Structure of human PINK1 at a mitochondrial TOM-VDAC array

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works

Accurate structure prediction of biomolecular interactions with AlphaFold 3

Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A. J., Bambrick, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07487-w · Cited by 15,861 · see citing works

cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination

Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix

Liebschner, D. C., Afonine, P. V., Baker, M. L., Bunkòczi, G., Chen, V. B., Croll, T. I., Hintze, B. J., Hung, L., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 6,709 · see citing works

The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences

Perez-Riverol, Y., Bai, J., Bandla, C., García-Seisdedos, D., Hewapathirana, S., Kamatchinathan, S., Kundu, D. J., Prakash, A., Frericks-Zipper, A., Eisenacher, M., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1038 · Cited by 6,125 · see citing works

Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment

Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A., Olsen, J. V., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr101065j · Cited by 5,349 · see citing works

UCSF ChimeraX : Tools for structure building and analysis

Meng, E. C., Goddard, T. D., Pettersen, E. F., Couch, G. S., Pearson, Z., Morris, J. H., & Ferrin, T. E. (2023) · Protein Science · doi:10.1002/pro.4792 · Cited by 4,575 · see citing works

A cross-platform toolkit for mass spectrometry and proteomics

Chambers, M., MacLean, B., Burke, R., Amodei, D., Ruderman, D., Neumann, S., Gatto, L., Fischer, B., Pratt, B. S., Egertson, J. D., et al. (2012) · Nature Biotechnology · doi:10.1038/nbt.2377 · Cited by 4,042 · see citing works

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in <i>PINK1</i>

Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481 · see citing works

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · 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

ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps

Croll, T. (2018) · Acta Crystallographica Section D: Structural Biology · doi:10.1107/s2059798318002425 · Cited by 1,934 · see citing works

Ubiquitin is phosphorylated by PINK1 to activate parkin

Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477 · see citing works

PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity

Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298 · see citing works

Mitochondrial proteins: from biogenesis to functional networks

Pfanner, N., Warscheid, B., & Wiedemann, N. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0092-0 · Cited by 1,028 · see citing works

Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization

Sarraf, S. A., Raman, M., Guarani, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,020 · see citing works

Protein kinases: evolution of dynamic regulatory proteins

Taylor, S. S., & Kornev, A. P. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.006 · Cited by 940 · see citing works

PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65

Kondapalli, C., Kazlauskaite, A., Zhang, N., Woodroof, H. I., Campbell, D. G., Gourlay, R., Burchell, L., Walden, H., Macartney, T. J., Deak, M., et al. (2012) · Open Biology · doi:10.1098/rsob.120080 · Cited by 940 · see citing works

VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis

Cheng, E. H.-Y., Sheiko, T. V., Fisher, J. K., Craigen, W. J., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1083995 · Cited by 852 · see citing works

Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65

Kazlauskaite, A., Kondapalli, C., Gourlay, R., Campbell, D. G., Ritorto, M. S., Hofmann, K., Alessi, D. R., Knebel, A., Trost, M., & Muqit, M. M. K. (2014) · Biochemical Journal · doi:10.1042/bj20140334 · Cited by 806 · see citing works

p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both

Narendra, D. P., Kane, L. A., Hauser, D. N., Fearnley, I. M., & Youle, R. J. (2010) · Autophagy · doi:10.4161/auto.6.8.13426 · Cited by 789 · see citing works

jPOSTrepo: an international standard data repository for proteomes

Okuda, S., Watanabe, Y., Moriya, Y., Kawano, S., Yamamoto, T., Matsumoto, M., Takami, T., Kobayashi, D., Araki, N., Yoshizawa, A. C., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1080 · Cited by 695 · see citing works

Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis

Ordureau, A., Sarraf, S. A., Duda, D. M., Heo, J., Jedrychowski, M. P., Sviderskiy, V. O., Olszewski, J. L., Koerber, J. T., Xie, T., Beausoleil, S. A., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.007 · Cited by 693 · see citing works

Role of PINK1 Binding to the TOM Complex and Alternate Intracellular Membranes in Recruitment and Activation of the E3 Ligase Parkin

Lazarou, M., Jin, S. M., Kane, L. A., & Youle, R. J. (2012) · Developmental Cell · doi:10.1016/j.devcel.2011.12.014 · Cited by 670 · see citing works

Building and decoding ubiquitin chains for mitophagy

Harper, J. W., Ordureau, A., & Heo, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.129 · Cited by 668 · see citing works

PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria

Okatsu, K., Oka, T., Iguchi, M., Imamura, K., Kosako, H., Tani, N., Kimura, M., Go, E., Koyano, F., Funayama, M., et al. (2012) · Nature Communications · doi:10.1038/ncomms2016 · Cited by 602 · see citing works

The role of PINK1–Parkin in mitochondrial quality control

Narendra, D. P., & Youle, R. J. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01513-9 · Cited by 580 · see citing works

Mitochondria and cell death

Glover, H. L., Schreiner, A., Dewson, G., & Tait, S. W. G. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01429-4 · Cited by 489 · see citing works

Mechanism of phospho-ubiquitin-induced PARKIN activation

Wauer, T., Šimíček, M., Schubert, A. F., & Komander, D. (2015) · Nature · doi:10.1038/nature14879 · Cited by 479 · see citing works

Mechanism of parkin activation by PINK1

Gladkova, C., Maslen, S., Skehel, M. J., & Komander, D. (2018) · Nature · doi:10.1038/s41586-018-0224-x · Cited by 390 · see citing works

Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities

Schmidt, M. F., Gan, Z. Y., Komander, D., & Dewson, G. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00706-7 · Cited by 373 · see citing works

Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis

Wauer, T., Swatek, K. N., Wagstaff, J. L., Gladkova, C., Pruneda, J. N., Michel, M. A., Gersch, M., Johnson, C. M., Freund, S. M. V., & Komander, D. (2014) · The EMBO Journal · doi:10.15252/embj.201489847 · Cited by 303 · see citing works

Tom5 functionally links mitochondrial preprotein receptors to the general import pore

Dietmeier, K., Hönlinger, A., Bömer, U., Dekker, P., Eckerskorn, C., Lottspeich, F., Kübrich, M., & Pfanner, N. (1997) · Nature · doi:10.1038/40663 · Cited by 293 · see citing works

A neo-substrate that amplifies catalytic activity of Parkinson's-disease-related kinase PINK1

Hertz, N. T., Berthet, A., Sos, M. L., Thorn, K. S., Burlingame, A. L., Nakamura, K., & Shokat, K. M. (2013) · Cell · doi:10.1016/j.cell.2013.07.030 · Cited by 275 · see citing works

A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment

Okatsu, K., Uno, M., Koyano, F., Go, E., Kimura, M., Oka, T., Tanaka, K., & Matsuda, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.509653 · Cited by 248 · see citing works

Voltage-dependent Anion Channels (VDACs) Recruit Parkin to Defective Mitochondria to Promote Mitochondrial Autophagy

Sun, Y., Vashisht, A. A., Tchieu, J. H., Wohlschlegel, J. A., & Dreier, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419721 · Cited by 244 · see citing works

Insights into ubiquitin chain architecture using Ub-clipping

Swatek, K. N., Usher, J. L., Kueck, A. F., Gladkova, C., Mevissen, T. E. T., Pruneda, J. N., Skern, T., & Komander, D. (2019) · Nature · doi:10.1038/s41586-019-1482-y · Cited by 236 · see citing works

Mitochondrial protein synthesis adapts to influx of nuclear-encoded protein

Richter-Dennerlein, R., Oeljeklaus, S., Lorenzi, I., Ronsör, C., Bareth, B., Schendzielorz, A. B., Wang, C., Warscheid, B., Rehling, P., & Dennerlein, S. (2016) · Cell · doi:10.1016/j.cell.2016.09.003 · Cited by 232 · see citing works

Molecular architecture of the active mitochondrial protein gate

Shiota, T., Imai, K., Qiu, J., Hewitt, V. L., Tan, K. S., Shen, H., Sakiyama, N., Fukasawa, Y., Hayat, S., Kamiya, M., et al. (2015) · Science · doi:10.1126/science.aac6428 · Cited by 228 · see citing works

An integrated workflow for crosslinking mass spectrometry

Mendes, M. L., Fischer, L., Chen, Z. A., Barbon, M., O’Reilly, F. J., Giese, S. H., Bohlke‐Schneider, M., Belsom, A., Dau, T., Combe, C., et al. (2019) · Molecular Systems Biology · doi:10.15252/msb.20198994 · Cited by 221 · see citing works

Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation

Iguchi, M., Kujuro, Y., Okatsu, K., Koyano, F., Kosako, H., Kimura, M., Suzuki, N., Uchiyama, S., Tanaka, K., & Matsuda, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.467530 · Cited by 209 · see citing works

Activation mechanism of PINK1

Gan, Z. Y., Callegari, S., Cobbold, S. A., Cotton, T. R., Mlodzianoski, M. J., Schubert, A. F., Geoghegan, N. D., Rogers, K. L., Leis, A. P., Dewson, G., et al. (2021) · Nature · doi:10.1038/s41586-021-04340-2 · Cited by 209 · see citing works

Global Landscape and Dynamics of Parkin and USP30-Dependent Ubiquitylomes in iNeurons during Mitophagic Signaling

Ordureau, A., Paulo, J. A., Zhang, J., An, H., Swatek, K. N., Cannon, J. R., Wan, Q., Komander, D., & Harper, J. W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.11.013 · Cited by 198 · see citing works

Mechanism of parkin activation by phosphorylation

Sauvé, V., Sung, G., Soya, N., Kozlov, G., Blaimschein, N., Miotto, L. S., Trempe, J., Lukács, G. L., & Gehring, K. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0088-7 · Cited by 186 · see citing works

Dynamics of PARKIN-Dependent Mitochondrial Ubiquitylation in Induced Neurons and Model Systems Revealed by Digital Snapshot Proteomics

Ordureau, A., Paulo, J. A., Zhang, W., Ahfeldt, T., Zhang, J., Cohn, E. F., Hou, Z., Heo, J., Rubin, L. L., Sidhu, S. S., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.012 · Cited by 184 · see citing works

Structure of PINK1 in complex with its substrate ubiquitin

Schubert, A. F., Gladkova, C., Pardon, E., Wagstaff, J. L., Freund, S. M. V., Steyaert, J., Maslen, S., & Komander, D. (2017) · Nature · doi:10.1038/nature24645 · Cited by 178 · see citing works

Cryo-EM Structure of the TOM Core Complex from Neurospora crassa

Bausewein, T., Mills, D. J., Langer, J. D., Nitschke, B., Nußberger, S., & Kühlbrandt, W. (2017) · Cell · doi:10.1016/j.cell.2017.07.012 · Cited by 176 · see citing works

Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution

Tucker, K., & Park, E. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0339-2 · Cited by 161 · see citing works

Reciprocal Roles of Tom7 and OMA1 during Mitochondrial Import and Activation of PINK1

Sekine, S., Wang, C., Sideris, D. P., Bunker, E. N., Zhang, Z., & Youle, R. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.002 · Cited by 160 · see citing works

Mitochondrial protein transport: Versatility of translocases and mechanisms

Busch, J. D., Fielden, L. F., Pfanner, N., & Wiedemann, N. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.020 · Cited by 156 · see citing works

High Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage-dependent Anion Channel 2 Reveal an Oligomeric Population

Schredelseker, J., Paz, A., López, C. J., Altenbach, C., Leung, C. S., Drexler, M. K., Chen, J., Hubbell, W. L., & Abramson, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.497438 · Cited by 153 · see citing works

Atomic structure of human TOM core complex

Wang, W., Chen, X., Zhang, L., Yi, J., Ma, Q., Yin, J. Y., Zhuo, W., Gu, J., & Yang, M. (2020) · Cell Discovery · doi:10.1038/s41421-020-00198-2 · Cited by 122 · see citing works

Role of the TOM Complex in Protein Import into Mitochondria: Structural Views

Araiso, Y., Imai, K., & Endo, T. (2022) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-032620-104527 · Cited by 117 · see citing works

Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex

Rasool, S., Veyron, S., Soya, N., Eldeeb, M. A., Lukács, G. L., Fon, E. A., & Trempe, J. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.11.012 · Cited by 110 · see citing works

Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations

Woodroof, H. I., Pogson, J. H., Begley, M., Cantley, L. C., Deák, M., Campbell, D. G., van Aalten, D. M. F., Whitworth, A. J., Alessi, D. R., & Muqit, M. M. K. (2011) · Open Biology · doi:10.1098/rsob.110012 · Cited by 103 · see citing works

Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations

Kumar, A., Tamjar, J., Waddell, A. D., Woodroof, H. I., Raimi, O. G., Shaw, A. M., Peggie, M. W., Muqit, M. M. K., & van Aalten, D. M. F. (2017) · eLife · doi:10.7554/elife.29985 · Cited by 102 · see citing works

xiVIEW: Visualisation of Crosslinking Mass Spectrometry Data

Combe, C., Graham, M., Kolbowski, L., Fischer, L., & Rappsilber, J. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168656 · Cited by 99 · see citing works

Tom20 gates PINK1 activity and mediates its tethering of the TOM and TIM23 translocases upon mitochondrial stress

Eldeeb, M. A., Bayne, A. N., Fallahi, A., Goiran, T., MacDougall, E. J., Soumbasis, A., Zorca, C. E., Jones-Tabah, J., Thomas, R. A., Karpilovsky, N. C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313540121 · Cited by 80 · see citing works

Dual Role of Mitochondrial Porin in Metabolite Transport across the Outer Membrane and Protein Transfer to the Inner Membrane

Ellenrieder, L., Dieterle, M. P., Doan, K. N., Mårtensson, C. U., Floerchinger, A., Campo, M. L., Pfanner, N., & Becker, T. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.014 · Cited by 78 · see citing works

Porin Associates with Tom22 to Regulate the Mitochondrial Protein Gate Assembly

Sakaue, H., Shiota, T., Ishizaka, N., Kawano, S., Tamura, Y., Tan, K. S., Imai, K., Motono, C., Hirokawa, T., Taki, K., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.003 · Cited by 74 · see citing works

Cryo-slicing Blue Native-Mass Spectrometry (csBN-MS), a Novel Technology for High Resolution Complexome Profiling

Müller, C. S., Bildl, W., Haupt, A., Ellenrieder, L., Becker, T., Hunte, C., Fakler, B., & Schulte, U. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.054080 · Cited by 73 · see citing works

Molecular pathway of mitochondrial preprotein import through the TOM–TIM23 supercomplex

Zhou, X., Yang, Y., Wang, G., Wang, S., Sun, D., Ou, X., Lian, Y., & Li, L. (2023) · Nature Structural &amp; Molecular Biology · doi:10.1038/s41594-023-01103-7 · Cited by 72 · see citing works

Structural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex receptors

Su, J., Liu, D., Yang, F., Zuo, M.-Q., Li, C., Dong, M., Sun, S., & Sui, S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2200158119 · Cited by 68 · see citing works

Renaissance of VDAC: New Insights on a Protein Family at the Interface between Mitochondria and Cytosol

Pinto, V. D. (2021) · Biomolecules · doi:10.3390/biom11010107 · Cited by 65 · see citing works

From TOM to the TIM23 complex – handing over of a precursor

Callegari, S., Cruz‐Zaragoza, L. D., & Rehling, P. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0101 · Cited by 65 · see citing works

Global ubiquitylation analysis of mitochondria in primary neurons identifies endogenous Parkin targets following activation of PINK1

Antico, O., Ordureau, A., Stevens, M., Singh, F., Nirujogi, R. S., Gierliński, M., Barini, E., Rickwood, M. L., Prescott, A. R., Toth, R. L., et al. (2021) · Science Advances · doi:10.1126/sciadv.abj0722 · Cited by 63 · see citing works

