. C., & Rouault, T. A. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq301 · Cited by 91 · see citing works

The association between insulin resistance and depression in the Korean general population

Lee, J.-H., Park, S. K., Ryoo, J., Oh, C., Mansur, R. B., Alfonsi, J., Cha, D. S., Lee, Y. L., McIntyre, R. S., & Jung, J. Y. (2016) · Journal of Affective Disorders · doi:10.1016/j.jad.2016.10.027 · Cited by 89 · see citing works

Mitochondrial Heat Shock Protein (Hsp) 70 and Hsp10 Cooperate in the Formation of Hsp60 Complexes

Böttinger, L., Oeljeklaus, S., Guiard, B., Rospert, S., Warscheid, B., & Becker, T. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.642017 · Cited by 81 · see citing works

Cellular Links between Neuronal Activity and Energy Homeostasis

Shetty, P. K., Galeffi, F., & Turner, D. A. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00043 · Cited by 80 · see citing works

Decreased expression of the mitochondrial matrix proteases Lon and ClpP in cells from a patient with hereditary spastic paraplegia (SPG13)

Hansen, J., Corydon, T. J., Palmfeldt, J., Dürr, A., Fontaine, B., Nielsen, M. N., Christensen, J., Gregersen, N. V., & Bross, P. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.070 · Cited by 79 · see citing works

Measures of striatal insulin resistance in a 6-hydroxydopamine model of Parkinson's disease

Morris, J. K., Zhang, H., Gupte, A. A., Bomhoff, G. L., Stanford, J. A., & Geiger, P. C. (2008) · Brain Research · doi:10.1016/j.brainres.2008.08.089 · Cited by 79 · see citing works

A homozygous missense mutation in ERAL1, encoding a mitochondrial rRNA chaperone, causes Perrault syndrome

Chatzispyrou, I. A., Alders, M. M., Guerrero‐Castillo, S., Perez, R. Z., Haagmans, M. A., Mouchiroud, L., Koster, J., Ofman, R., Baas, F., Waterham, H. R., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx152 · Cited by 79 · see citing works

Mutational screening of the mortalin gene (HSPA9) in Parkinson’s disease

de Mena, L., Coto, E., Sánchez-Ferrero, E., Ribacoba, R., Guisasola, L. M., Salvador, C., Estrada, M. B., & Álvarez, V. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0273-2 · Cited by 75 · see citing works

CLPB Variants Associated with Autosomal-Recessive Mitochondrial Disorder with Cataract, Neutropenia, Epilepsy, and Methylglutaconic Aciduria

Saunders, C., Smith, L. D., Wibrand, F., Ravn, K., Bross, P., Thiffault, I., Christensen, M., Atherton, A. M., Farrow, E., Miller, N., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.12.020 · Cited by 73 · see citing works

ClpX stimulates the mitochondrial unfolded protein response (UPRmt) in mammalian cells

Al-Furoukh, N., Ianni, A., Nolte, H., Hölper, S., Krüger, M., Wanrooij, S., & Braun, T. W. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.06.016 · Cited by 71 · see citing works

Higher levels of heat shock proteins in longer-lived mammals and birds

Salway, K. D., Gallagher, E. J., Page, M. M., & Stuart, J. A. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.06.002 · Cited by 70 · see citing works

Intrathecal heat shock protein 60 mediates neurodegeneration and demyelination in the CNS through a TLR4- and MyD88-dependent pathway

Rosenberger, K., Dembny, P., Derkow, K., Engel, O., Krüger, C., Wolf, S. A., Kettenmann, H., Schott, E., Meisel, A., & Lehnardt, S. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0003-1 · Cited by 70 · see citing works

Deletion of the Mitochondrial Chaperone TRAP-1 Uncovers Global Reprogramming of Metabolic Networks

Lisanti, S., Tavecchio, M., Chae, Y. C., Liu, Q., Brice, A. K., Thakur, M. L., Languino, L. R., & Altieri, D. C. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.061 · Cited by 68 · see citing works

Cytochrome c oxidase deficiency accelerates mitochondrial apoptosis by activating ceramide synthase 6

Schüll, S., Günther, S. D., Brodesser, S., Seeger, J. M., Tosetti, B., Wiegmann, K., Pongratz, C., Díaz, F., Witt, A., Andree, M., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.62 · Cited by 67 · see citing works

Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain

Zhang, Y., Appleton, B. A., Wu, P., Wiesmann, C., & Sidhu, S. S. (2007) · Protein Science · doi:10.1110/ps.072833207 · Cited by 66 · see citing works

Knockdown of Human COX17 Affects Assembly and Supramolecular Organization of Cytochrome c Oxidase

Oswald, C., Krause‐Buchholz, U., & Rödel, G. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.034 · Cited by 60 · see citing works

CLPP deficiency protects against metabolic syndrome but hinders adaptive thermogenesis

Becker, C., Kukat, A., Szczepanowska, K., Hermans, S., Senft, K., Brandscheid, C. P., Maiti, P., & Trifunovic, A. (2018) · The EMBO Reports · doi:10.15252/embr.201745126 · Cited by 60 · see citing works

Tid1, a Cochaperone of the Heat Shock 70 Protein and the Mammalian Counterpart of the Drosophila Tumor Suppressor l(2)tid, Is Critical for Early Embryonic Development and Cell Survival

Lo, J., Hayashi, M., Woo-Kim, S., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2226-2236.2004 · Cited by 58 · see citing works

Analysis of HSPA8 and HSPA9 mRNA Expression and Promoter Methylation in the Brain and Blood of Alzheimer's Disease Patients

