{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T12:53:58Z","timestamp":1788872038722,"version":"build-2803163510"},"reference-count":73,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"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":1086,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100004587","name":"Instituto de Salud Carlos III","doi-asserted-by":"publisher","award":["SAF-2007-60934"],"award-info":[{"award-number":["SAF-2007-60934"]}],"id":[{"id":"10.13039\/501100004587","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012818","name":"Comunidad de Madrid","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012818","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006049","name":"Comisi\u00f3n Sectorial de Investigaci\u00f3n Cient\u00edfica","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100006049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013248","name":"Family Process Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100013248","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008054","name":"Fundaci\u00f3n Ram\u00f3n Areces","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100016967","name":"Ministerio de Educaci\u00f3n Superior, Ciencia y Tecnolog\u00eda, Rep\u00fablica Dominicana","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100016967","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"published-print":{"date-parts":[[2010,9]]},"DOI":"10.1016\/j.bbamcr.2010.06.001","type":"journal-article","created":{"date-parts":[[2010,6,9]],"date-time":"2010-06-09T04:50:19Z","timestamp":1276059019000},"page":"1094-1105","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["Accumulation of polyubiquitylated proteins in response to Ala-Ala-Phe-chloromethylketone is independent of the inhibition of tripeptidyl peptidase II"],"prefix":"10.1016","volume":"1803","author":[{"given":"Eugenia M.","family":"Villasevil","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"Guil","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lorena","family":"L\u00f3pez-Ferreras","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos","family":"S\u00e1nchez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Margarita","family":"Del Val","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis C.","family":"Ant\u00f3n","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamcr.2010.06.001_bib1","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/S1357-2725(02)00390-4","article-title":"Substrate access and processing by the 20S proteasome core particle","volume":"35","author":"Groll","year":"2003","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib2","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/nrm1336","article-title":"Proteasomes and their kin: proteases in the machine age","volume":"5","author":"Pickart","year":"2004","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib3","doi-asserted-by":"crossref","first-page":"7151","DOI":"10.1093\/emboj\/17.24.7151","article-title":"The ubiquitin\u2013proteasome pathway: on protein death and cell life","volume":"17","author":"Ciechanover","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib4","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/j.tibs.2005.04.005","article-title":"Regulated protein degradation","volume":"30","author":"Varshavsky","year":"2005","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib5","doi-asserted-by":"crossref","first-page":"46723","DOI":"10.1074\/jbc.M406537200","article-title":"Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases","volume":"279","author":"Saric","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib6","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1038\/nri1250","article-title":"Making sense of mass destruction: quantitating MHC class I antigen presentation","volume":"3","author":"Yewdell","year":"2003","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib7","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/S0161-5890(02)00104-9","article-title":"Multiple proteases process viral antigens for presentation by MHC class I molecules to CD8(+) T lymphocytes","volume":"39","author":"Del Val","year":"2002","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib8","doi-asserted-by":"crossref","first-page":"1823","DOI":"10.4049\/jimmunol.157.5.1823","article-title":"Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules?","volume":"157","author":"Yewdell","year":"1996","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib9","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/35008103","article-title":"The major substrates for TAP in vivo are derived from newly synthesized proteins","volume":"404","author":"Reits","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib10","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1038\/35008096","article-title":"Rapid degradation of a large fraction of newly synthesized proteins by proteasomes","volume":"404","author":"Schubert","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib11","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1016\/0309-1651(80)90045-4","article-title":"Kinetics of degradation of \u2018short-\u2019 and \u2018long-lived\u2019 proteins in cultured mammalian cells","volume":"4","author":"Wheatley","year":"1980","journal-title":"Cell Biol. Int. Rep."