Succination is Increased on Select Proteins in the Brainstem of the NADH dehydrogenase (ubiquinone) Fe-S protein 4 (Ndufs4) Knockout Mouse, a Model of Leigh Syndrome

Piroli, G. G., Manuel, A. M., Clapper, A. C., Walla, M. D., Baatz, J. E., Palmiter, R. D., Quintana, A., & Frizzell, N. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.051516 · Cited by 47 · see citing works

Structural insights into ubiquitin phosphorylation by PINK1

Okatsu, K., Sato, Y., Yamano, K., Matsuda, N., Negishi, L., Takahashi, A., Yamagata, A., Goto‐Ito, S., Mishima, M., Ito, Y., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-28656-8 · Cited by 47 · see citing works

Structural insights into assembly of human mitochondrial translocase TOM complex

Guan, Z., Yan, L., Wang, Q., Qi, L., Hong, S., Gong, Z., Yan, C., & Yin, P. (2021) · Cell Discovery · doi:10.1038/s41421-021-00252-7 · Cited by 47 · see citing works

TIM23 facilitates PINK1 activation by safeguarding against OMA1-mediated degradation in damaged mitochondria

Akabane, S., Kiyona, W., Kosako, H., Yamashita, S., Nishino, K., Kato, M., Sekine, S., Kanki, T., Matsuda, N., Endo, T., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112454 · Cited by 45 · see citing works

Mechanism of human PINK1 activation at the TOM complex in a reconstituted system

(2024) · doi:10.1126/sciadv.adn7191 · Cited by 39 · see citing works

Crystal structural characterization reveals novel oligomeric interactions of human voltage‐dependent anion channel 1

Hosaka, T., Okazaki, M., Kimura‐Someya, T., Ishizuka‐Katsura, Y., Ito, K., Yokoyama, S., Dodo, K., Sodeoka, M., & Shirouzu, M. (2017) · Protein Science · doi:10.1002/pro.3211 · Cited by 33 · see citing works

Phospho-ubiquitin-PARK2 complex as a marker for mitophagy defects

Callegari, S., Oeljeklaus, S., Warscheid, B., Dennerlein, S., Thumm, M., Rehling, P., & Dudek, J. (2017) · Autophagy · doi:10.1080/15548627.2016.1254852 · Cited by 29 · see citing works

The role of the individual TOM subunits in the association of PINK1 with depolarized mitochondria

Maruszczak, K. K., Jung, M., Rasool, S., Trempe, J.-F., & Rapaport, D. (2022) · Journal of Molecular Medicine · doi:10.1007/s00109-022-02191-6 · Cited by 29 · see citing works

Two conformations of the Tom20 preprotein receptor in the TOM holo complex

Ornelas, P., Bausewein, T., Martin, J., Morgner, N., Nussberger, S., & Kühlbrandt, W. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2301447120 · Cited by 27 · see citing works

Pharmacological PINK1 activation ameliorates Pathology in Parkinson’s Disease modelsPreprint

Hertz, N. T., Chin, R., Rakhit, R., Ditsworth, D., Wang, C., Bartholoméüs, J., Liu, S., Mody, A., Laihsu, A., Eastes, A., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4356493/v1 · Cited by 23 · see citing works

Defining the architecture of the human TIM22 complex by chemical crosslinking

Valpadashi, A., Callegari, S., Linden, A., Neumann, P., Ficner, R., Urlaub, H., Deckers, M., & Rehling, P. (2020) · FEBS Letters · doi:10.1002/1873-3468.13978 · Cited by 23 · see citing works

Structural overview of the translocase of the mitochondrial outer membrane complex

Araiso, Y., & Endo, T. (2022) · Biophysics and Physicobiology · doi:10.2142/biophysico.bppb-v19.0022 · Cited by 17 · see citing works

Crosstalk between Mitochondrial Protein Import and Lipids

Hoffmann, J. J., & Becker, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095274 · Cited by 16 · see citing works

Interaction of PINK1 with nucleotides and kinetin

Gan, Z. Y., Callegari, S., Nguyen, T. N., Kirk, N. S., Leis, A., Lazarou, M., Dewson, G., & Komander, D. (2024) · Science Advances · doi:10.1126/sciadv.adj7408 · Cited by 14 · see citing works

Transient Transfection and Expression of Eukaryotic Membrane Proteins in Expi293F Cells and Their Screening on a Small Scale: Application for Structural Studies

Krasnoselska, G. O., Dumoux, M., Gamage, N., Cheruvara, H., Birch, J., Quigley, A., & Owens, R. J. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1406-8_5 · Cited by 12 · see citing works

The architecture of substrate-engaged TOM–TIM23 supercomplex reveals preprotein proximity sites for mitochondrial protein translocation

Wang, Q., Zhuang, J., Huang, R., Guan, Z., Yan, L., Hong, S., Zhang, L., Huang, C. Y., Liu, Z., & Yin, P. (2024) · Cell Discovery · doi:10.1038/s41421-023-00643-y · Cited by 11 · see citing works

Structure of the intact Tom20 receptor in the human translocase of the outer membrane complex

Su, J., Tian, X., Wang, Z., Yang, J.-W., Sun, S., & Sui, S. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae269 · Cited by 9 · see citing works

Molecular machineries and pathways of mitochondrial protein transport

Endo, T., & Wiedemann, N. (2025) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-025-00865-w · Cited by 47 · see citing works

A unified mechanism for mitochondrial damage sensing in PINK1-Parkin–mediated mitophagy

