Mitochondrial Proteolysis and Metabolic Control

Mitochondrial Fission, Fusion, and Stress

Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works

Journal of Biological Chemistry

Kurkinensp, M., CondongT, M. R., Blumberg, B., Barlow, D. P., Quiñones, S., Sausg, J., & Pihlajaniemisyy, T. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc · Cited by 3,409 · see citing works

The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease

Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310 · see citing works

During autophagy mitochondria elongate, are spared from degradation and sustain cell viability

Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735 · see citing works

Mitochondrial transcription factor A is necessary for mtDNA maintance and embryogenesis in mice

Larsson, N.-G., Wang, J., Wilhelmsson, H., Oldfors, A., Rustin, P., Lewandoski, M., Barsh, G. S., & Clayton, D. A. (1998) · Nature Genetics · doi:10.1038/ng0398-231 · Cited by 1,594 · see citing works

Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy

Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446 · see citing works

Mitochondrial Dynamics Controls T Cell Fate through Metabolic Programming

Buck, M. D., O’Sullivan, D., Geltink, R. I. K., Curtis, J. D., Chang, C., Sanin, D. E., Qiu, J., Kretz, O., Braas, D., van der Windt, G. J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.035 · Cited by 1,444 · see citing works

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL

Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works

OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28

Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330 · see citing works

Mitochondrial Dynamics and Metabolic Regulation

Wai, T., & Langer, T. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.12.001 · Cited by 1,304 · see citing works

HIF-1 Regulates Cytochrome Oxidase Subunits to Optimize Efficiency of Respiration in Hypoxic Cells

Fukuda, R., Zhang, H., Kim, J.-W., Shimoda, L., Dang, C. V., & Semenza, G. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.047 · Cited by 1,225 · see citing works

Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation

Rambold, A. S., Kostelecky, B., Elia, N., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107402108 · Cited by 1,144 · 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

Mitochondrial transcription factor A regulates mtDNA copy number in mammals

Ekstrand, M. I. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh109 · Cited by 919 · see citing works

Lipids of mitochondria

Horvath, S. E., & Daum, G. (2013) · Progress in Lipid Research · doi:10.1016/j.plipres.2013.07.002 · Cited by 906 · see citing works

Regulation of mitochondrial morphology through proteolytic cleavage of OPA1

Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899 · see citing works

The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy

Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., Foreman, O., Kirkpatrick, D. S., & Sheng, M. (2014) · Nature · doi:10.1038/nature13418 · Cited by 855 · see citing works

Spastic Paraplegia and OXPHOS Impairment Caused by Mutations in Paraplegin, a Nuclear-Encoded Mitochondrial Metalloprotease

Casari, G., Fusco, M. D., Ciarmatori, S., Zeviani, M., Mora, M., Fernández‐Silva, P., Michele, G. D., Filla, A., Cocozza, S., Marconi, R., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81203-9 · Cited by 826 · see citing works

The <i>i</i> -AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission

Anand, R., Wai, T., Baker, M. J., Kladt, N., Schauss, A. C., Rugarli, E., & Langer, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201308006 · Cited by 812 · see citing works

Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment

Greene, A. W., Grenier, K., Aguileta, M. A., Muise, S., Farazifard, R., Haque, M. E., McBride, H. M., Park, D. S., & Fon, E. A. (2012) · The EMBO Reports · doi:10.1038/embor.2012.14 · Cited by 711 · cited 2× · see citing works

PINK1 is degraded through the N-end rule pathway

Yamano, K., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.24633 · Cited by 669 · see citing works

Proteomic Discovery of Cellular Substrates of the ClpXP Protease Reveals Five Classes of ClpX-Recognition Signals

Flynn, J. M., Neher, S. B., Kim, Y., Sauer, R. T., & Baker, T. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00060-1 · Cited by 605 · see citing works

A Regulatory Signaling Loop Comprising the PGAM5 Phosphatase and CK2 Controls Receptor-Mediated Mitophagy

