{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T19:50:43Z","timestamp":1793044243562,"version":"4.5.0"},"reference-count":71,"publisher":"Elsevier BV","issue":"12","license":[{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,10,24]],"date-time":"2025-10-24T00:00:00Z","timestamp":1761264000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100005242","name":"Universit\u00e9 de Montr\u00e9al","doi-asserted-by":"publisher","award":["SCR_022303"],"award-info":[{"award-number":["SCR_022303"]}],"id":[{"id":"10.13039\/501100005242","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN-2022-04042"],"award-info":[{"award-number":["RGPIN-2022-04042"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000864","name":"Michael J Fox Foundation for Parkinson&apos;s Research","doi-asserted-by":"publisher","award":["MJFF-023912"],"award-info":[{"award-number":["MJFF-023912"]}],"id":[{"id":"10.13039\/100000864","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["PJT-195804"],"award-info":[{"award-number":["PJT-195804"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["39044"],"award-info":[{"award-number":["39044"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["229792"],"award-info":[{"award-number":["229792"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001804","name":"Canada Research Chairs","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001804","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001805","name":"Canada Foundation for Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001805","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"publisher","award":["30574"],"award-info":[{"award-number":["30574"]}],"id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2025,12]]},"DOI":"10.1016\/j.jbc.2025.110860","type":"journal-article","created":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T18:02:54Z","timestamp":1761588174000},"page":"110860","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"title":["Substrate recognition by the human mitochondrial processing peptidase and its processing of PINK1"],"prefix":"10.1016","volume":"301","author":[{"given":"Andrew N.","family":"Bayne","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-0154-0279","authenticated-orcid":false,"given":"Danielle M.","family":"Simons","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0086-4389","authenticated-orcid":false,"given":"Naoto","family":"Soya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl","family":"Grenier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gergely L.","family":"Lukacs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward A.","family":"Fon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6543-3371","authenticated-orcid":false,"given":"Jean-Fran\u00e7ois","family":"Trempe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2025.110860_bib1","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a007559","article-title":"Quality control of mitochondrial proteostasis","volume":"3","author":"Baker","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib2","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.tins.2022.12.001","article-title":"Mitochondrial signalling and homeostasis: from cell biology to neurological disease","volume":"46","author":"Collier","year":"2023","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.jbc.2025.110860_bib3","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1038\/ni.3704","article-title":"Mitochondria are the powerhouses of immunity","volume":"18","author":"Mills","year":"2017","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.jbc.2025.110860_bib4","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1016\/j.molcel.2023.02.020","article-title":"Mitochondrial protein transport: versatility of translocases and mechanisms","volume":"83","author":"Busch","year":"2023","journal-title":"Mol. Cell."},{"key":"10.1016\/j.jbc.2025.110860_bib5","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1002\/j.1460-2075.1988.tb02859.x","article-title":"Amphiphilicity is essential for mitochondrial presequence function","volume":"7","author":"Roise","year":"1988","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2025.110860_bib6","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.cell.2009.07.045","article-title":"Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability","volume":"139","author":"V\u00f6gtle","year":"2009","journal-title":"Cell."},{"key":"10.1016\/j.jbc.2025.110860_bib7","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/0962-8924(96)81000-2","article-title":"Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp 70","volume":"6","author":"Mihara","year":"1996","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib8","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2200158119","article-title":"Structural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex receptors","volume":"119","author":"Su","year":"2022","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2025.110860_bib9","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1038\/s41586-019-1680-7","article-title":"Structure of the mitochondrial import gate reveals distinct preprotein paths","volume":"575","author":"Araiso","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2025.110860_bib10","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1515\/hsz-2020-0101","article-title":"From TOM to the TIM23 complex - handing over of a precursor","volume":"401","author":"Callegari","year":"2020","journal-title":"Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib11","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1016\/j.bbabio.2010.01.026","article-title":"The many faces of the mitochondrial TIM23 complex","volume":"1797","author":"Mokranjac","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110860_bib12","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1038\/ncb1635","article-title":"Motor-free mitochondrial presequence translocase drives membrane integration of preproteins","volume":"9","author":"van der Laan","year":"2007","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib13","doi-asserted-by":"crossref","first-page":"4028","DOI":"10.1038\/s41467-018-06492-8","article-title":"Motor