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib12","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/35060076","article-title":"c-myc overexpression activates alternative pathways for intracellular proteolysis in lymphoma cells","volume":"3","author":"Gavioli","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib13","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1038\/33443","article-title":"A proteolytic system that compensates for loss of proteasome function","volume":"392","author":"Glas","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib14","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1126\/science.283.5404.978","article-title":"A giant protease with potential to substitute for some functions of the proteasome","volume":"283","author":"Geier","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib15","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.4049\/jimmunol.0803441","article-title":"Processing of two latent membrane protein 1 MHC class I epitopes requires tripeptidyl peptidase II involvement","volume":"183","author":"Diekmann","year":"2009","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib16","doi-asserted-by":"crossref","first-page":"39925","DOI":"10.1074\/jbc.M608522200","article-title":"Need for tripeptidyl-peptidase II in major histocompatibility complex class I viral antigen processing when proteasomes are detrimental","volume":"281","author":"Guil","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib17","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1038\/ni905","article-title":"An essential role for tripeptidyl peptidase in the generation of an MHC class I epitope","volume":"4","author":"Seifert","year":"2003","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib18","doi-asserted-by":"crossref","first-page":"1933","DOI":"10.1016\/j.biocel.2005.02.009","article-title":"Tripeptidyl-peptidase II: a multi-purpose peptidase","volume":"37","author":"Tomkinson Test","year":"2005","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib19","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/S1074-7613(04)00074-3","article-title":"A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation","volume":"20","author":"Reits","year":"2004","journal-title":"Immunity"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib20","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1073\/pnas.98.2.513","article-title":"Cells adapted to the proteasome inhibitor 4-hydroxy-5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survival","volume":"98","author":"Princiotta","year":"2001","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib21","doi-asserted-by":"crossref","first-page":"9990","DOI":"10.1073\/pnas.180328897","article-title":"Integration of the ubiquitin\u2013proteasome pathway with a cytosolic oligopeptidase activity","volume":"97","author":"Wang","year":"2000","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib22","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1084\/jem.20020801","article-title":"Tumors acquire inhibitor of apoptosis protein (IAP)-mediated apoptosis resistance through altered specificity of cytosolic proteolysis","volume":"197","author":"Hong","year":"2003","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib23","doi-asserted-by":"crossref","first-page":"24769","DOI":"10.1074\/jbc.271.40.24769","article-title":"Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells","volume":"271","author":"Zhou","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib24","doi-asserted-by":"crossref","first-page":"9086","DOI":"10.1074\/jbc.272.14.9086","article-title":"Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance","volume":"272","author":"Bush","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib25","doi-asserted-by":"crossref","first-page":"4859","DOI":"10.4049\/jimmunol.160.10.4859","article-title":"Dissociation of proteasomal degradation of biosynthesized viral proteins from generation of MHC class I-associated antigenic peptides","volume":"160","author":"Ant\u00f3n","year":"1998","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib26","doi-asserted-by":"crossref","first-page":"1883","DOI":"10.1083\/jcb.143.7.1883","article-title":"Aggresomes: a cellular response to misfolded proteins","volume":"143","author":"Johnston","year":"1998","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib27","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1083\/jcb.146.1.113","article-title":"Intracellular localization of proteasomal degradation of a viral antigen","volume":"146","author":"Ant\u00f3n","year":"1999","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib28","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1083\/jcb.146.6.1239","article-title":"Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera","volume":"146","author":"Garc\u00eda-Mata","year":"1999","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib29","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1083\/jcb.145.3.481","article-title":"Dynamic association of proteasomal machinery with the centrosome","volume":"145","author":"Wigley","year":"1999","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib30","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/S0092-8674(03)00939-5","article-title":"The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress","volume":"115","author":"Kawaguchi","year":"2003","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib31","first-page":"311","article-title":"Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome","volume":"71","author":"W\u00f3jcik","year":"1996","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib32","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0896-6273(01)00177-5","article-title":"Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases","volume":"29","author":"Sherman","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib33","doi-asserted-by":"crossref","first-page":"8567","DOI":"10.1073\/pnas.0503221102","article-title":"Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma","volume":"102","author":"Hideshima","year":"2005","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib34","doi-asserted-by":"crossref","first-page":"3773","DOI":"10.1158\/0008-5472.CAN-05-2961","article-title":"Aggresome disruption: a novel strategy to enhance bortezomib-induced apoptosis in pancreatic cancer cells","volume":"66","author":"Nawrocki","year":"2006","journal-title":"Cancer Res."