Chen, G., Han, Z., Feng, D., Chen, Y., Chen, L., Wu, H., Huang, L., Zhou, C., Cai, X., Fu, C., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.034 · Cited by 600 · see citing works

ClpP Mediates Activation of a Mitochondrial Unfolded Protein Response in C. elegans

Haynes, C. M., Petrova, K., Benedetti, C., Yang, Y., & Ron, D. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.016 · Cited by 595 · see citing works

Imbalanced OPA1 processing and mitochondrial fragmentation cause heart failure in mice

Wai, T., García-Prieto, J., Baker, M. J., Merkwirth, C., Benit, P., Rustin, P., Rupérez, F. J., Barbas, C., Ibañez, B., & Langer, T. (2015) · Science · doi:10.1126/science.aad0116 · Cited by 551 · see citing works

New roles for mitochondrial proteases in health, ageing and disease

Quirós, P. M., Langer, T., & López-Otı́n, C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3984 · Cited by 546 · see citing works

Bcl-2-like protein 13 is a mammalian Atg32 homologue that mediates mitophagy and mitochondrial fragmentation

Murakawa, T., Yamaguchi, O., Hashimoto, A., Hikoso, S., Takeda, T., Oka, T., Yasui, H., Ueda, H., Akazawa, Y., Nakayama, H., et al. (2015) · Nature Communications · doi:10.1038/ncomms8527 · Cited by 521 · see citing works

Multiple dynamin family members collaborate to drive mitochondrial division

Lee, J. E., Westrate, L. M., Wu, H., Page, C., & Voeltz, G. K. (2016) · Nature · doi:10.1038/nature20555 · Cited by 512 · see citing works

Proteolytic Cleavage of Opa1 Stimulates Mitochondrial Inner Membrane Fusion and Couples Fusion to Oxidative Phosphorylation

Mishra, P., Carelli, V., Manfredi, G., & Chan, D. C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.011 · Cited by 473 · see citing works

The Opa1-Dependent Mitochondrial Cristae Remodeling Pathway Controls Atrophic, Apoptotic, and Ischemic Tissue Damage

Varanita, T., Soriano, M. E., Romanello, V., Zaglia, T., Quintana-Cabrera, R., Semenzato, M., Menabò, R., Costa, V., Civiletto, G., Pesce, P., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.007 · Cited by 460 · see citing works

Mitochondrial Dynamics in Regulating the Unique Phenotypes of Cancer and Stem Cells

Chen, H., & Chan, D. C. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.05.016 · Cited by 445 · see citing works

Mitochondrial processing peptidases

Gakh, O., Cavadini, P., & Isaya, G. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(02)00265-3 · Cited by 436 · see citing works

The Mitochondrial Transcription Factor TFAM Coordinates the Assembly of Multiple DNA Molecules into Nucleoid-like Structures

Kaufman, B. A., Durisic, N., Mativetsky, J. M., Costantino, S., Hancock, M. A., Grütter, P., & Shoubridge, E. A. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-05-0404 · Cited by 431 · see citing works

OPA1 processing in cell death and disease – the long and short of it

MacVicar, T., & Langer, T. (2016) · Journal of Cell Science · doi:10.1242/jcs.159186 · Cited by 420 · see citing works

The three ‘P’s of mitophagy: PARKIN.; PINK1.; and post-translational modifications

Durcan, T. M., & Fon, E. A. (2015) · Genes &amp; Development · doi:10.1101/gad.262758.115 · Cited by 400 · see citing works

The m-AAA Protease Defective in Hereditary Spastic Paraplegia Controls Ribosome Assembly in Mitochondria

Nolden, M., Ehses, S., Koppen, M., Bernacchia, A., Rugarli, E. I., & Langer, T. (2005) · Cell · doi:10.1016/j.cell.2005.08.003 · Cited by 398 · see citing works