recruitment to the TIM23 channel\u2019s lateral gate restricts polypeptide release into the inner membrane","volume":"9","author":"Schendzielorz","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2025.110860_bib14","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0167-4889(02)00265-3","article-title":"Mitochondrial processing peptidases","volume":"1592","author":"Gakh","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110860_bib15","doi-asserted-by":"crossref","first-page":"9284","DOI":"10.1016\/S0021-9258(17)37105-3","article-title":"Rat liver mitochondrial processing peptidase. Both alpha- and beta-subunits are required for activity","volume":"269","author":"Saavedra-Alanis","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib16","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1006\/jmbi.1998.1858","article-title":"The mitochondrial processing peptidase behaves as a zinc-metallopeptidase","volume":"280","author":"Luciano","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib17","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/S0969-2126(01)00621-9","article-title":"Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences","volume":"9","author":"Taylor","year":"2001","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2025.110860_bib18","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1016\/j.jmb.2009.12.054","article-title":"Glycine-rich loop of mitochondrial processing peptidase alpha-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20","volume":"396","author":"Dvor\u00e1kov\u00e1-Hol\u00e1","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib19","doi-asserted-by":"crossref","first-page":"34552","DOI":"10.1074\/jbc.M003110200","article-title":"Glycine-rich region of mitochondrial processing peptidase alpha-subunit is essential for binding and cleavage of the precursor proteins","volume":"275","author":"Nagao","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib20","doi-asserted-by":"crossref","first-page":"25158","DOI":"10.1074\/jbc.273.39.25158","article-title":"Role of alpha-subunit of mitochondrial processing peptidase in substrate recognition","volume":"273","author":"Shimokata","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib21","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1146\/annurev-biochem-062917-012739","article-title":"Mitochondrial proteases: multifaceted regulators of mitochondrial plasticity","volume":"89","author":"Deshwal","year":"2020","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jbc.2025.110860_bib22","doi-asserted-by":"crossref","first-page":"D981","DOI":"10.1093\/nar\/gkaa1083","article-title":"Mouse Genome Database (MGD): knowledgebase for mouse-human comparative biology","volume":"49","author":"Blake","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2025.110860_bib23","doi-asserted-by":"crossref","first-page":"e19","DOI":"10.1093\/brain\/awv362","article-title":"Autosomal recessive cerebellar ataxia caused by a homozygous mutation in PMPCA","volume":"139","author":"Choquet","year":"2016","journal-title":"Brain"},{"key":"10.1016\/j.jbc.2025.110860_bib24","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1093\/brain\/awv057","article-title":"PMPCA mutations cause abnormal mitochondrial protein processing in patients with non-progressive cerebellar ataxia","volume":"138","author":"Jobling","year":"2015","journal-title":"Brain"},{"key":"10.1016\/j.jbc.2025.110860_bib25","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.braindev.2020.11.008","article-title":"A severe form of autosomal recessive spinocerebellar ataxia associated with novel PMPCA variants","volume":"43","author":"Takahashi","year":"2021","journal-title":"Brain Dev."},{"key":"10.1016\/j.jbc.2025.110860_bib26","doi-asserted-by":"crossref","DOI":"10.1101\/mcs.a000786","article-title":"Mutations in the substrate binding glycine-rich loop of the mitochondrial processing peptidase-\u03b1 protein (PMPCA) cause a severe mitochondrial disease","volume":"2","author":"Joshi","year":"2016","journal-title":"Cold Spring Harb. Mol. Case Stud."},{"key":"10.1016\/j.jbc.2025.110860_bib27","doi-asserted-by":"crossref","first-page":"e200106","DOI":"10.1212\/NXG.0000000000200106","article-title":"PMPCA-Related encephalopathy: novel variants, phenotype extension, and mitochondrial morphology","volume":"9","author":"Rambani","year":"2023","journal-title":"Neurol. Genet."},{"key":"10.1016\/j.jbc.2025.110860_bib28","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/j.ajhg.2018.02.014","article-title":"Mutations in PMPCB encoding the catalytic subunit of the mitochondrial presequence protease cause neurodegeneration in early childhood","volume":"102","author":"V\u00f6gtle","year":"2018","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.jbc.2025.110860_bib29","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/s10038-024-01226-9","article-title":"Leigh syndrome with developmental regression and ataxia due to a novel splicing variant in the PMPCB gene","volume":"69","author":"Matthews","year":"2024","journal-title":"J. Hum. Genet."},{"key":"10.1016\/j.jbc.2025.110860_bib30","doi-asserted-by":"crossref","first-page":"30322","DOI":"10.1074\/jbc.270.51.30322","article-title":"Analysis of elements in the substrate required for processing by mitochondrial processing peptidase","volume":"270","author":"Ogishima","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib31","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1074\/mcp.M116.063818","article-title":"Comparative analysis of mitochondrial N-Termini from Mouse, human, and yeast","volume":"16","author":"Calvo","year":"2017","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.jbc.2025.110860_bib32","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1126\/science.1096284","article-title":"Hereditary early-onset Parkinson\u2019s disease caused by mutations in PINK1","volume":"304","author":"Valente","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.jbc.2025.110860_bib33","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/nature14893","article-title":"The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy","volume":"524","author":"Lazarou","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2025.110860_bib34","first-page":"964","article-title":"Unconventional PINK1 localization to the outer membrane of depolarized mitochondria drives Parkin recruitment","volume":"128","author":"Okatsu","year":"2015","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2025.110860_bib35","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1016\/j.molcel.2019.01.002","article-title":"Reciprocal roles of Tom7 and OMA1 during mitochondrial import and activation of PINK1","volume":"73","author":"Sekine","year":"2019","journal-title":"Mol. Cell."