Mitochondria

Molecular characterization of mitochondrial apoptosis-inducing factor

Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060

Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178

The Combined Functions of Proapoptotic Bcl-2 Family Members Bak and Bax Are Essential for Normal Development of Multiple Tissues

Lindsten, T., Ross, A. J., King, A., Zong, W.-X., Rathmell, J. C., Shiels, H. A., Ulrich, E., Waymire, K. G., Mahar, P., Frauwirth, K., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00136-2 · Cited by 1,489

Generation of reactive oxygen species by the mitochondrial electron transport chain

Liu, Y., Fiskum, G., & Schubert, D. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00744.x · Cited by 1,260

Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis

Marzo, I., Brenner, C., Zamzami, N., Jürgensmeier, J. M., Susin, S. A., Vieira, H. L. A., Prévost, M.-C., Xie, Z., Matsuyama, S., Reed, J. C., et al. (1998) · Science · doi:10.1126/science.281.5385.2027 · Cited by 1,168

Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis

Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200209124 · Cited by 846

Free radicals and antioxidants in normal physiological functions and human disease

Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269

Nitric Oxide and Peroxynitrite in Health and Disease

Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390

Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases

Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792

Mechanisms of Pancreatic β-Cell Death in Type 1 and Type 2 Diabetes

Cnop, M., Welsh, N., Jonas, J.-C., Jörns, A., Lenzen, S., & Eizirik, D. L. (2005) · Diabetes · doi:10.2337/diabetes.54.suppl_2.s97 · Cited by 1,491

Chemical Inhibition of the Mitochondrial Division Dynamin Reveals Its Role in Bax/Bak-Dependent Mitochondrial Outer Membrane Permeabilization

Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200

BH3 Domains of BH3-Only Proteins Differentially Regulate Bax-Mediated Mitochondrial Membrane Permeabilization Both Directly and Indirectly

Kuwana, T., Bouchier-Hayes, L., Chipuk, J. E., Bonzon, C., Sullivan, B. A., Green, D. R., & Newmeyer, D. D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.003 · Cited by 1,185

The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus

Eizirik, D. L., Cardozo, A. K., & Cnop, M. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0015 · Cited by 1,173

Supporting aspartate biosynthesis is an essential function of respiration in proliferating cells

Sullivan, L. B., Gui, D. Y., Hosios, A. M., Bush, L. N., Freinkman, E., & Vander Heiden, M. G. (2015) · Cell · doi:10.1016/j.cell.2015.07.017 · Cited by 1,173

Estrogens and androgens in skeletal physiology and pathophysiology

Almeida, M., Laurent, M. R., Dubois, V., Claessens, F., O'Brien, C. A., Bouillon, R., Vanderschueren, D., & Manolagas, S. C. (2017) · Physiological Reviews · doi:10.1152/physrev.00033.2015 · Cited by 860

MicroRNA-21 Targets a Network of Key Tumor-Suppressive Pathways in Glioblastoma Cells

Papagiannakopoulos, T., Shapiro, A., & Kosik, K. S. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1305 · Cited by 705

Mitochondrial DNA mutations and human disease

Tuppen, H. A. L., Blakely, E. L., Turnbull, D. M., & Taylor, R. W. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.09.005 · Cited by 676

Mitochondrial point mutations do not limit the natural lifespan of mice

Vermulst, M., Bielas, J. H., Kujoth, G. C., Ladiges, W. C., Rabinovitch, P. S., Prolla, T. A., & Loeb, L. A. (2007) · Nature Genetics · doi:10.1038/ng1988 · Cited by 404

Mitochondria: diversity in the regulation of the NLRP3 inflammasome

Gurung, P., Lukens, J. R., & Kanneganti, T.-D. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.11.008 · Cited by 393

Peroxiredoxin III, a Mitochondrion-specific Peroxidase, Regulates Apoptotic Signaling by Mitochondria

Chang, T.-S., Cho, C.-S., Park, S., Yu, S., Kang, S. W., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407707200 · Cited by 388

Control of mitochondrial permeability by Bcl-2 family members

Sharpe, J. C., Arnoult, D., & Youle, R. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2003.10.016 · Cited by 367

Diabetes and the Impairment of Reproductive Function: Possible Role of Mitochondria and Reactive Oxygen Species

Ramalho-Santos, J., Amaral, S., & Oliveira, P. (2008) · Current Diabetes Reviews · doi:10.2174/157339908783502398 · Cited by 359

The Protein Import Machinery of Mitochondria

Wiedemann, N., Frazier, A. E., & Pfanner, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400003200 · Cited by 336

Amyloid β-induced Changes in Nitric Oxide Production and Mitochondrial Activity Lead to Apoptosis

Keil, U., Bonert, A., Marques, C. A., Scherping, I., Weyermann, J., Strosznajder, J. B., Müller-Spahn, F., Haass, C., Czech, C., Pradier, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405600200 · Cited by 287

The ROS production induced by a reverse-electron flux at respiratory-chain complex 1 is hampered by metformin

Batandier, C., Guigas, B., Detaille, D., El-Mir, M., Fontaine, E., Rigoulet, M., & Leverve, X. M. (2006) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9003-8 · Cited by 279

Toxicity of statins on rat skeletal muscle mitochondria

Kaufmann, P., Török, M., Zahno, A., Waldhauser, K. M., Brecht, K., & Krähenbühl, S. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6235-z · Cited by 263

Nicastrin, Presenilin, APH-1, and PEN-2 Form Active γ-Secretase Complexes in Mitochondria

Hansson, C. A., Frykman, S., Farmery, M. R., Tjernberg, L. O., Nilsberth, C., Pursglove, S. E., Ito, A., Winblad, B., Cowburn, R. F., Thyberg, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404500200 · Cited by 256