Processing of Mgm1 by the Rhomboid-type Protease Pcp1 Is Required for Maintenance of Mitochondrial Morphology and of Mitochondrial DNA

Herlan, M., Vogel, F., Bornhövd, C., Neupert, W., & Reichert, A. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211311200 · Cited by 378 · see citing works

The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking

Meißner, C., Lorenz, H., Weihofen, A., Selkoe, D. J., & Lemberg, M. K. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07253.x · Cited by 375 · see citing works

Stress‐induced OMA1 activation and autocatalytic turnover regulate OPA1‐dependent mitochondrial dynamics

Baker, M. J., Lampe, P., Stojanovski, D., Korwitz, A., Anand, R., Tatsuta, T., & Langer, T. (2014) · The EMBO Journal · doi:10.1002/embj.201386474 · Cited by 346 · see citing works

Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28

Bella, D. D., Lazzaro, F., Brusco, A., Plumari, M., Battaglia, G. S., Pastore, A., Finardi, A., Cagnoli, C., Tempia, F., Frontali, M., et al. (2010) · Nature Genetics · doi:10.1038/ng.544 · Cited by 345 · see citing works

Circadian Control of DRP1 Activity Regulates Mitochondrial Dynamics and Bioenergetics

Schmitt, K., Grimm, A., Dallmann, R., Oettinghaus, B., Restelli, L. M., Witzig, M., Ishihara, N., Mihara, K., Ripperger, J. A., Albrecht, U., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.011 · Cited by 336 · see citing works

Programmed mitophagy is essential for the glycolytic switch during cell differentiation

Esteban‐Martínez, L., Sierra‐Filardi, E., McGreal, R., Salazar‐Roa, M., Mariño, G., Seco, E., Durand, S., Enot, D. P., Graña‐Castro, O., Malumbres, M., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201695916 · Cited by 333 · see citing works

USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria

Cunningham, C. N., Baughman, J. M., Phu, L., Tea, J. S., Yu, C., Coons, M. M., Kirkpatrick, D. S., Bingol, B., & Corn, J. E. (2015) · Nature Cell Biology · doi:10.1038/ncb3097 · Cited by 329 · see citing works

Structures of mitochondrial oxidative phosphorylation supercomplexes and mechanisms for their stabilisation

Chaban, Y. L., Boekema, E. J., & Dudkina, N. V. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.004 · Cited by 321 · see citing works

Phosphorylation of Human TFAM in Mitochondria Impairs DNA Binding and Promotes Degradation by the AAA+ Lon Protease

Lü, B., Lee, J., Nie, X., Li, M., Morozov, Y. I., Venkatesh, S., Bogenhagen, D. F., Temiakov, D., & Suzuki, C. K. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.10.023 · Cited by 320 · see citing works

Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM)

Matsushima, Y., Goto, Y.-I., & Kaguni, L. S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008924107 · Cited by 294 · 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 and PFKFB3 mediate glycolysis and survival in response to mitophagy during mitotic arrest

Domènech, E. B., Maestre, C., Esteban‐Martínez, L., Partida, D., Pascual, R., Fernández‐Miranda, G., Seco, E., Campos‐Olivas, R., Pérez‐Martínez, M., Megı́as, D., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3231 · Cited by 267 · see citing works

The PERK Arm of the Unfolded Protein Response Regulates Mitochondrial Morphology during Acute Endoplasmic Reticulum Stress

Lebeau, J., Saunders, J. M., Moraes, V., Madhavan, A., Madrazo, N., Anthony, M. C., & Wiseman, R. L. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.055 · Cited by 267 · see citing works

Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian dysgenesis and sensorineural hearing loss of Perrault syndrome

Pierce, S. B., Chisholm, K. M., Lynch, E. D., Lee, M. K., Walsh, T., Opitz, J. M., Li, W., Klevit, R. E., & King, M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103471108 · Cited by 255 · see citing works

