{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T06:22:35Z","timestamp":1791354155913,"version":"4.3.1"},"reference-count":147,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2012,1,1]],"date-time":"2012-01-01T00:00:00Z","timestamp":1325376000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2012,1,1]],"date-time":"2012-01-01T00:00:00Z","timestamp":1325376000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":563,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemistry & Biology"],"published-print":{"date-parts":[[2012,1]]},"DOI":"10.1016\/j.chembiol.2012.01.003","type":"journal-article","created":{"date-parts":[[2012,1,30]],"date-time":"2012-01-30T04:33:00Z","timestamp":1327897980000},"page":"99-115","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":499,"title":["Proteasome Inhibitors: An Expanding Army Attacking a Unique Target"],"prefix":"10.1016","volume":"19","author":[{"given":"Alexei\u00a0F.","family":"Kisselev","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wouter A.","family":"van\u00a0der\u00a0Linden","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Herman\u00a0S.","family":"Overkleeft","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.chembiol.2012.01.003_bib1","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/S1535-6108(04)00120-5","article-title":"The development of proteasome inhibitors as anticancer drugs","volume":"5","author":"Adams","year":"2004","journal-title":"Cancer Cell"},{"key":"10.1016\/j.chembiol.2012.01.003_bib2","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/S0960-894X(98)00029-8","article-title":"Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids","volume":"8","author":"Adams","year":"1998","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.chembiol.2012.01.003_bib3","first-page":"2615","article-title":"Proteasome inhibitors: a novel class of potent and effective antitumor agents","volume":"59","author":"Adams","year":"1999","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib4","first-page":"2505","article-title":"A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies","volume":"8","author":"Aghajanian","year":"2002","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib5","doi-asserted-by":"crossref","first-page":"7896","DOI":"10.1158\/0008-5472.CAN-05-0506","article-title":"Effects of PS-341 on the activity and composition of proteasomes in multiple myeloma cells","volume":"65","author":"Altun","year":"2005","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib6","doi-asserted-by":"crossref","first-page":"13120","DOI":"10.1073\/pnas.95.22.13120","article-title":"An inhibitor of HIV-1 protease modulates proteasome activity, antigen presentation, and T\u00a0cell responses","volume":"95","author":"Andr\u00e9","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2012.01.003_bib7","doi-asserted-by":"crossref","first-page":"2734","DOI":"10.1158\/1078-0432.CCR-10-1950","article-title":"Nonproteasomal targets of the proteasome inhibitors bortezomib and carfilzomib: a link to clinical adverse events","volume":"17","author":"Arastu-Kapur","year":"2011","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib8","doi-asserted-by":"crossref","first-page":"7156","DOI":"10.1073\/pnas.94.14.7156","article-title":"Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation","volume":"94","author":"Arendt","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2012.01.003_bib9","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.bcp.2003.08.035","article-title":"A new structural class of proteasome inhibitors identified by microbial screening using yeast-based assay","volume":"67","author":"Asai","year":"2004","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib10","doi-asserted-by":"crossref","first-page":"634","DOI":"10.4049\/jimmunol.0903182","article-title":"Prevention of experimental colitis by a selective inhibitor of the immunoproteasome","volume":"185","author":"Basler","year":"2010","journal-title":"J.\u00a0Immunol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib11","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/nmeth759","article-title":"Activity probe for in\u00a0vivo profiling of the specificity of proteasome inhibitor bortezomib","volume":"2","author":"Berkers","year":"2005","journal-title":"Nat. Methods"},{"key":"10.1016\/j.chembiol.2012.01.003_bib12","doi-asserted-by":"crossref","first-page":"3040","DOI":"10.1182\/blood-2008-08-172734","article-title":"The proteasome load versus capacity balance determines apoptotic sensitivity of multiple myeloma cells to proteasome inhibition","volume":"113","author":"Bianchi","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2012.01.003_bib13","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1042\/BJ20100383","article-title":"Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S beta5-subunit","volume":"430","author":"Blackburn","year":"2010","journal-title":"Biochem. J."