},{"key":"10.1016\/j.jbc.2025.110860_bib36","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1038\/nchembio.2493","article-title":"Stendomycin selectively inhibits TIM23-dependent mitochondrial protein import","volume":"13","author":"Filipuzzi","year":"2017","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib37","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1038\/embor.2012.14","article-title":"Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment","volume":"13","author":"Greene","year":"2012","journal-title":"EMBO Rep."},{"key":"10.1016\/j.jbc.2025.110860_bib38","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1093\/hmg\/ddq526","article-title":"PINK1 cleavage at position A103 by the mitochondrial protease PARL","volume":"20","author":"Deas","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2025.110860_bib39","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1083\/jcb.201008084","article-title":"Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL","volume":"191","author":"Jin","year":"2010","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib40","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.4161\/auto.24633","article-title":"PINK1 is degraded through the N-end rule pathway","volume":"9","author":"Yamano","year":"2013","journal-title":"Autophagy"},{"key":"10.1016\/j.jbc.2025.110860_bib41","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2313540121","article-title":"Tom20 gates PINK1 activity and mediates its tethering of the TOM and TIM23 translocases upon mitochondrial stress","volume":"121","author":"Eldeeb","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2025.110860_bib42","doi-asserted-by":"crossref","first-page":"112454","DOI":"10.1016\/j.celrep.2023.112454","article-title":"TIM23 facilitates PINK1 activation by safeguarding against OMA1-mediated degradation in damaged mitochondria","volume":"42","author":"Akabane","year":"2023","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2025.110860_bib43","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1038\/nature13392","article-title":"Ubiquitin is phosphorylated by PINK1 to activate parkin","volume":"510","author":"Koyano","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2025.110860_bib44","doi-asserted-by":"crossref","first-page":"36372","DOI":"10.1074\/jbc.M113.509653","article-title":"A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment","volume":"288","author":"Okatsu","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib45","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.molcel.2021.11.012","article-title":"Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex","volume":"82","author":"Rasool","year":"2022","journal-title":"Mol. Cell."},{"key":"10.1016\/j.jbc.2025.110860_bib46","doi-asserted-by":"crossref","first-page":"e1000298","DOI":"10.1371\/journal.pbio.1000298","article-title":"PINK1 is selectively stabilized on impaired mitochondria to activate Parkin","volume":"8","author":"Narendra","year":"2010","journal-title":"Plos Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib47","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.4161\/auto.26122","article-title":"The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2\/Parkin-mediated mitophagy of polarized mitochondria","volume":"9","author":"Jin","year":"2013","journal-title":"Autophagy"},{"key":"10.1016\/j.jbc.2025.110860_bib48","doi-asserted-by":"crossref","first-page":"100383","DOI":"10.1016\/j.jbc.2021.100383","article-title":"Insights into the catalytic properties of the mitochondrial rhomboid protease PARL","volume":"296","author":"Lysyk","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib49","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2025.110860_bib50","doi-asserted-by":"crossref","first-page":"1879","DOI":"10.1074\/jbc.M209263200","article-title":"Determination of the cleavage site of the presequence by mitochondrial processing peptidase on the substrate binding scaffold and the multiple subsites inside a molecular cavity","volume":"278","author":"Kitada","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib51","doi-asserted-by":"crossref","first-page":"e0284541","DOI":"10.1371\/journal.pone.0284541","article-title":"MTSviewer: a database to visualize mitochondrial targeting sequences, cleavage sites, and mutations on protein structures","volume":"18","author":"Bayne","year":"2023","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.110860_bib52","doi-asserted-by":"crossref","first-page":"24719","DOI":"10.1016\/S0021-9258(17)31450-3","article-title":"Arginine residues in the extension peptide are required for cleavage of a precursor by mitochondrial processing peptidase. Demonstration using synthetic peptide as a substrate","volume":"269","author":"Niidome","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib53","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/0009-8981(82)90083-3","article-title":"A highly sensitive colorimetric determination of serum zinc using water-soluble pyridylazo dye","volume":"120","author":"Makino","year":"1982","journal-title":"Clin. Chim. Acta"},{"key":"10.1016\/j.jbc.2025.110860_bib54","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.mito.2019.03.001","article-title":"The first direct activity assay for the mitochondrial protease OMA1","volume":"46","author":"Tobacyk","year":"2019","journal-title":"Mitochondrion"},{"key":"10.1016\/j.jbc.2025.110860_bib55","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1093\/oxfordjournals.jbchem.a022198","article-title":"Importance of residues carboxyl terminal relative to the cleavage site in substrates of mitochondrial processing peptidase for their specific recognition and cleavage","volume":"124","author":"Song","year":"1998","journal-title":"J. Biochem."