Thayer, J. A., Petersen, J. D., Huang, X., Budet, L. M. G., Hawrot, J., Ramos, D. M., Sekine, S., Li, Y., Ward, M. E., & Narendra, D. P. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00604-z · Cited by 32 · see citing works

In situ cryo-ET visualization of mitochondrial depolarization and mitophagic engulfment

Rose, K. M., Herrmann, E., Kakudji, E. V., Lizarrondo, J., Celebi, A. Y., Wilfling, F., Lewis, S. C., & Hurley, J. H. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2511890122 · Cited by 25 · see citing works

The Roles of Lactate and Lactylation in Diseases Related to Mitochondrial Dysfunction

Ma, F., & Yu, W. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157149 · Cited by 20 · see citing works

Conformational plasticity of mitochondrial VDAC2 controls the kinetics of its interaction with cytosolic proteins

Rosencrans, W. M., Khuntia, H., Larimi, M. G., Mahalakshmi, R., Yu, T., Bezrukov, S. M., & Rostovtseva, T. K. (2025) · Science Advances · doi:10.1126/sciadv.adv4410 · Cited by 19 · see citing works

Ubiquitin signaling in PINK1/Parkin-dependent mitophagy

Okatsu, K., & Fukai, S. (2025) · The Journal of Biochemistry · doi:10.1093/jb/mvaf079 · Cited by 19 · see citing works

The dual role of VDAC in cancer: Molecular mechanisms and advances in targeted therapy

Huang, H., Chen, M., Feng, S., Lin, Z., & Liu, Y. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118530 · Cited by 15 · see citing works

Oligomer-based functions of mitochondrial porin

Takeda, H., Shinoda, S., Goto, C., Tsutsumi, A., Sakaue, H., Zhang, C., Hirashima, T., Konishi, Y., Ono, H., Yamamori, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62021-4 · Cited by 14 · see citing works

Stressful situations: Molecular insights on mitochondrial quality control pathways

Romanelli, S., & Trempe, J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110483 · Cited by 10 · see citing works

From Biogenesis to Breakdown: How Protein Biogenesis and Quality Control Failures Drive Mitochondrial Disease

Leeming, P. J., Mercuri-Svik, J., & Stojanovski, D. (2025) · Molecular and Cellular Biology · doi:10.1080/10985549.2025.2566671 · Cited by 9 · see citing works

Levodopa–Carbidopa–Entacapone Intestinal Gel for Advanced Parkinson’s Disease—Results from a Monocentric Study Evaluating Both Motor and Non-Motor Manifestations

Lungu, M., Oprea, V. D., Apostol, L. L., Elkan, E. M., Ionescu, A. M., Tudor, A., & Zaharia, A. L. (2025) · Biomedicines · doi:10.3390/biomedicines13092191 · Cited by 6 · see citing works

Sources of Oxidative Stress in Parkinson’s Disease: Pathways and Therapeutic Implications

Yordanov, Y., Stefanova, D., Kondeva-Burdina, M., & Tzankova, V. (2026) · Antioxidants · doi:10.3390/antiox15020187 · Cited by 6 · see citing works

Function and regulation of the mitochondrial stress response

Sheetz, J. B., Chandrasekhar, S., & Rapé, M. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01769-9 · Cited by 8 · see citing works

Research on the Application of Mesenchymal Stem Cells for Addressing Mitochondrial Damage in Neurodegenerative Diseases

Zhang, L., Ge, Y., Wu, J., Wang, M., Huang, N., & Luo, Y. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01624-3 · Cited by 5 · see citing works

Molecular mechanism of PINK1 regulation by the Hsp90 machinery

Tian, X., Su, J., Wang, Z., Liu, T., Xiong, H., Sun, S., Mei, K., & Sui, S. (2025) · Nature Communications · doi:10.1038/s41467-025-65859-w · Cited by 5 · see citing works

IER3 drives the transition from sepsis-associated AKI to CKD by suppressing the mitochondrial translocation of PRDX5

Dou, Q., Tong, H., Chen, J., Yi, X., Bai, L., He, J., & Chen, K. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05963-8 · Cited by 5 · see citing works

Synuclein and Mitochondrial Dysfunction: Regulating the Protein Import Complex toward PD Treatment?

Dash, U. K., & Mahalakshmi, R. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00323 · Cited by 5 · see citing works

Molecular mechanisms of PINK1/Parkin-mediated mitochondrial quality control

Bayne, A. N., & Trempe, J. (2026) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2026.02.014 · Cited by 5 · see citing works

Parkinson’s Disease Through the Lens of Metabolomics: A Targeted Systematic Review on Human Studies (2019–2024)

Cannas, F., Kopeć, K. K., Zuddas, N., Marincola, F. C., Arcara, G., Loi, M., Mussap, M., & Fanos, V. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14176277 · Cited by 4 · see citing works

Is the Voltage-Dependent Anion Channel a Major Player in Neurodegenerative Diseases?