},{"key":"10.1016\/j.chembiol.2012.01.003_bib14","doi-asserted-by":"crossref","first-page":"6629","DOI":"10.1073\/pnas.94.13.6629","article-title":"Covalent modification of the active site threonine of proteasome beta subunits and the Escherichia coli homologs HslV by a new class of inhibitors","volume":"94","author":"Bogyo","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2012.01.003_bib15","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1016\/j.chembiol.2009.11.015","article-title":"Selective inhibitor of proteasome's caspase-like sites sensitizes cells to specific inhibition of chymotrypsin-like sites","volume":"16","author":"Britton","year":"2009","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib16","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1038\/sj.emboj.7601009","article-title":"Progressively impaired proteasomal capacity during terminal plasma cell differentiation","volume":"25","author":"Cenci","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/j.chembiol.2012.01.003_bib17","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.ceb.2010.11.004","article-title":"Proteostenosis and plasma cell pathophysiology","volume":"23","author":"Cenci","year":"2011","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib18","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/j.ccr.2005.10.013","article-title":"A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from Bortezomib","volume":"8","author":"Chauhan","year":"2005","journal-title":"Cancer Cell"},{"key":"10.1016\/j.chembiol.2012.01.003_bib19","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1146\/annurev.pharmtox.45.120403.100037","article-title":"Proteasome inhibition in multiple myeloma: therapeutic implication","volume":"45","author":"Chauhan","year":"2005","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib20","doi-asserted-by":"crossref","first-page":"5311","DOI":"10.1158\/1078-0432.CCR-11-0476","article-title":"Vitro and in\u00a0vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor mln9708 against multiple myeloma cells","volume":"17","author":"Chauhan","year":"2011","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib21","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/S0092-8674(00)80171-3","article-title":"Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly","volume":"86","author":"Chen","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2012.01.003_bib22","doi-asserted-by":"crossref","first-page":"4318","DOI":"10.1158\/0008-5472.CAN-09-4428","article-title":"Genome-wide siRNA screen for modulators of cell death induced by proteasome inhibitor bortezomib","volume":"70","author":"Chen","year":"2010","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib23","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1146\/annurev.bi.65.070196.004101","article-title":"Structure and functions of the 20S and 26S proteasomes","volume":"65","author":"Coux","year":"1996","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib24","doi-asserted-by":"crossref","first-page":"13437","DOI":"10.1074\/jbc.272.20.13437","article-title":"Lactacystin and clasto-lactacystin \u03b2-lactone modify multiple proteasome \u03b2-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation","volume":"272","author":"Craiu","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib25","doi-asserted-by":"crossref","first-page":"4080","DOI":"10.1128\/AAC.00088-09","article-title":"The proteasome inhibitor epoxomicin has potent Plasmodium falciparum gametocytocidal activity","volume":"53","author":"Czesny","year":"2009","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.chembiol.2012.01.003_bib26","doi-asserted-by":"crossref","first-page":"1636","DOI":"10.1038\/nm.2536","article-title":"Inhibition of proteasome deubiquitinating activity as a new cancer therapy","volume":"17","author":"D'Arcy","year":"2011","journal-title":"Nat. Med."},{"key":"10.1016\/j.chembiol.2012.01.003_bib27","doi-asserted-by":"crossref","first-page":"6383","DOI":"10.1158\/0008-5472.CAN-06-4086","article-title":"Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome","volume":"67","author":"Demo","year":"2007","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib28","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1074\/jbc.272.1.182","article-title":"Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells","volume":"272","author":"Dick","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib29","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s00109-003-0422-2","article-title":"Proteasome inhibition: a new anti-inflammatory strategy","volume":"81","author":"Elliott","year":"2003","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.chembiol.2012.01.003_bib30","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/S0091-6749(99)70369-6","article-title":"Proteasome inhibition: A novel mechanism to combat asthma","volume":"104","author":"Elliott","year":"1999","journal-title":"J. Allergy Clin. Immunol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib31","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1016\/S1074-5521(99)80128-8","article-title":"Towards subunit-specific proteasome inhibitors: synthesis and evaluation of peptide alpha\u2032,beta\u2032-epoxyketones","volume":"6","author":"Elofsson","year":"1999","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib32","first-page":"323","article-title":"A summary of bortezomib use in transplantation across 29 centers","author":"Everly","year":"2009","journal-title":"Clin. Transpl."},{"key":"10.1016\/j.chembiol.2012.01.003_bib33","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1038\/sj.onc.1210744","article-title":"BCL-2 family regulation by the 20S proteasome inhibitor bortezomib","volume":"27","author":"Fennell","year":"2008","journal-title":"Oncogene"},{"key":"10.1016\/j.chembiol.2012.01.003_bib34","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1126\/science.7732382","article-title":"Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin","volume":"268","author":"Fenteany","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2012.01.003_bib35","doi-asserted-by":"crossref","first-page":"6294","DOI":"10.1158\/0008-5472.CAN-05-0686","article-title":"Differential regulation of noxa in normal melanocytes and melanoma cells by proteasome inhibition: therapeutic implications","volume":"65","author":"Fern\u00e1ndez","year":"2005","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib36","doi-asserted-by":"crossref","first-page":"1578","DOI":"10.1046\/j.1471-4159.1994.63041578.x","article-title":"A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces accumulation of ubiquitin-protein conjugates in a neuronal cell","volume":"63","author":"Figueiredo-Pereira","year":"1994","journal-title":"J. Neurochem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib37","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1146\/annurev.biochem.78.081507.101607","article-title":"Recognition and processing of ubiquitin-protein conjugates by the proteasome","volume":"78","author":"Finley","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib38","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1021\/cb100408w","article-title":"Active-site-directed chemical tools for profiling mitochondrial Lon protease","volume":"6","author":"Fishovitz","year":"2011","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib39","doi-asserted-by":"crossref","first-page":"2401","DOI":"10.1002\/eji.200838413","article-title":"Dual inhibition of proteasomal and lysosomal proteolysis ameliorates autoimmune central nervous system inflammation","volume":"38","author":"Fissolo","year":"2008","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib40","doi-asserted-by":"crossref","first-page":"8264","DOI":"10.1021\/bi060542e","article-title":"Identification of the proteasome inhibitor MG262 as a potent ATP-dependent inhibitor of the Salmonella enterica serovar Typhimurium Lon protease","volume":"45","author":"Frase","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2012.01.003_bib41","doi-asserted-by":"crossref","first-page":"4810","DOI":"10.1021\/jm049660v","article-title":"Entry into a new class of potent proteasome inhibitors having high antiproliferative activity by structure-based design","volume":"47","author":"Furet","year":"2004","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib42","doi-asserted-by":"crossref","first-page":"8663","DOI":"10.1021\/bi034784f","article-title":"Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity","volume":"42","author":"Gaczynska","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2012.01.003_bib147","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1002\/anie.201106010","article-title":"Hydroxyureas as noncovalent proteasome inhibitors","volume":"51","author":"Gallastegui","year":"2012","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.chembiol.2012.01.003_bib43","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1038\/nm1683","article-title":"In\u00a0vivo gene silencing identifies the Mycobacterium tuberculosis proteasome as essential for the bacteria to persist in mice","volume":"13","author":"Gandotra","year":"2007","journal-title":"Nat. Med."},{"key":"10.1016\/j.chembiol.2012.01.003_bib44","doi-asserted-by":"crossref","first-page":"247","DOI":"10.2174\/1389557023406142","article-title":"Recent advances in the identification and development of 20S proteasome inhibitors","volume":"2","author":"Garc\u00eda-Echeverr\u00eda","year":"2002","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib45","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1172\/JCI16198","article-title":"Selective inhibitors of the osteoblast proteasome stimulate bone formation in\u00a0vivo and in\u00a0vitro","volume":"111","author":"Garrett","year":"2003","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.chembiol.2012.01.003_bib46","doi-asserted-by":"crossref","first-page":"2319","DOI":"10.1021\/jm9015685","article-title":"Incorporation of fluorinated phenylalanine generates highly specific inhibitor of proteasome's chymotrypsin-like sites","volume":"53","author":"Geurink","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib47","series-title":"Bortezomib in the Treatment of Multiple Myeloma","first-page":"1","article-title":"Bortezomib's Scientific Origins and Its Tortuous Path to the Clinic","author":"Goldberg","year":"2010"},{"key":"10.1016\/j.chembiol.2012.01.003_bib48","doi-asserted-by":"crossref","first-page":"2503","DOI":"10.4049\/jimmunol.1002539","article-title":"Proteasome inhibition with bortezomib depletes plasma cells and autoantibodies in experimental autoimmune myasthenia gravis","volume":"186","author":"Gomez","year":"2011","journal-title":"J. Immunol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib49","doi-asserted-by":"crossref","first-page":"2164","DOI":"10.1210\/me.2005-0458","article-title":"Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors","volume":"21","author":"Granot","year":"2007","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib50","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1002\/anie.201005488","article-title":"Elucidation of the \u03b1-keto-aldehyde binding mechanism: a lead structure motif for proteasome inhibition","volume":"50","author":"Gr\u00e4wert","year":"2011","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.chembiol.2012.01.003_bib51","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.bbamcr.2004.09.025","article-title":"Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach","volume":"1695","author":"Groll","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.chembiol.2012.01.003_bib52","doi-asserted-by":"crossref","first-page":"2850","DOI":"10.2174\/156802611798281320","article-title":"Proteasome structure, function, and lessons learned from beta-lactone inhibitors","volume":"11","author":"Groll","year":"2011","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib53","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1021\/ja993588m","article-title":"Crystal structure of epoxomicin: 20S proteasome reveals a molecular basis for selectivity of \u03b1\u2032,beta\u2032-epoxyketone proteasome