{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:14:21Z","timestamp":1791306861461,"version":"4.3.1"},"reference-count":41,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2005,10,1]],"date-time":"2005-10-01T00:00:00Z","timestamp":1128124800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2005,10,1]],"date-time":"2005-10-01T00:00:00Z","timestamp":1128124800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2013,8,22]],"date-time":"2013-08-22T00:00:00Z","timestamp":1377129600000},"content-version":"vor","delay-in-days":2882,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2005,10,1]],"date-time":"2005-10-01T00:00:00Z","timestamp":1128124800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2005,10,1]],"date-time":"2005-10-01T00:00:00Z","timestamp":1128124800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2005,10,1]],"date-time":"2005-10-01T00:00:00Z","timestamp":1128124800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2005,10,1]],"date-time":"2005-10-01T00:00:00Z","timestamp":1128124800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2005,10,1]],"date-time":"2005-10-01T00:00:00Z","timestamp":1128124800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell"],"published-print":{"date-parts":[[2005,10]]},"DOI":"10.1016\/j.cell.2005.08.003","type":"journal-article","created":{"date-parts":[[2005,10,21]],"date-time":"2005-10-21T07:13:38Z","timestamp":1129878818000},"page":"277-289","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":365,"title":["The m-AAA Protease Defective in Hereditary Spastic Paraplegia Controls Ribosome Assembly in Mitochondria"],"prefix":"10.1016","volume":"123","author":[{"given":"Mark","family":"Nolden","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah","family":"Ehses","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mirko","family":"Koppen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Bernacchia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena I.","family":"Rugarli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Langer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cell.2005.08.003_bib1","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1016\/S0092-8674(00)81271-4","article-title":"The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria","volume":"85","author":"Arlt","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.cell.2005.08.003_bib2","doi-asserted-by":"crossref","first-page":"4837","DOI":"10.1093\/emboj\/17.16.4837","article-title":"The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease","volume":"17","author":"Arlt","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2005.08.003_bib3","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1083\/jcb.200304112","article-title":"Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia","volume":"163","author":"Atorino","year":"2003","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.cell.2005.08.003_bib4","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1091\/mbc.5.8.899","article-title":"Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue","volume":"5","author":"Campbell","year":"1994","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.cell.2005.08.003_bib5","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/S0092-8674(00)81203-9","article-title":"Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease","volume":"93","author":"Casari","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.cell.2005.08.003_bib6","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/nrm1552","article-title":"Proteolysis: from the lysosome to ubiquitin and the proteasome","volume":"6","author":"Ciechanover","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.cell.2005.08.003_bib7","doi-asserted-by":"crossref","first-page":"2656","DOI":"10.1056\/NEJMra022567","article-title":"Mitochondrial respiratory-chain diseases","volume":"348","author":"DiMauro","year":"2003","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.cell.2005.08.003_bib8","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1172\/JCI200420138","article-title":"Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport","volume":"113","author":"Ferreirinha","year":"2004","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.cell.2005.08.003_bib9","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1128\/EC.2.3.651-653.2003","article-title":"Evidence that synthesis of the Saccharomyces cerevisiae mitochondrially encoded ribosomal protein Var1p may be membrane localized","volume":"2","author":"Fiori","year":"2003","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.cell.2005.08.003_bib10","doi-asserted-by":"crossref","first-page":"38338","DOI":"10.1074\/jbc.M405871200","article-title":"Reversible assembly of the ATP-binding cassette transporter Mdl1 with the F1FO-ATP synthase in mitochondria","volume":"279","author":"Galluhn","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2005.08.003_bib11","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/0014-5793(91)80759-V","article-title":"Extended N-terminal sequencing of proteins of the large ribosomal subunit from yeast mitochondria","volume":"284","author":"Grohmann","year":"1991","journal-title":"FEBS Lett."},{"key":"10.1016\/j.cell.2005.08.003_bib12","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1002\/yea.320101016","article-title":"Sequence of the AFG3 gene encoding a new member of the FtsH\/Yme1\/Tma subfamily of the AAA-protein family","volume":"10","author":"Gu\u00e9lin","year":"1994","journal-title":"Yeast"},{"key":"10.1016\/j.cell.2005.08.003_bib13","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/S0092-8674(01)00546-3","article-title":"High resolution structure of the large ribosomal subunit from a mesophilic eubacterium","volume":"107","author":"Harms","year":"2001","journal-title":"Cell"},{"key":"10.1016\/j.cell.2005.08.003_bib14","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.tig.2005.04.003","article-title":"Nuclear genes and mitochondrial translation: a new class of genetic disease","volume":"21","author":"Jacobs","year":"2005","journal-title":"Trends Genet."},{"key":"10.1016\/j.cell.2005.08.003_bib15","doi-asserted-by":"crossref","first-page":"3863","DOI":"10.1002\/j.1460-2075.1988.tb03272.x","article-title":"Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit","volume":"7","author":"Jensen","year":"1988","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2005.08.003_bib16","doi-asserted-by":"crossref","first-page":"6438","DOI":"10.1093\/emboj\/cdg624","article-title":"Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1","volume":"22","author":"Jia","year":"2003","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2005.08.003_bib17","doi-asserted-by":"crossref","first-page":"20132","DOI":"10.1074\/jbc.M500398200","article-title":"Role of the novel metallopeptidase MOP112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria","volume":"280","author":"Kambacheld","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2005.08.003_bib18","doi-asserted-by":"crossref","first-page":"5967","DOI":"10.4049\/jimmunol.161.11.5967","article-title":"MHC class I molecules compete in the endoplasmic reticulum for access to transporter associated with antigen processing","volume":"161","author":"Knittler","year":"1998","journal-title":"J. Immunol."