The constriction and scission machineries involved in mitochondrial fission

Kraus, F., & Ryan, M. T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199562 · Cited by 244 · see citing works

OPA1 Isoforms in the Hierarchical Organization of Mitochondrial Functions

Dotto, V. D., Mishra, P., Vidoni, S., Fogazza, M., Maresca, A., Caporali, L., McCaffery, J. M., Cappelletti, M., Baruffini, E., Lenaers, G., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.073 · Cited by 243 · see citing works

Mitochondrial dynamics and disease, OPA1

Olichon, A., Guillou, E., Delettre, C., Landes, T., Pelloquin, L., Emorine, L. J., Mils, V., Daloyau, M., Hamel, C., Amati‐Bonneau, P., et al. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.04.003 · Cited by 238 · see citing works

ATP-Dependent Lon Protease Controls Tumor Bioenergetics by Reprogramming Mitochondrial Activity

Quirós, P. M., Español, Y., Acín-Pérez, R., Rodríguez, F., Bárcena, C., Watanabe, K., Calvo, E., Loureiro, M., Fernández-García, M. S., Fueyo, A., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.018 · Cited by 233 · see citing works

Intramitochondrial Transport of Phosphatidic Acid in Yeast by a Lipid Transfer Protein

Connerth, M., Tatsuta, T., Haag, M., Klecker, T., Westermann, B., & Langer, T. (2012) · Science · doi:10.1126/science.1225625 · Cited by 232 · see citing works

SENP3‐mediated deSUMOylation of dynamin‐related protein 1 promotes cell death following ischaemia

Guo, C., Hildick, K. L., Luo, J., Dearden, L., Wilkinson, K. A., & Henley, J. M. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.65 · Cited by 226 · see citing works

Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor

Herlan, M., Bornhövd, C., Hell, K., Neupert, W., & Reichert, A. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403022 · Cited by 223 · see citing works

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

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

Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis

Jiang, X., Jiang, H., Shen, Z., & Wang, X. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417253111 · Cited by 220 · see citing works

Membrane Protein Degradation by AAA Proteases in Mitochondria

Leonhard, K., Guiard, B., Pellecchia, G., Tzagoloff, A., Neupert, W., & Langer, T. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80242-7 · Cited by 218 · see citing works

Mutations in LARS2, Encoding Mitochondrial Leucyl-tRNA Synthetase, Lead to Premature Ovarian Failure and Hearing Loss in Perrault Syndrome

Pierce, S. B., Geršak, K., Michaelson‐Cohen, R., Walsh, T., Lee, M. K., Malach, D., Klevit, R. E., King, M., & Levy‐Lahad, E. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.03.007 · Cited by 216 · see citing works

Opa1 Overexpression Ameliorates the Phenotype of Two Mitochondrial Disease Mouse Models

Civiletto, G., Varanita, T., Cerutti, R., Gorletta, T., Barbaro, S., Marchet, S., Lamperti, C., Viscomi, C., Scorrano, L., & Zeviani, M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.016 · Cited by 216 · see citing works

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

Yue, W., Chen, Z., Liu, H., Chen, Y., Chen, M., Feng, D., Yan, C., Wu, H., Du, L., Wang, Y., et al. (2014) · Cell Research · doi:10.1038/cr.2014.20 · Cited by 213 · see citing works

Stress-Regulated Translational Attenuation Adapts Mitochondrial Protein Import through Tim17A Degradation

Rainbolt, T. K., Atanassova, N., Genereux, J. C., & Wiseman, R. L. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.006 · Cited by 205 · see citing works

Degradation of the Amyloid β-Protein by the Novel Mitochondrial Peptidasome, PreP

Falkevall, A., Alikhani, N., Bhushan, S., Pavlov, P. F., Busch, K., Johnson, K. A., Eneqvist, T., Tjernberg, L. O., Ankarcrona, M., & Glaser, E. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602532200 · Cited by 202 · see citing works