inhibitors","volume":"122","author":"Groll","year":"2000","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2012.01.003_bib54","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1016\/S1074-5521(02)00144-8","article-title":"Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome","volume":"9","author":"Groll","year":"2002","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib55","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1016\/j.str.2005.11.019","article-title":"Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome","volume":"14","author":"Groll","year":"2006","journal-title":"Structure"},{"key":"10.1016\/j.chembiol.2012.01.003_bib56","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.chembiol.2006.04.005","article-title":"TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome","volume":"13","author":"Groll","year":"2006","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib57","doi-asserted-by":"crossref","first-page":"5136","DOI":"10.1021\/ja058320b","article-title":"Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding","volume":"128","author":"Groll","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2012.01.003_bib58","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1006\/jmbi.2001.4869","article-title":"Crystal structure of the 20\u00a0S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor","volume":"311","author":"Groll","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib59","doi-asserted-by":"crossref","first-page":"4576","DOI":"10.1073\/pnas.0600647103","article-title":"Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation","volume":"103","author":"Groll","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2012.01.003_bib60","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/nature06782","article-title":"A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism","volume":"452","author":"Groll","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2012.01.003_bib61","doi-asserted-by":"crossref","first-page":"6107","DOI":"10.1200\/JCO.2005.01.136","article-title":"Proteasome inhibition with bortezomib (PS-341): a phase I study with pharmacodynamic end points using a day 1 and day 4 schedule in a 14-day cycle","volume":"23","author":"Hamilton","year":"2005","journal-title":"J. Clin. Oncol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib62","doi-asserted-by":"crossref","first-page":"25200","DOI":"10.1074\/jbc.272.40.25200","article-title":"The active sites of the eukaryotic 20\u00a0S proteasome and their involvement in subunit precursor processing","volume":"272","author":"Heinemeyer","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib63","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","article-title":"The ubiquitin system","volume":"67","author":"Hershko","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib64","doi-asserted-by":"crossref","first-page":"16639","DOI":"10.1074\/jbc.M200360200","article-title":"NF-kappa B as a therapeutic target in multiple myeloma","volume":"277","author":"Hideshima","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib65","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/j.chembiol.2008.03.020","article-title":"Proteasome inhibition by fellutamide B induces nerve growth factor synthesis","volume":"15","author":"Hines","year":"2008","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib66","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.chembiol.2007.03.008","article-title":"LMP2-specific inhibitors: chemical genetic tools for proteasome biology","volume":"14","author":"Ho","year":"2007","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib67","article-title":"Novel proteasome inhibitors have a beneficial effect in murine lupus via the dual inhibition of type I Interferon and autoantibody secreting cells","author":"Ichikawa","year":"2011","journal-title":"Arthritis Rheum."},{"key":"10.1016\/j.chembiol.2012.01.003_bib68","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.bmcl.2006.10.047","article-title":"Novel beta-lactam derivatives: potent and selective inhibitors of the chymotrypsin-like activity of the human 20S proteasome","volume":"17","author":"Imbach","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.chembiol.2012.01.003_bib69","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1021\/cb2002544","article-title":"Bacterial self-resistance to the natural proteasome inhibitor salinosporamide a","volume":"6","author":"Kale","year":"2011","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib70","doi-asserted-by":"crossref","first-page":"1940","DOI":"10.4161\/cc.8.12.8798","article-title":"Discovery of a novel proteasome inhibitor selective for cancer cells over non-transformed cells","volume":"8","author":"Kazi","year":"2009","journal-title":"Cell Cycle"},{"key":"10.1016\/j.chembiol.2012.01.003_bib71","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1126\/science.274.5293.1652","article-title":"How proteolysis drives the cell cycle","volume":"274","author":"King","year":"1996","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2012.01.003_bib72","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/S1074-5521(01)00056-4","article-title":"Proteasome inhibitors: from research tools to drug candidates","volume":"8","author":"Kisselev","year":"2001","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib73","doi-asserted-by":"crossref","first-page":"8582","DOI":"10.1074\/jbc.M509043200","article-title":"Importance of different active sites in protein breakdown by 26S proteasomes and the efficacy of proteasome inhibitors varies with the protein substrate","volume":"281","author":"Kisselev","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib74","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.coi.2003.11.004","article-title":"Proteasome and peptidase function in MHC-class-I-mediated