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib35","doi-asserted-by":"crossref","first-page":"329","DOI":"10.4049\/jimmunol.164.1.329","article-title":"Limited diversity of peptides related to an alloreactive T cell epitope in the HLA-B27-bound peptide repertoire results from restrictions at multiple steps along the processing-loading pathway","volume":"164","author":"Paradela","year":"2000","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib36","doi-asserted-by":"crossref","first-page":"38818","DOI":"10.1074\/jbc.M205547200","article-title":"Fusion proteins with COOH-terminal ubiquitin are stable and maintain dual functionality in vivo","volume":"277","author":"Qian","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib37","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1126\/science.292.5521.1552","article-title":"Impairment of the ubiquitin\u2013proteasome system by protein aggregation","volume":"292","author":"Bence","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib38","unstructured":"Rasband, Wayne S. (2009) ImageJ http:\/\/rsb.info.nih.gov\/ij\/ U. S. National Institutes of Health, Bethesda, Maryland, USA."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib39","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/0003-2697(86)90166-1","article-title":"Enhancement of immunoblot sensitivity by heating of hydrated filters","volume":"156","author":"Swerdlow","year":"1986","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib40","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/S0962-8924(00)01852-3","article-title":"Aggresomes, inclusion bodies and protein aggregation","volume":"10","author":"Kopito","year":"2000","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib41","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1083\/jcb.200510071","article-title":"A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling","volume":"173","author":"Dantuma","year":"2006","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib42","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.4049\/jimmunol.176.4.2249","article-title":"Re-evaluating the generation of a \u201cproteasome-independent\u201d MHC class I-restricted CD8 T cell epitope","volume":"176","author":"Wherry","year":"2006","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib43","doi-asserted-by":"crossref","first-page":"14418","DOI":"10.1021\/bi970998j","article-title":"Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: effects on replication, transcription, translation, and the cellular stress response","volume":"36","author":"Mimnaugh","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib44","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/0167-4838(88)90035-0","article-title":"Inactivation of chymotrypsin and human skin chymase: kinetics of time-dependent inhibition in the presence of substrate","volume":"953","author":"Johnson","year":"1988","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib45","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1038\/380403a0","article-title":"Characterization and inhibition of a cholecystokinin-inactivating serine peptidase","volume":"380","author":"Rose","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib46","doi-asserted-by":"crossref","first-page":"5177","DOI":"10.1073\/pnas.0801413105","article-title":"Activation of cellular death programs associated with immunosenescence-like phenotype in TPPII knockout mice","volume":"105","author":"Huai","year":"2008","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib47","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1038\/nrc1716","article-title":"HSP90 and the chaperoning of cancer","volume":"5","author":"Whitesell Test","year":"2005","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib48","doi-asserted-by":"crossref","first-page":"22796","DOI":"10.1074\/jbc.271.37.22796","article-title":"Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin","volume":"271","author":"Mimnaugh","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib49","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1042\/BJ20071640","article-title":"The Hsp90 molecular chaperone: an open and shut case for treatment","volume":"410","author":"Pearl","year":"2008","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib50","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/s002800050817","article-title":"The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin","volume":"42","author":"Schulte","year":"1998","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib51","doi-asserted-by":"crossref","first-page":"27575","DOI":"10.1074\/jbc.M802216200","article-title":"Triggering aggresome formation: dissecting aggresome-targeting and aggregation signals in synphilin 1","volume":"283","author":"Zaarur","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib52","doi-asserted-by":"crossref","first-page":"50908","DOI":"10.1074\/jbc.M307637200","article-title":"G protein-coupled receptor kinase interaction with Hsp90 mediates kinase maturation","volume":"278","author":"Luo Test","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib53","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1042\/BST0360839","article-title":"Is there an alternative to the proteasome in cytosolic protein degradation?","volume":"36","author":"Ant\u00f3n","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib54","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1002\/jcb.21405","article-title":"Increased expression and altered subunit composition of proteasomes induced by continuous proteasome inhibition establish apoptosis resistance and hyperproliferation of Burkitt lymphoma cells","volume":"103","author":"Fuchs","year":"2007","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib55","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.1038\/leu.2009.8","article-title":"Characterization of the ubiquitin\u2013proteasome system in bortezomib-adapted cells","volume":"23","author":"R\u00fcckrich","year":"2009","journal-title":"Leukemia"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib56","doi-asserted-by":"crossref","first-page":"10013","DOI":"10.1074\/jbc.M211221200","article-title":"Pathways accessory to proteasomal proteolysis are less efficient in major histocompatibility complex class I antigen production","volume":"278","author":"Kessler","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib57","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1158\/0008-5472.CAN-04-2085","article-title":"Mitotic infidelity and centrosome duplication errors in cells overexpressing tripeptidyl-peptidase II","volume":"65","author":"Stavropoulou","year":"2005","journal-title":"Cancer Res."