The m -AAA Protease Associated with Neurodegeneration Limits MCU Activity in Mitochondria

König, T., Tröder, S. E., Bakka, K., Korwitz, A., Richter‐Dennerlein, R., Lampe, P., Patrón, M., Mühlmeister, M., Guerrero‐Castillo, S., Brandt, U., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.020 · Cited by 201 · see citing works

DNAJC19, a Mitochondrial Cochaperone Associated with Cardiomyopathy, Forms a Complex with Prohibitins to Regulate Cardiolipin Remodeling

Richter‐Dennerlein, R., Korwitz, A., Haag, M., Tatsuta, T., Dargazanli, S., Baker, M., Decker, T., Lamkemeyer, T., Rugarli, E. I., & Langer, T. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.016 · Cited by 200 · see citing works

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

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

Mitochondria: Impaired mitochondrial translation in human disease

Boczonadi, V., & Horváth, R. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.12.011 · Cited by 194 · see citing works

The short variant of the mitochondrial dynamin OPA1 maintains mitochondrial energetics and cristae structure

Lee, H., Smith, S. B., & Yoon, Y. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762567 · Cited by 190 · see citing works

Mammalian transcription factor A is a core component of the mitochondrial transcription machinery

Shi, Y.-H., Dierckx, A., Wanrooij, P. H., Wanrooij, S., Larsson, N., Wilhelmsson, L., Falkenberg, M., & Gustafsson, C. (2012) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1119738109 · Cited by 189 · see citing works

Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors

Gispert, S., Parganlija, D., Klinkenberg, M., Dröse, S., Wittig, I., Mittelbronn, M. G. A., Grzmil, P., Koob, S., Hamann, A., Walter, M. J., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt338 · Cited by 188 · see citing works

The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i‐AAA protease YME1L

Wai, T., Saita, S., Nolte, H., Müller, S., König, T., Richter‐Dennerlein, R., Sprenger, H., Madrenas, J., Mühlmeister, M., Brandt, U., et al. (2016) · EMBO Reports · doi:10.15252/embr.201642698 · Cited by 188 · see citing works

Rhomboid Protease PARL Mediates the Mitochondrial Membrane Potential Loss-induced Cleavage of PGAM5

Sekine, S., Kanamaru, Y., Koike, M., Nishihara, A., Okada, M., Kinoshita, H., Kamiyama, M., Maruyama, J., Uchiyama, Y., Ishihara, N., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.357509 · Cited by 187 · see citing works

LACTB is a tumour suppressor that modulates lipid metabolism and cell state

Keckesova, Z., Donaher, J. L., Cock, J. M. D., Freinkman, E., Lingrell, S., Bachovchin, D. A., Bierie, B., Tischler, V., Noske, A., Okondo, M. C., et al. (2017) · Nature · doi:10.1038/nature21408 · Cited by 187 · see citing works

Disruption of a Novel Gene (IMMP2L) by a Breakpoint in 7q31 Associated with Tourette Syndrome

Petek, E., Windpassinger, C., Vincent, J. B., Cheung, J., Boright, A. P., Scherer, S. W., Kroisel, P. M., & Wagner, K. (2001) · The American Journal of Human Genetics · doi:10.1086/319523 · Cited by 185 · see citing works

Regulation of mitochondrial phospholipids by Ups1/PRELI‐like proteins depends on proteolysis and Mdm35

Potting, C., Wilmes, C., Engmann, T., Osman, C., & Langer, T. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.169 · Cited by 184 · see citing works

The BCL2L1 and PGAM5 axis defines hypoxia-induced receptor-mediated mitophagy

Wu, H., Xue, D., Chen, G., Han, Z., Huang, L., Zhu, C., Wang, X., Jin, H., Wang, J., Zhu, Y., et al. (2014) · Autophagy · doi:10.4161/auto.29568 · Cited by 183 · see citing works

YME1L controls the accumulation of respiratory chain subunits and is required for apoptotic resistance, cristae morphogenesis, and cell proliferation