antigen presentation","volume":"16","author":"Kloetzel","year":"2004","journal-title":"Curr. Opin. Immunol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib75","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1016\/S1097-2765(01)00274-X","article-title":"The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release","volume":"7","author":"K\u00f6hler","year":"2001","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2012.01.003_bib76","doi-asserted-by":"crossref","first-page":"1927","DOI":"10.1021\/np100600z","article-title":"Scytonemides A and B, cyclic peptides with 20S proteasome inhibitory activity from the cultured cyanobacterium Scytonema hofmanii","volume":"73","author":"Krunic","year":"2010","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.chembiol.2012.01.003_bib77","doi-asserted-by":"crossref","first-page":"4667","DOI":"10.1182\/blood-2008-07-171637","article-title":"Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors","volume":"113","author":"Kuhn","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2012.01.003_bib78","doi-asserted-by":"crossref","first-page":"1970","DOI":"10.1158\/0008-5472.CAN-09-2766","article-title":"Evaluation of the proteasome inhibitor MLN9708 in preclinical models of human cancer","volume":"70","author":"Kupperman","year":"2010","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib79","doi-asserted-by":"crossref","first-page":"4579","DOI":"10.1016\/j.bmc.2008.02.042","article-title":"Proteasome inhibition by peptide-semicarbazones","volume":"16","author":"Leban","year":"2008","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib80","first-page":"4996","article-title":"Proteasome inhibitor PS-341 inhibits human myeloma cell growth in\u00a0vivo and prolongs survival in a murine model","volume":"62","author":"LeBlanc","year":"2002","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib81","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/nature09299","article-title":"Enhancement of proteasome activity by a small-molecule inhibitor of USP14","volume":"467","author":"Lee","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2012.01.003_bib82","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.R110.003871","article-title":"Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes","volume":"10","author":"Lee","year":"2011","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.chembiol.2012.01.003_bib83","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1093\/jnci\/djq198","article-title":"Effect of noncompetitive proteasome inhibition on bortezomib resistance","volume":"102","author":"Li","year":"2010","journal-title":"J. Natl. Cancer Inst."},{"key":"10.1016\/j.chembiol.2012.01.003_bib84","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/nrc2129","article-title":"Triterpenoids and rexinoids as multifunctional agents for the prevention and treatment of cancer","volume":"7","author":"Liby","year":"2007","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.chembiol.2012.01.003_bib85","doi-asserted-by":"crossref","first-page":"12936","DOI":"10.1021\/ja075469+","article-title":"Periodate-triggered cross-linking reveals Sug2\/Rpt4 as the molecular target of a peptoid inhibitor of the 19S proteasome regulatory particle","volume":"129","author":"Lim","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2012.01.003_bib86","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1038\/nature08357","article-title":"Inhibitors selective for mycobacterial versus human proteasomes","volume":"461","author":"Lin","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2012.01.003_bib87","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1038\/nbt851","article-title":"A transgenic mouse model of the ubiquitin\/proteasome system","volume":"21","author":"Lindsten","year":"2003","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib88","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S1074-5521(99)80036-2","article-title":"Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes","volume":"6","author":"Loidl","year":"1999","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib89","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0960-894X(98)00015-8","article-title":"Selective inhibition of the chymotrypsin-like activity of the 20S proteasome by 5-methoxy-1-indanone dipeptide benzamides","volume":"8","author":"Lum","year":"1998","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.chembiol.2012.01.003_bib90","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1016\/S0960-894X(98)00030-4","article-title":"Inhibitors of the chymotrypsin-like activity of proteasome based on di- and tri-peptidyl alpha-keto aldehydes (glyoxals)","volume":"8","author":"Lynas","year":"1998","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.chembiol.2012.01.003_bib91","doi-asserted-by":"crossref","first-page":"6711","DOI":"10.1021\/jm800548b","article-title":"Leaving groups prolong the duration of 20S proteasome inhibition and enhance the potency of salinosporamides","volume":"51","author":"Manam","year":"2008","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib92","doi-asserted-by":"crossref","first-page":"5038","DOI":"10.1021\/jm040905d","article-title":"Peptidyl vinyl ester derivatives: new class of selective inhibitors of proteasome trypsin-like activity","volume":"48","author":"Marastoni","year":"2005","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib93","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1158\/0008-5472.CAN-06-2258","article-title":"Extensive immunoglobulin production sensitizes myeloma cells for proteasome inhibition","volume":"67","author":"Meister","year":"2007","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib94","doi-asserted-by":"crossref","first-page":"10403","DOI":"10.1073\/pnas.96.18.10403","article-title":"Epoxomicin, a