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib58","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.bbrc.2006.05.141","article-title":"TPPII promotes genetic instability by allowing the escape from apoptosis of cells with activated mitotic checkpoints","volume":"346","author":"Stavropoulou","year":"2006","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib59","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1158\/1535-7163.MCT-08-0735","article-title":"Aminopeptidase inhibition as a targeted treatment strategy in myeloma","volume":"8","author":"Moore","year":"2009","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib60","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1038\/sj.leu.2401388","article-title":"Induction of apoptosis by bestatin (ubenimex) in human leukemic cell lines","volume":"13","author":"Sekine","year":"1999","journal-title":"Leukemia"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib61","doi-asserted-by":"crossref","first-page":"1434","DOI":"10.4049\/jimmunol.177.3.1434","article-title":"Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation","volume":"177","author":"York","year":"2006","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib62","doi-asserted-by":"crossref","first-page":"8582","DOI":"10.1074\/jbc.M509043200","article-title":"Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate","volume":"281","author":"Kisselev","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib63","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1038\/sj.embor.7401086","article-title":"Tripeptidyl peptidase II promotes fat formation in a conserved fashion","volume":"8","author":"McKay","year":"2007","journal-title":"EMBO Rep."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib64","doi-asserted-by":"crossref","first-page":"8137","DOI":"10.4049\/jimmunol.179.12.8137","article-title":"Analysis of direct and cross-presentation of antigens in TPPII knockout mice1","volume":"179","author":"Firat","year":"2007","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib65","doi-asserted-by":"crossref","first-page":"6069","DOI":"10.4049\/jimmunol.0803564","article-title":"Analysis of the role of tripeptidyl peptidase II in MHC class I antigen presentation in vivo","volume":"183","author":"Kawahara","year":"2009","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib66","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1083\/jcb.200104079","article-title":"Hsp90: a specialized but essential protein-folding tool","volume":"154","author":"Young","year":"2001","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib67","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1093\/embo-reports\/kve206","article-title":"From the cradle to the grave: molecular chaperones that may choose between folding and degradation","volume":"2","author":"H\u00f6hfeld","year":"2001","journal-title":"EMBO Rep."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib68","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1038\/35050618","article-title":"The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins","volume":"3","author":"Connell","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib69","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1016\/j.cell.2006.09.051","article-title":"Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities","volume":"127","author":"Crosas","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib70","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.molcel.2005.12.014","article-title":"Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone","volume":"21","author":"Rumpf","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib71","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1038\/sj.leu.2404278","article-title":"Proteasome inhibitor bortezomib for the treatment of multiple myeloma","volume":"20","author":"Cavo","year":"2006","journal-title":"Leukemia"},{"key":"10.1016\/j.bbamcr.2010.06.001_bib72","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1158\/1078-0432.CCR-06-2966","article-title":"Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells","volume":"13","author":"Xu","year":"2007","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.bbamcr.2010.06.001_bib73","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1158\/1078-0432.CCR-06-1892","article-title":"Phase I pharmacokinetic and pharmacodynamic study of 17-n-allylamino-17-demethoxygeldanamycin in pediatric patients with recurrent or refractory solid tumors: a pediatric oncology experimental therapeutics investigators consortium study","volume":"13","author":"Bagatell","year":"2007","journal-title":"Clin. Cancer Res."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167488910001618?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167488910001618?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,28]],"date-time":"2025-09-28T19:43:41Z","timestamp":1759088621000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0167488910001618"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,9]]},"references-count":73,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2010,9]]}},"alternative-id":["S0167488910001618"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamcr.2010.06.001","relation":{},"ISSN":["0167-4889"],"issn-type":[{"value":"0167-4889","type":"print"}],"subject":[],"published":{"date-parts":[[2010,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Accumulation of polyubiquitylated proteins in response to Ala-Ala-Phe-chloromethylketone is independent of the inhibition of tripeptidyl peptidase II","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Cell Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamcr.2010.06.001","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2010 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}