Neumann, S., & Heumann, R. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136138 · Cited by 4 · see citing works

A membrane-disruptive action of VBIT-4 challenges its role as a widely used VDAC1 oligomerization inhibitorPreprint

Ravishankar, V., Borges-Araújo, L., Rajendran, M., Lafargue, E., Byrne, D., Buzhinsky, N., Wolfe, M. S., Fitzgerald, W., Bautista, N. A., Beyene, B. G., et al. (2026) · eLife · doi:10.7554/elife.111980 · Cited by 4 · see citing works

Modulation of mitochondrial voltage dependent anion channel: studies on bilayer electrophysiology

Koren, D. T., Malik, C., Siddiqui, S. I., Shrivastava, R., & Ghosh, S. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1666994 · Cited by 3 · see citing works

Cis or trans: a puzzle of Parkin activation mechanism

Sherawat, M., Kumar, A., Lenka, D. R., & Kumar, A. (2026) · Essays in Biochemistry · doi:10.1042/ebc20253048 · Cited by 3 · see citing works

Myricetin stabilizes PINK1 to activate mitophagy and ameliorate metabolic dysfunction-associated steatotic liver disease

Xu, W., Nie, L., Cao, J., Shan, C., Cao, Y., Yu, J., Tuo, P., Yu, J., Fujii, H., Thủy, L. T. T., et al. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.158009 · Cited by 3 · see citing works

Transmembrane domain switching controls PINK1 import and fate in mitochondria

Lorriman, J. S., Hughes, R., Grieve, A. G., Corey, R. A., & Collinson, I. R. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00789-x · Cited by 3 · see citing works

Iron Deficiency Impairs Mitochondrial Energetics and Early Axonal Growth and Branching in Developing Hippocampal Neurons

Méndez, D., Devgun, K., Carlson, L. H., Mickelson, D. J., Monko, T. R., Reeves, L., Lanier, L. M., Georgieff, M., & Bastian, T. W. (2026) · Journal of Nutrition · doi:10.1016/j.tjnut.2026.101630 · Cited by 3 · see citing works

Structures of Chaetomium thermophilum TOM complexes with bound preproteins

Agip, A.-N. A., Ornelas, P., Yang, T., Uboldi, E., Häder, S., McDowell, M. A., & Kühlbrandt, W. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2507279122 · Cited by 4 · see citing works

Targeting of kinases to treat neurodegenerative diseases

Shomali, T., & Trempe, J.-F. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100128 · Cited by 4 · see citing works

Decoding Outer Membrane β-Barrels: From Structural Curiosity to Engineered Nanotherapeutics

Mahalakshmi, R. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00902 · Cited by 2 · see citing works

A pore is a pore is a pore (or a hub?): VDAC oligomerization in mitochondrial connectivity and modulation

Pinto, V. D., Battiato, G., Nibali, S. C., & Cubisino, S. A. M. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250480 · Cited by 2 · see citing works

Mitophagy-mediated immune evasion: Shared strategies of pathogens

Li, J., Li, W., (34472), D. W., & Liu, Y. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104247 · Cited by 2 · see citing works

Mitochondrial Voltage-Dependent Anion Channel: From a Passive Pore to a Cellular Hub Through Protein Complexation

Rajendran, M., Bezrukov, S. M., & Rostovtseva, T. K. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27135804 · Cited by 2 · see citing works

Mitochondrial DNA homeostasis: A novel therapeutic target for neurodegenerative diseases

Fu, T., Chen, X., Zhang, S., Fu, Y., Huang, L., & Xiong, W. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00495 · Cited by 1 · see citing works

Protein mechanism and therapeutic design in Parkinson's disease: A structural biology perspective

Simons, D. M., & Trempe, J.-F. (2025) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2025.103140 · Cited by 1 · see citing works

Proteostasis at the mitochondrial outer membrane: Quality control of mitochondrial protein transport

Matsumoto, S., Ono, S., & Endo, T. (2026) · Protein Science · doi:10.1002/pro.70587 · Cited by 1 · see citing works

Direct coupling of human TOM and TIM22 complexes drives mitochondrial carrier import

Liu, X., Cai, H., Wang, H., Zhou, X., Zhang, Y., Liu, S., Zhu, J., & Li, L. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01849-w · Cited by 1 · see citing works

Targeting TOMM40 unleashes immunogenic mitophagy to facilitate antigen presentation and immunotherapy sensitization

Zhang, Z., Xie, Y.-A., Mu, C., Sheng, S., Zhang, J., Han, J., Li, J., He, Z., & Liu, X. (2026) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2026-015462 · Cited by 1 · see citing works

Membrane curvature regulates Ups1 dependent phosphatidic acid transfer across lipid bilayersPreprint

Sadeqi, F., Dong, D., Stroh, K. S., Vache, M., Metz, J., Riedel, D., Janshoff, A., Risselada, H. J., Kolenda, C., & Meinecke, M. (2025) · eLife · doi:10.7554/elife.106979.1 · Cited by 1 · see citing works

Membrane curvature regulates Ups1 dependent phosphatidic acid transfer across lipid bilayersPreprint

Sadeqi, F., Dong, D., Stroh, K. S., Vache, M., Metz, J., Riedel, D., Janshoff, A., Risselada, H. J., Kolenda, C., & Meinecke, M. (2025) · eLife · doi:10.7554/elife.106979 · Cited by 1 · see citing works

Self-Assembling Synthetic Peptides Remodel Mitochondrial Properties via Nanopore FormationPreprint

Nguyen, N., Fujita, S., Takeuchi, N., Kawano, R., & Inoue, T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.26.672490 · Cited by 1 · see citing works

miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A

Markham, B. N., Ramnarine, C., Kim, S., Grever, W. E., Soto-Beasley, A. I., Heckman, M. G., Ren, Y., Osborne, A. C., Kehili, M., Bhagwate, A. V., et al. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00029-w