Silva, P. N., Furuya, T. K., Braga, I. L. S., Rasmussen, L. T., de Lábio, R. W., Bertolucci, P. H. F., Chen, E., Turecki, G., Mechawar, N., Payão, S. L. M., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130428 · Cited by 55 · see citing works

Novel variant Pro143Ala in HTRA2 contributes to Parkinson’s disease by inducing hyperphosphorylation of HTRA2 protein in mitochondria

Lin, C., Chen, M., Chen, G. S., Tai, C., & Wu, R. (2011) · Human Genetics · doi:10.1007/s00439-011-1041-6 · Cited by 53 · see citing works

Metabolism Regulates the Spontaneous Firing of Substantia Nigra Pars Reticulata Neurons via KATPand Nonselective Cation Channels

Lutas, A., Birnbaumer, L., & Yellen, G. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-14.2014 · Cited by 50 · see citing works

Effects of a Mutation in the HSPE1 Gene Encoding the Mitochondrial Co-chaperonin HSP10 and Its Potential Association with a Neurological and Developmental Disorder

Bie, A. S., Guerra, P. F., Birkler, R. I. D., Nisemblat, S., Pelnēna, D., Lu, X., Deignan, J. L., Lee, H., Dorrani, N., Corydon, T. J., et al. (2016) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2016.00065 · Cited by 49 · see citing works

Dynamin-Related Protein 1-Dependent Mitochondrial Fission Changes in the Dorsal Vagal Complex Regulate Insulin Action

Filippi, B., Abraham, M. A., Silva, P. N., Rasti, M., LaPierre, M. P., Bauer, P. V., Rocheleau, J. V., & Lam, T. K. T. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.035 · Cited by 48 · see citing works

Heat shock protein 60: an endogenous inducer of dopaminergic cell death in Parkinson disease

Noelker, C., Morel, L. J., Osterloh, A., Alvarez‐Fischer, D., Lescot, T., Breloer, M., Gold, M., Oertel, W. H., Henze, C., Michel, P. P., et al. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-86 · Cited by 44 · see citing works

Hsp78 chaperone functions in restoration of mitochondrial network following heat stress

Lewandowska, A., Gierszewska, M., Marszałek, J., et al. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.01.007 · Cited by 43 · see citing works

Essential Role of TID1 in Maintaining Mitochondrial Membrane Potential Homogeneity and Mitochondrial DNA Integrity

Ng, A. C.-H., Baird, S. D., & Screaton, R. A. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01021-13 · Cited by 41 · see citing works

Hippocampal insulin resistance links maternal obesity with impaired neuronal plasticity in adult offspring

Schmitz, L., Kuglin, R., Bae‐Gartz, I., Janoschek, R., Appel, S., Mesaros, A., Jakovčevski, I., Vohlen, C., Handwerk, M., Ensenauer, R. E., et al. (2017) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2017.12.023 · Cited by 41 · see citing works

TRAP1 Controls Mitochondrial Fusion/Fission Balance through Drp1 and Mff Expression

Takamura, H., Koyama, Y., Matsuzaki, S., Yamada, K., Hattori, T., Miyata, S., Takemoto, K., Tohyama, M., & Katayama, T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051912 · Cited by 39 · see citing works

Modulation of Molecular Chaperones in Huntington’s Disease and Other Polyglutamine Disorders

Reis, S., Pinho, B. R., & Oliveira, J. M. A. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0120-z · Cited by 36 · see citing works

Characterization of Human SCO1 and COX17 Genes in Mitochondrial Cytochrome-c-Oxidase Deficiency

Horváth, R., Lochmüller, H., Stucka, R., et al. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3495 · Cited by 35 · see citing works

Mitochondrial Dysfunction, Proteotoxicity, and Aging

Hipkiss, A. R. (2010) · Advances in clinical chemistry · doi:10.1016/s0065-2423(10)50007-6 · Cited by 35 · see citing works

Mitochondrial dysfunction, proteotoxicity, and aging: causes or effects, and the possible impact of NAD+-controlled protein glycation.

Hipkiss, A. R. (2010) · PubMed · Cited by 34 · see citing works

Stimulatory Effect of Insulin on Glucose Uptake by Muscle Involves the Central Nervous System in Insulin-Sensitive Mice

Coomans, C. P., Biermasz, N. R., Geerling, J. J., Guigas, B., Rensen, P. C. N., Havekes, L. M., & Romijn, J. A. (2011) · Diabetes · doi:10.2337/db10-1100 · Cited by 26 · see citing works

A Mutation in the Flavin Adenine Dinucleotide-Dependent Oxidoreductase FOXRED1 Results in Cell-Type-Specific Assembly Defects in Oxidative Phosphorylation Complexes I and II

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Lappalainen, Z., Lappalainen, J., Oksala, N., et al. (2010) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2008.00872.x · Cited by 19 · see citing works

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Tytell, M., Davis, A., Giles, J. M., Snider, L. C., Xiao, R., Dozier, S., Presley, T. D., & Kavanagh, K. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0835-4 · Cited by 14 · see citing works

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Parlevliet, E. T., Coomans, C. P., Rensen, P. C. N., & Romijn, J. A. (2014) · Frontiers of hormone research · doi:10.1159/000358314 · Cited by 10 · see citing works

Untitled work

(1996) · doi:10.1379/1466-1268(1996)001

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Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85 · see citing works

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Gaurav, S. K., & Swarnkar, P. (2017) · International research journal of multidisciplinary studies

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Кенжебaевa, У., Nadirova, G. E., & Seitmetova, Z. (2018) · DOAJ (DOAJ: Directory of Open Access Journals)

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