},{"key":"10.1016\/j.jbc.2025.110860_bib56","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1093\/oxfordjournals.jbchem.a021841","article-title":"Substrate recognition by mitochondrial processing peptidase toward the malate dehydrogenase precursor","volume":"122","author":"Shimokata","year":"1997","journal-title":"J. Biochem."},{"key":"10.1016\/j.jbc.2025.110860_bib57","doi-asserted-by":"crossref","first-page":"19906","DOI":"10.1016\/S0021-9258(19)36598-6","article-title":"Import, processing, and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase","volume":"268","author":"Thornton","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110860_bib58","doi-asserted-by":"crossref","first-page":"8610","DOI":"10.1021\/bi00194a028","article-title":"Structure of the signal sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import","volume":"33","author":"Hammen","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.110860_bib59","doi-asserted-by":"crossref","first-page":"874","DOI":"10.1093\/oxfordjournals.jbchem.a022529","article-title":"Analysis of recognition elements for mitochondrial processing peptidase using artificial amino acids: roles of the intervening portion and proximal arginine","volume":"126","author":"Moriwaki","year":"1999","journal-title":"J. Biochem."},{"key":"10.1016\/j.jbc.2025.110860_bib60","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1110\/ps.3760102","article-title":"Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP)","volume":"11","author":"Mukhopadhyay","year":"2002","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2025.110860_bib61","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1083\/jcb.200403022","article-title":"Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor","volume":"165","author":"Herlan","year":"2004","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib62","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/s12915-017-0470-7","article-title":"PINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol","volume":"16","author":"Sekine","year":"2018","journal-title":"BMC Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib63","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1038\/sj.emboj.7601514","article-title":"m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria","volume":"26","author":"Tatsuta","year":"2007","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2025.110860_bib64","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1016\/S0022-2836(02)01000-8","article-title":"A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1","volume":"323","author":"Esser","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib65","doi-asserted-by":"crossref","first-page":"3163","DOI":"10.1002\/pmic.201400441","article-title":"Version 4.0 of PaxDb: protein abundance data, integrated across model organisms, tissues, and cell-lines","volume":"15","author":"Wang","year":"2015","journal-title":"Proteomics"},{"key":"10.1016\/j.jbc.2025.110860_bib66","doi-asserted-by":"crossref","first-page":"2464","DOI":"10.1016\/j.cmet.2021.11.001","article-title":"Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context","volume":"33","author":"Morgenstern","year":"2021","journal-title":"Cell Metab."},{"key":"10.1016\/j.jbc.2025.110860_bib67","doi-asserted-by":"crossref","first-page":"e52482","DOI":"10.1371\/journal.pone.0052482","article-title":"Stabilizing additives added during cell lysis aid in the solubilization of recombinant proteins","volume":"7","author":"Leibly","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.110860_bib68","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.pep.2005.01.016","article-title":"Protein production by auto-induction in high density shaking cultures","volume":"41","author":"Studier","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jbc.2025.110860_bib71","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1002\/pro.2253","article-title":"Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm","volume":"22","author":"Anthis","year":"2013","journal-title":"Protein Sci"},{"key":"10.1016\/j.jbc.2025.110860_bib69","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1007\/978-1-4939-8820-4_4","article-title":"Differential scanning fluorimetry and hydrogen Deuterium Exchange Mass spectrometry to monitor the conformational dynamics of NBD1 in cystic fibrosis","volume":"1873","author":"Soya","year":"2019","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jbc.2025.110860_bib70","doi-asserted-by":"crossref","first-page":"W404","DOI":"10.1093\/nar\/gkad350","article-title":"PAE viewer: a webserver for the interactive visualization of the predicted aligned error for multimer structure predictions and crosslinks","volume":"51","author":"Elfmann","year":"2023","journal-title":"Nucleic Acids Res."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825027127?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825027127?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,3,18]],"date-time":"2026-03-18T01:48:10Z","timestamp":1773798490000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925825027127"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12]]},"references-count":71,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2025,12]]}},"alternative-id":["S0021925825027127"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2025.110860","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2025,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Substrate recognition by the human mitochondrial processing peptidase and its processing of PINK1","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2025.110860","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology\u00e9","name":"copyright","label":"Copyright"}],"article-number":"110860"}}