Stibůrek, L., Cesnekova, J., Kostková, O., Fornůsková, D., Vinšová, K., Wenchich, L., Houštěk, J., & Zeman, J. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-08-0674 · Cited by 180 · see citing works

MICOS and phospholipid transfer by Ups2–Mdm35 organize membrane lipid synthesis in mitochondria

Aaltonen, M. J., Friedman, J. R., Osman, C., Salin, B., di Rago, J., Nunnari, J. M., Langer, T., & Tatsuta, T. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201602007 · Cited by 180 · see citing works

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

Nakamura, N., & Hirose, S. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-11-1103 · Cited by 178 · see citing works

Processing of mitochondrial presequences

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Proteomic Identification of Coxiella burnetii Effector Proteins Targeted to the Host Cell Mitochondria During Infection

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The C-terminal region of the oxidoreductase MIA40 stabilizes its cytosolic precursor during mitochondrial import

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SLC25A45 is required for mitochondrial uptake of methylated amino acids and de novo carnitine biosynthesis

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The Diagnostic Value of Mitochondrial Mass of Peripheral T Lymphocytes in Early Sepsis

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Integrated approach to reducing polypharmacy in older people: exploring the role of oxidative stress and antioxidant potential therapy

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The coupling of mitoproteolysis and oxidative phosphorylation enables tracking of an active mitochondrial state through MitoTimer fluorescence

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Mitochondrial protein import machinery conveys stress signals to the cytosol and beyond

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Targeting mitochondrial quality control in muscle aging: Natural dietary products as potential interventions

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Mitochondrial DNA release and inflammation in mitochondrial disease pathogenesis

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Synthesis of Veliparib Prodrugs and Determination of Drug-Release-Dependent PARP-1 Inhibition

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Mitochondria (cross)talk with proteostatic mechanisms: Focusing on ageing and neurodegenerative diseases

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mTOR inhibition triggers mitochondrial fragmentation in cardiomyocytes through proteosome-dependent prohibitin degradation and OPA-1 cleavage

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Mitochondria: Master Regulator of Metabolism, Homeostasis, Stress, Aging and Epigenetics

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Mitochondrial Maintenance in Skeletal MusclePreprint

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Dynamic proteomics profiling of Legionella pneumophila infection unveils modulation of the host mitochondrial stress response pathwayPreprint

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Targeting the mitochondrial metabolite-dynamics-MDVs-MitoEVs axis: a new frontier in osteoarthritis management

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Mitochondrial metabolic reprogramming in diabetic cardiomyopathy

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Computation of the mitochondrial age distribution along the axon length

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The iAAA-mitochondrial protease YME1L1 regulates the degradation of the short-lived mitochondrial transporter SLC25A38Preprint

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Translation Termination in Human Mitochondria: The Role of mtRF1 and mtRF1a

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Mitochondrial proteases in cancer development and progression

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Mass spectrometry proteomics for studying mitostasis

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Mitochondrial calcium transport in amino acid metabolism: from nutritional responses to metabolic regulation

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Reframing neuropsychiatric disorders: Nuclear calcium signaling as a core signaling axis of mitochondrial proteostasis and synaptic energy homeostasis.

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Elucidating the Molecular Impact of DA29‐Induced ClpP Chemoactivation on Mitochondrial Function

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BindingDB Entry 50019063: Synthesis of Veliparib Prodrugs and Determination of Drug-Release-Dependent PARP-1 Inhibition.

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Mitochondrial Proteases: Multifaceted Regulators of Mitochondrial Plasticity

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Proteolytic control of mitochondrial function and morphogenesis

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Mitochondrial proteases modulate mitochondrial stress signalling and cellular homeostasis in health and disease

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Coordinating Mitochondrial Biology Through the Stress-Responsive Regulation of Mitochondrial Proteases

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Reprogramming of mitochondria by proteolysis

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