Membrane curvature regulates Ups1 dependent phosphatidic acid transfer across lipid bilayersPreprint

Sadeqi, F., Dong, D., Stroh, K. S., Vache, M., Metz, J., Riedel, D., Janshoff, A., Risselada, H. J., Kolenda, C., & Meinecke, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.03.647039

A Photo-regulatable Intein Based Trans-Splicing tool for Protein and Organelle Relocalization to Different Subcellular CompartmentsPreprint

Tang, C., Zhou, Q., Gao, Z., Peng, P., Wang, B., Liu, Z., Xu, S., & Li, H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.20.665713

Structural characterization of intra- and intermolecular disulfide bonds in voltage-dependent anion channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry

Pittalà, M. G. G., Cucina, A., Nibali, S. C., Cunsolo, V., Francesco, A. D., Battiato, G., Reina, S., Foti, S., Pinto, V. D., & Saletti, R. (2025) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-025-06074-w

Structural basis for the folding of PINK1 by the HSP90–CDC37 chaperone complexPreprint

Okatsu, K., Yamamoto, H., Okamoto, A., Goto, S. H., Nishimoto, Y., Sugita, Y., Noda, T., & Fukai, S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.17.682828

BRET-Based Mitochondrial Subcompartment Localization BiosensorsPreprint

Abdulrahman, A. O., Lescuyer, M., Zein, R. M. E., Cecon, E., Dam, J., Masri, B., & Jockers, R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.27.684728

2025: A year of resilience and resourcefulness

Clarke, J., & Editors, O. B. O. T. P. B. S. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003582

CryoEM screening with a blotting instrument: quantifying parameters affecting ice thickness using semi-automated image analysis

Valimehr, S., Cho, E., Brown, H. G., McMillan, P. J., & Hanssen, E. G. (2025) · Methods in microscopy · doi:10.1515/mim-2025-0028

Trim15 stabilizes VDAC3 via ubiquitination to suppress autophagy and enhance chemosensitivity in hypopharyngeal squamous cell carcinoma

Wang, G., Shen, Y., Wang, L., Fu, T., Huang, Y., Chai, F., Xu, M., Jiang, Y., & Zhang, J. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-02943-0

Structural basis for the folding of PINK1 by the HSP90–CDC37 chaperone complexPreprint

Okatsu, K., Yamamoto, H., Okamoto, A., Goto, S., Nishimoto, Y., Sugita, Y., Noda, T., & Fukai, S. (2026) · eLife · doi:10.7554/elife.110255.1

Structural basis for the folding of PINK1 by the HSP90–CDC37 chaperone complexPreprint

Okatsu, K., Yamamoto, H., Okamoto, A., Goto, S., Nishimoto, Y., Sugita, Y., Noda, T., & Fukai, S. (2026) · eLife · doi:10.7554/elife.110255

Membrane curvature regulates Ups1 dependent phosphatidic acid transfer across lipid bilayersPreprint

Sadeqi, F., Dong, D., Stroh, K. S., Vache, M., Metz, J., Riedel, D., Janshoff, A., Risselada, H. J., Kolenda, C., & Meinecke, M. (2026) · eLife · doi:10.7554/elife.106979.2

Modulation of PKCα/ETS1 by klotho restores CYB5R4-dependent mitochondrial function in proximal tubular epithelial cells to attenuate the progression of diabetic kidney disease

Gan, C., Zhou, X., Qiu, L., Chen, D., Shi, Y., Yang, Q., Jiang, H., Xiao, H., Chen, W., Yang, X., et al. (2026) · Cardiovascular Diabetology · doi:10.1186/s12933-026-03150-y

Phosphorylated ubiquitin is a secondary messenger and an epigenetic mark mediating mitochondria to nucleus signalingPreprint

Mercer, T. J., Dániel, B., Fredrickson, C., Le, D., Lee, S., Kulkarni, V. V., Hou, X., Fiesel, F. C., Ngu, H., Jung, M., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.24.719390 · Cited by 1 · see citing works

Cynandione A improves white adipose tissue homeostasis in high-fat diet-fed mice

Sawamoto, A., Shiba, M., Okuyama, S., Cho, C. J., Kim, J. H., & Nakajima, M. (2026) · Journal of Pharmacy and Pharmacology · doi:10.1093/jpp/rgag038

Dynamic disorder is crucial for mitochondrial protein import

Schneider, J., Guillerm, U., Pereira, C. S., & Schanda, P. (2026) · Protein Science · doi:10.1002/pro.70630

Higher-order structural organization of mitochondrial metabolism

Kafetzopoulos, G., Döbler, J., & Kastritis, P. L. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113174

Lishui Xiaozhong granules protect against diabetic retinopathy by activating PINK1/parkin-mediated mitophagy and suppressing ferroptosis

Yu, D., Tao, Y.-J., Yali, Q., Jianwei, W., & Chuanhong, J. (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.121898

Super-resolution complexome of human mitochondria elucidates translocase, morphology and OXPHOS networksPreprint

Schulte, U., Haupt, A., Steiert, C., Melchionda, L., Feignier, A., von der Malsburg, K., Bildl, W., van den Broucke, J.-B., Müller, C. S., Becker, T., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.29.728872

Regulation of mitochondrial protein translocases

Bertgen, L., & Chacińska, A. (2026) · Protein Science · doi:10.1002/pro.70662

Physical exercise as a precision strategy for targeted PINK1 recruitment- a mechanistic review