An interconnected hierarchical model of cell death regulation by the BCL-2 family

Chen, H.-C., Kanai, M., Inoue-Yamauchi, A., Tu, H.-C., Huang, Y., Ren, D., Kim, H., Takeda, S., Reyna, D. E., Chan, P. M., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3236 · Cited by 249

SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability Transition Pore

Shanmughapriya, S., Rajan, S., Hoffman, N. E., Higgins, A. M., Tomar, D., Nemani, N., Hines, K. J., Smith, D. J., Eguchi, A., Vallem, S., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.009 · Cited by 209

Mitochondrial membrane permeability transition and cell death

Tsujimoto, Y., Nakagawa, T., & Shimizu, S. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.017 · Cited by 188

Accelerated evolution of the electron transport chain in anthropoid primates

Grossman, L. I., Wildman, D. E., Schmidt, T. R., & Goodman, M. (2004) · Trends in Genetics · doi:10.1016/j.tig.2004.09.002 · Cited by 186

Mitochondrial function and myocardial aging. A critical analysis of the role of permeability transition

DILISA, F., & BERNARDI, P. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.02.009 · Cited by 139

Cardiolipin Remodeling in the Heart

Sparagna, G. C., & Lesnefsky, E. J. (2009) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e31819b5461 · Cited by 128

Lifespan and mitochondrial control of neurodegeneration

Wright, A. F., Jacobson, S. G., Cideciyan, A. V., Roman, A. J., Shu, X., Vlachantoni, D., McInnes, R. R., & Riemersma, R. A. (2004) · Nature Genetics · doi:10.1038/ng1448 · Cited by 111

ER-Mitochondria Communication. How Privileged?

Franzini-Armstrong, C. (2007) · Physiology · doi:10.1152/physiol.00017.2007 · Cited by 109

Mitochondrial calcium cycling in neuronal function and neurodegeneration

Walters, G. C., & Usachev, Y. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094356 · Cited by 105

Plin4-Dependent Lipid Droplets Hamper Neuronal Mitophagy in the MPTP/p-Induced Mouse Model of Parkinson’s Disease

Han, X., Zhu, J., Zhang, X., Song, Q., Ding, J., Lu, M., Sun, S., & Hu, G. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00397 · Cited by 91

Effects of ginseng saponins isolated from red ginseng on ultraviolet B-induced skin aging in hairless mice

Kim, Y. G., Sumiyoshi, M., Sakanaka, M., & Kimura, Y. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.11.021 · Cited by 88

Dynamin-related protein 1 mediates high glucose induced pancreatic beta cell apoptosis

Men, X., Wang, H., Li, M., Cai, H., Xu, S., Zhang, W., Xu, Y., Ye, L., Yang, W., Wollheim, C. B., et al. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.031 · Cited by 83

Human papillomavirus type 16 E5 protein inhibits hydrogen-peroxide-induced apoptosis by stimulating ubiquitin-proteasome-mediated degradation of Bax in human cervical cancer cells

Oh, J.-M., Kim, S.-H., Cho, E.-A., Song, Y.-S., Kim, W.-H., & Juhnn, Y.-S. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp318 · Cited by 80

HIV TAT-mediated microglial senescence: Role of SIRT3-dependent mitochondrial oxidative stress

Thangaraj, A., Chivero, E. T., Tripathi, A., Singh, S., Niu, F., Guo, M.-L., Pillai, P., Periyasamy, P., & Buch, S. (2021) · Redox Biology · doi:10.1016/j.redox.2020.101843 · Cited by 76

Function of Cytosolic Chaperones in Tom70-Mediated Mitochondrial Import

C.Y. Fan, A., & C. Young, J. (2011) · Protein & Peptide Letters · doi:10.2174/092986611794475020 · Cited by 64

High-performance liquid chromatography-based methods of enzymatic analysis: electron transport chain activity in mitochondria from human skeletal muscle

Ritov, V. B., Menshikova, E. V., & Kelley, D. E. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.05.014 · Cited by 52

MiR-182-5p protects inner ear hair cells from cisplatin-induced apoptosis by inhibiting FOXO3a

Li, Y., Li, A., Wu, J., He, Y., Yu, H., Chai, R., & Li, H. (2016) · Cell Death & Disease · doi:10.1038/cddis.2016.246 · Cited by 46

The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID

Fernández‐Marrero, Y., Bleicken, S., Das, K. K., Bachmann, D., Kaufmann, T., & Garcia‐Saez, A. J. (2017) · The FEBS Journal · doi:10.1111/febs.14008 · Cited by 47

Protective Role of Mitochondrial Peroxiredoxin III against UVB-Induced Apoptosis of Epidermal Keratinocytes

Baek, J. Y., Park, S., Park, J., Jang, J. Y., Wang, S. B., Kim, S. R., Woo, H. A., Lim, K. M., & Chang, T.-S. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.01.027 · Cited by 43

Mitochondrial targeted β-lapachone induces mitochondrial dysfunction and catastrophic vacuolization in cancer cells

Ma, J., Lim, C., Sacher, J. R., Van Houten, B., Qian, W., & Wipf, P. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.06.073 · Cited by 27

Mitochondrial Transmembrane Potential and Reactive Oxygen Species Generation Regulate the Enhanced Effect of CCCP on TRAIL-Induced SNU-638 Cell Apoptosis

CHAUDHARI, A. A., SEOL, J.-W., KANG, S.-J., & PARK, S.-Y. (2008) · Journal of Veterinary Medical Science · doi:10.1292/jvms.70.537 · Cited by 22