potent and selective proteasome inhibitor, exhibits in\u00a0vivo antiinflammatory activity","volume":"96","author":"Meng","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2012.01.003_bib95","first-page":"2798","article-title":"Eponemycin exerts its antitumor effect through the inhibition of proteasome function","volume":"59","author":"Meng","year":"1999","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib96","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1016\/j.chembiol.2011.02.015","article-title":"Specific cell-permeable inhibitor of proteasome trypsin-like sites selectively sensitizes myeloma cells to bortezomib and carfilzomib","volume":"18","author":"Mirabella","year":"2011","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib97","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1158\/1078-0432.CCR-11-0853","article-title":"Molecular pathways: targeting proteasomal protein degradation in cancer","volume":"18","author":"Molineaux","year":"2012","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib98","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.7164\/antibiotics.54.1004","article-title":"Tyropeptins A and B, new proteasome inhibitors produced by Kitasatospora sp. MK993-dF2. II. Structure determination and synthesis","volume":"54","author":"Momose","year":"2001","journal-title":"J. Antibiot."},{"key":"10.1016\/j.chembiol.2012.01.003_bib99","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/nm.1978","article-title":"A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis","volume":"15","author":"Muchamuel","year":"2009","journal-title":"Nat. Med."},{"key":"10.1016\/j.chembiol.2012.01.003_bib100","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1196\/annals.1402.077","article-title":"Proteasome inhibitors stimulate both bone formation and hair growth by similar mechanisms","volume":"1117","author":"Mundy","year":"2007","journal-title":"Ann. N Y Acad. Sci."},{"key":"10.1016\/j.chembiol.2012.01.003_bib101","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1126\/science.1141915","article-title":"Regulation of CD8+ T\u00a0cell development by thymus-specific proteasomes","volume":"316","author":"Murata","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2012.01.003_bib102","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/S1097-2765(01)00188-5","article-title":"Lack of proteasome active site allostery as revealed by subunit-specific inhibitors","volume":"7","author":"Myung","year":"2001","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2012.01.003_bib103","doi-asserted-by":"crossref","first-page":"13322","DOI":"10.1074\/jbc.M004209200","article-title":"Ester bond-containing tea polyphenols potently inhibit proteasome activity in\u00a0vitro and in\u00a0vivo","volume":"276","author":"Nam","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib104","doi-asserted-by":"crossref","first-page":"2967","DOI":"10.1073\/pnas.061028898","article-title":"Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors","volume":"98","author":"Nazif","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2012.01.003_bib105","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1038\/nm1763","article-title":"The proteasome inhibitor bortezomib depletes plasma cells and protects mice with lupus-like disease from nephritis","volume":"14","author":"Neubert","year":"2008","journal-title":"Nat. Med."},{"key":"10.1016\/j.chembiol.2012.01.003_bib106","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.ccr.2008.05.016","article-title":"Argyrin a reveals a critical role for the tumor suppressor protein p27(kip1) in mediating antitumor activities in response to proteasome inhibition","volume":"14","author":"Nickeleit","year":"2008","journal-title":"Cancer Cell"},{"key":"10.1016\/j.chembiol.2012.01.003_bib107","doi-asserted-by":"crossref","first-page":"4907","DOI":"10.1182\/blood-2005-08-3531","article-title":"Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells","volume":"107","author":"Obeng","year":"2006","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2012.01.003_bib108","doi-asserted-by":"crossref","first-page":"7085","DOI":"10.1158\/1078-0432.CCR-09-0822","article-title":"A phase 1 dose escalation study of the safety and pharmacokinetics of the novel proteasome inhibitor carfilzomib (PR-171) in patients with hematologic malignancies","volume":"15","author":"O'Connor","year":"2009","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib109","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.7164\/antibiotics.41.1338","article-title":"Glidobactins A, B and C, new antitumor antibiotics. II. Structure elucidation","volume":"41","author":"Oka","year":"1988","journal-title":"J. Antibiot."},{"key":"10.1016\/j.chembiol.2012.01.003_bib110","doi-asserted-by":"crossref","first-page":"4420","DOI":"10.1200\/JCO.2002.01.133","article-title":"Phase I trial of the proteasome inhibitor PS-341 in patients with refractory hematologic malignancies","volume":"20","author":"Orlowski","year":"2002","journal-title":"J. Clin. Oncol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib111","doi-asserted-by":"crossref","first-page":"6853","DOI":"10.1038\/sj.onc.1203239","article-title":"Activators and target genes of Rel\/NF-kappaB transcription factors","volume":"18","author":"Pahl","year":"1999","journal-title":"Oncogene"},{"key":"10.1016\/j.chembiol.2012.01.003_bib112","doi-asserted-by":"crossref","first-page":"3193","DOI":"10.1021\/jm00017a002","article-title":"Vinyl sulfones as mechanism-based cysteine protease inhibitors","volume":"38","author":"Palmer","year":"1995","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib113","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1016\/S0092-8674(94)90482-0","article-title":"The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B","volume":"78","author":"Palombella","year":"1994","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2012.01.003_bib114","doi-asserted-by":"crossref","first-page":"15671","DOI":"10.1073\/pnas.95.26.15671","article-title":"Role of the proteasome and NF-kappaB in streptococcal cell wall-induced polyarthritis","volume":"95","author":"Palombella","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2012.01.003_bib115","doi-asserted-by":"crossref","first-page":"43","DOI":"10.4161\/cbt.11.1.13854","article-title":"Proteasome inhibitory activity of thiazole antibiotics","volume":"11","author":"Pandit","year":"2011","journal-title":"Cancer Biol. Ther."