Zhu, J., Tong, L., & Thirupathi, A. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1836651

Selenoprotein S plays a role in translation and membrane protein biogenesisPreprint

Ghelichkhani, F., Kapitonova, M. A., Odunsi, A., Rahmani, E., Arana, A. O. B., Kaniyar, M. H., LaCava, J., & Rozovsky, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.08.725543

ROS Impair Mitophagy via PARylation of PINK1Preprint

Gao, L., Wang, H., Zhuang, X., Rong, D., Gao, X.-Z., Xie, L., Wang, Z., Tang, M., Chen, Y., Zhang, Y., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.18.733102

Inhibiting PPM1D Perturbs Mitochondrial Integrity to Stimulate cGAS-STING Signaling and Antitumor Immunity

Zhang, L., Zheng, X., Fu, H., Liu, L., Zhang, W., Zhang, Y., Gao, Z., Zhang, S., Jin, Y., & Yan, S. (2026) · Cancer Research · doi:10.1158/0008-5472.can-25-5286

Selenoprotein S associates with complexes governing membrane protein biogenesis and translation-associated processes

Ghelichkhani, F., Kapitonova, M. A., Odunsi, A., Rahmani, E., Bringas, O. G. R., Kaniyar, M. H., LaCava, J., & Rozovsky, S. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104336

FTO-mediated m6A demethylation of SNHG9 enhances PINK1-dependent mitophagy and reverses cisplatin resistance via nuclear EZH2 ubiquitination

Jing, Z., Ren, X., Wang, R., An, B., Gao, W., Jin, Y., Shang, L., Jia, D., & Yu, Y. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118345

Regulation and roles of mammalian mitophagy

Martens, S., & Ganley, I. G. (2026) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-026-01012-9 · Cited by 1 · see citing works

Exploring the shared genetic architecture between post-traumatic stress disorder (PTSD) and obstructive sleep apnea (OSA)

Liu, X., Liu, Y., Gao, M., Lu, J., Lu, D., Song, Z., Wang, M., Song, B., Li, H., Qiu, Y., et al. (2026) · European Journal of Psychotraumatology · doi:10.1080/20008066.2026.2709174

A cellular state-gated model for the biogenesis and function of mitochondrial extracellular vesicles

Zhai, P., Ma, T., Wu, W., Lu, H., Chen, Y., Zhang, T., Peng, Z., Xu, D., & Li, Y. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102203

Mitophagy in neuronal health and disease: from mechanisms to neurodegeneration

Basak, B., Riley, J. F., Nataraj, N. M., & Holzbaur, E. L. F. (2026) · Journal of Clinical Investigation · doi:10.1172/jci199847 · Cited by 1 · see citing works

Modulation of mitochondrial quality control in sepsis by traditional Chinese medicine: mechanistic insights and translational perspectives

Chang, M., Hu, D., Zhang, K., Liu, S., Xue, H., Zhu, Y., Chen, S., Liu, L., Wu, C., Fu, H., et al. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1865750

Evolutionary analysis of PINK1 reveals key roles of the N- and C-terminal extensions and TOM20 in folding its kinase domainPreprint

Shomali, T., Veyron, S., & Trempe, J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.05.749644

BRET-Based Mitochondrial Subcompartment Localization Biosensors Reveal the Impact of Pesticides and Food Additives on Mitochondrial Protein Localization

Abdulrahman, A. O., Lescuyer, M., Zein, R. M. E., Debbiche, R., Cecon, E., Dam, J., Masri, B., & Jockers, R. (2026) · ACS Sensors · doi:10.1021/acssensors.6c01115

Mitophagy coordinates organelle crosstalk in health and diseases

Wu, M., He, P., Lian, Y., Zhang, T., Wu, Y., Wang, L., Tang, D., Yao, Y.-M., & Yao, R.-Q. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02812-3

So similar, yet so different: α-synuclein recognition of the isoform-specific VDAC protein–lipid interfacePreprint

Rostovtseva, T. K., Rajendran, M., Rosencrans, W. M., Queralt-Martín, M., Wolfe, M. S., Bautista, N. A., Beyene, B. G., Larimi, M. G., Sodt, A. J., & Bezrukov, S. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.13.758914

Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex

Rasool, S., Veyron, S., Soya, N., Eldeeb, M. A., Lukács, G. L., Fon, E. A., & Trempe, J. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.11.012 · Cited by 110 · see citing works

Reconstitution of human PINK1 and outer mitochondria TOM complex in yeast v1Preprint

Raimi, O. G., & Muqit, M. M. K. (2024) · doi:10.17504/protocols.io.n2bvj37kwlk5/v1

India issues new requirements for clinical trial approval

Bagcchi, S. (2014) · BMJ · doi:10.1136/bmj.g5648 · Cited by 1 · see citing works

Dissecting the interactions of PINK1 with the TOM complex in depolarized mitochondriaPreprint

Maruszczak, K. K., Jung, M., Rasool, S., Trempe, J., & Rapaport, D. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.13.476189 · Cited by 1 · see citing works

The role of the individual TOM subunits in the association of PINK1 with depolarized mitochondria

Maruszczak, K. K., Jung, M., Rasool, S., Trempe, J.-F., & Rapaport, D. (2022) · Journal of Molecular Medicine · doi:10.1007/s00109-022-02191-6 · Cited by 29 · see citing works