},{"key":"10.1016\/j.cell.2005.08.003_bib19","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1007\/s00294-004-0503-y","article-title":"Saccharomyces cerevisiae translational activator Cbs2p is associated with mitochondrial ribosomes","volume":"46","author":"Krause-Buchholz","year":"2004","journal-title":"Curr. Genet."},{"key":"10.1016\/j.cell.2005.08.003_bib20","doi-asserted-by":"crossref","first-page":"4218","DOI":"10.1002\/j.1460-2075.1996.tb00796.x","article-title":"AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria","volume":"15","author":"Leonhard","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2005.08.003_bib21","doi-asserted-by":"crossref","first-page":"29400","DOI":"10.1074\/jbc.M002173200","article-title":"Interaction of mammalian mitochondrial ribosomes with the inner membrane","volume":"275","author":"Liu","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2005.08.003_bib22","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1136\/jnnp.69.2.150","article-title":"Hereditary spastic paraparesis: a review of new developments","volume":"69","author":"McDermott","year":"2000","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"10.1016\/j.cell.2005.08.003_bib23","doi-asserted-by":"crossref","first-page":"11737","DOI":"10.1016\/S0021-9258(19)50261-7","article-title":"COX3 mRNA-specific translational activator proteins are associated with the inner mitochondrial membrane in Saccharomyces cerevisiae","volume":"268","author":"McMullin","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2005.08.003_bib24","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1007\/BF00290666","article-title":"Association of cytochrome b translational activator proteins with the mitochondrial membrane: implications for cytochrome b expression in yeast","volume":"230","author":"Michaelis","year":"1991","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.cell.2005.08.003_bib25","doi-asserted-by":"crossref","first-page":"2087","DOI":"10.1002\/j.1460-2075.1985.tb03896.x","article-title":"Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae","volume":"4","author":"Myers","year":"1985","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2005.08.003_bib26","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1091\/mbc.e02-08-0490","article-title":"Interactions among COX1, COX2, and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae","volume":"14","author":"Naithani","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.cell.2005.08.003_bib27","unstructured":"Nolden, M., Kisters-Woike, B., Langer, T., and Graef, M. (2005). Quality control of proteins in the mitochondrion. Curr. Topics Gen., in press."},{"key":"10.1016\/j.cell.2005.08.003_bib28","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.bbamcr.2004.09.022","article-title":"Productive RUPture: activation of transcription factors by proteasomal processing","volume":"1695","author":"Rape","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.cell.2005.08.003_bib29","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1007\/s002940050122","article-title":"Three genes for mitochondrial proteins suppress null-mutations in both AFG3 and RCA1 when overexpressed","volume":"30","author":"Rep","year":"1996","journal-title":"Curr. Genet."},{"key":"10.1016\/j.cell.2005.08.003_bib30","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1042\/bj20021594","article-title":"Mitochondrial threshold effects","volume":"370","author":"Rossignol","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.cell.2005.08.003_bib31","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/BF00267380","article-title":"Mutations of the mitochondrial DNA of Saccharomyces cerevisiae which affect the interaction between mitochondrial ribosomes and the inner mitochondrial membrane","volume":"164","author":"Spithill","year":"1978","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.cell.2005.08.003_bib32","doi-asserted-by":"crossref","first-page":"3435","DOI":"10.1128\/MCB.19.5.3435","article-title":"Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria","volume":"19","author":"Steglich","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.cell.2005.08.003_bib33","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1126\/science.8146662","article-title":"Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration","volume":"264","author":"Suzuki","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.cell.2005.08.003_bib34","doi-asserted-by":"crossref","first-page":"6448","DOI":"10.1093\/emboj\/cdg623","article-title":"Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria","volume":"22","author":"Szyrach","year":"2003","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2005.08.003_bib35","unstructured":"Tatsuta, T., and Langer, T. (2005). Studying proteolysis within mitochondria. Curr. Topics Gen., in press."},{"key":"10.1016\/j.cell.2005.08.003_bib36","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/nrg1606","article-title":"Mitochondrial DNA mutations in human disease","volume":"6","author":"Taylor","year":"2005","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.cell.2005.08.003_bib37","first-page":"5418","article-title":"Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae","volume":"13","author":"Thorsness","year":"1993","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.cell.2005.08.003_bib38","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1126\/science.7973708","article-title":"The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria","volume":"266","author":"Ungermann","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.cell.2005.08.003_bib39","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1002\/jemt.1070270404","article-title":"A morphological view on mitochondrial protein targeting","volume":"27","author":"Van der Klei","year":"1994","journal-title":"Microsc. Res. Tech."},{"key":"10.1016\/j.cell.2005.08.003_bib40","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1007\/s000180050029","article-title":"ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae","volume":"55","author":"Van Dyck","year":"1999","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.cell.2005.08.003_bib41","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/S0021-9258(17)42340-4","article-title":"PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae","volume":"269","author":"Van Dyck","year":"1994","journal-title":"J. Biol. Chem."}],"container-title":["Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867405008068?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867405008068?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,25]],"date-time":"2025-09-25T10:54:03Z","timestamp":1758797643000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0092867405008068"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,10]]},"references-count":41,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2005,10]]}},"alternative-id":["S0092867405008068"],"URL":"https:\/\/doi.org\/10.1016\/j.cell.2005.08.003","relation":{},"ISSN":["0092-8674"],"issn-type":[{"value":"0092-8674","type":"print"}],"subject":[],"published":{"date-parts":[[2005,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The m-AAA Protease Defective in Hereditary Spastic Paraplegia Controls Ribosome Assembly in Mitochondria","name":"articletitle","label":"Article Title"},{"value":"Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cell.2005.08.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2005 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}