},{"key":"10.1016\/j.chembiol.2012.01.003_bib116","doi-asserted-by":"crossref","first-page":"3439","DOI":"10.1182\/blood-2009-05-223677","article-title":"Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome","volume":"114","author":"Parlati","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2012.01.003_bib117","doi-asserted-by":"crossref","first-page":"2765","DOI":"10.1182\/blood-2007-07-100651","article-title":"CEP-18770: A novel, orally active proteasome inhibitor with a tumor-selective pharmacologic profile competitive with bortezomib","volume":"111","author":"Piva","year":"2008","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2012.01.003_bib118","doi-asserted-by":"crossref","first-page":"254","DOI":"10.2174\/156800911794519716","article-title":"Marizomib, a proteasome inhibitor for all seasons: preclinical profile and a framework for clinical trials","volume":"11","author":"Potts","year":"2011","journal-title":"Curr. Cancer Drug Targets"},{"key":"10.1016\/j.chembiol.2012.01.003_bib119","doi-asserted-by":"crossref","first-page":"6282","DOI":"10.1158\/0008-5472.CAN-05-0676","article-title":"Proteasome inhibitors trigger NOXA-mediated apoptosis in melanoma and myeloma cells","volume":"65","author":"Qin","year":"2005","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib120","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1056\/NEJMoa030288","article-title":"A phase 2 study of bortezomib in relapsed, refractory myeloma","volume":"348","author":"Richardson","year":"2003","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.chembiol.2012.01.003_bib121","doi-asserted-by":"crossref","first-page":"2487","DOI":"10.1056\/NEJMoa043445","article-title":"Bortezomib or high-dose dexamethasone for relapsed multiple myeloma","volume":"352","author":"Richardson","year":"2005","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.chembiol.2012.01.003_bib122","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1146\/annurev.immunol.17.1.739","article-title":"Degradation of cell proteins and the generation of MHC class I-presented peptides","volume":"17","author":"Rock","year":"1999","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib123","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/S0092-8674(94)90462-6","article-title":"Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules","volume":"78","author":"Rock","year":"1994","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2012.01.003_bib124","doi-asserted-by":"crossref","first-page":"6609","DOI":"10.1158\/1078-0432.CCR-09-0548","article-title":"SC68896, a novel small molecule proteasome inhibitor, exerts antiglioma activity in\u00a0vitro and in\u00a0vivo","volume":"15","author":"Roth","year":"2009","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib125","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/S1054-3589(08)57003-7","article-title":"The development and pharmacology of proteasome inhibitors for the management and treatment of cancer","volume":"57","author":"Ruggeri","year":"2009","journal-title":"Adv. Pharmacol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib126","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1136\/gut.2009.203554","article-title":"Targeting the proteasome: partial inhibition of the proteasome by bortezomib or deletion of the immunosubunit LMP7 attenuates experimental colitis","volume":"59","author":"Schmidt","year":"2010","journal-title":"Gut"},{"key":"10.1016\/j.chembiol.2012.01.003_bib127","doi-asserted-by":"crossref","first-page":"40125","DOI":"10.1074\/jbc.M110.160606","article-title":"Nature of pharmacophore influences active site specificity of proteasome inhibitors","volume":"285","author":"Screen","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib128","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1046\/j.1365-2125.2002.01638.x","article-title":"Early clinical experience with the novel proteasome inhibitor PS-519","volume":"54","author":"Shah","year":"2002","journal-title":"Br. J. Clin. Pharmacol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib129","doi-asserted-by":"crossref","first-page":"9967","DOI":"10.1021\/ja991175f","article-title":"A novel and efficient synthesis of a highly active analogue of clasto-lactacystin beta-lactone","volume":"121","author":"Soucy","year":"1999","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2012.01.003_bib130","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1007\/s00436-004-1253-y","article-title":"Trypanocidal activities of trileucine methyl vinyl sulfone proteasome inhibitors","volume":"95","author":"Steverding","year":"2005","journal-title":"Parasitol. Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib131","first-page":"2638","article-title":"The proteasome inhibitor PS-341 in cancer therapy","volume":"5","author":"Teicher","year":"1999","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2012.01.003_bib132","doi-asserted-by":"crossref","first-page":"4027","DOI":"10.1182\/blood-2008-09-179796","article-title":"Identification of a potent natural triterpenoid inhibitor of proteosome chymotrypsin-like activity and NF-kappaB with antimyeloma activity in\u00a0vitro and in\u00a0vivo","volume":"113","author":"Tiedemann","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2012.01.003_bib133","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1097\/TP.0b013e3181a4b91b","article-title":"Abrogation of anti-HLA antibodies via proteasome inhibition","volume":"87","author":"Trivedi","year":"2009","journal-title":"Transplantation"},{"key":"10.1016\/j.chembiol.2012.01.003_bib134","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1006\/bbrc.1993.2378","article-title":"Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: a novel catalytic activity in proteasome","volume":"196","author":"Tsubuki","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.chembiol.2012.01.003_bib135","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1093\/oxfordjournals.jbchem.a021280","article-title":"Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine","volume":"119","author":"Tsubuki","year":"1996","journal-title":"J. Biochem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib136","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1039\/C1OB06554H","article-title":"Discovery of a potent and highly \u03b21 specific proteasome inhibitor from a focused library of urea-containing peptide vinyl sulfones and peptide epoxyketones","volume":"10","author":"van der Linden","year":"2012","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib137","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1016\/j.chembiol.2006.09.013","article-title":"A fluorescent broad-spectrum proteasome inhibitor for labeling proteasomes in\u00a0vitro and in\u00a0vivo","volume":"13","author":"Verdoes","year":"2006","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib138","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1039\/c001036g","article-title":"A panel of subunit-selective activity-based proteasome probes","volume":"8","author":"Verdoes","year":"2010","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.chembiol.2012.01.003_bib139","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1126\/science.1075898","article-title":"Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome","volume":"298","author":"Verma","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2012.01.003_bib140","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1126\/science.1100946","article-title":"Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain","volume":"306","author":"Verma","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2012.01.003_bib141","doi-asserted-by":"crossref","first-page":"2200","DOI":"10.1073\/pnas.0807611106","article-title":"ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells","volume":"106","author":"Wang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2012.01.003_bib142","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.neuint.2006.03.018","article-title":"Neuroprotection with the proteasome inhibitor MLN519 in focal ischemic brain injury: relation to nuclear factor kappaB (NF-kappaB), inflammatory gene expression, and leukocyte infiltration","volume":"49","author":"Williams","year":"2006","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.chembiol.2012.01.003_bib143","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1038\/nrc2641","article-title":"Cancer prevention by tea: animal studies, molecular mechanisms and human relevance","volume":"9","author":"Yang","year":"2009","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.chembiol.2012.01.003_bib144","doi-asserted-by":"crossref","first-page":"46","DOI":"10.2174\/157016310791162785","article-title":"Targeting tumor proteasome with traditional Chinese medicine","volume":"7","author":"Yang","year":"2010","journal-title":"Curr. Drug Discov. Technol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib145","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1111\/j.1365-2141.2005.05733.x","article-title":"Response to bortezomib is associated to osteoblastic activation in patients with multiple myeloma","volume":"131","author":"Zangari","year":"2005","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.chembiol.2012.01.003_bib146","doi-asserted-by":"crossref","first-page":"3028","DOI":"10.1021\/jm801329v","article-title":"Design and synthesis of an orally bioavailable and selective peptide epoxyketone proteasome inhibitor (PR-047)","volume":"52","author":"Zhou","year":"2009","journal-title":"J. Med. Chem."}],"container-title":["Chemistry & Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1074552112000129?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1074552112000129?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T07:18:38Z","timestamp":1761031118000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1074552112000129"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,1]]},"references-count":147,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2012,1]]}},"alternative-id":["S1074552112000129"],"URL":"https:\/\/doi.org\/10.1016\/j.chembiol.2012.01.003","relation":{},"ISSN":["1074-5521"],"issn-type":[{"value":"1074-5521","type":"print"}],"subject":[],"published":{"date-parts":[[2012,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Proteasome Inhibitors: An Expanding Army Attacking a Unique Target","name":"articletitle","label":"Article Title"},{"value":"Chemistry & Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.chembiol.2012.01.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2012 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}