{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T12:57:45Z","timestamp":1787662665744,"version":"build-2736575974"},"reference-count":59,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2002,8,1]],"date-time":"2002-08-01T00:00:00Z","timestamp":1028160000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Current Opinion in Cell Biology"],"published-print":{"date-parts":[[2002,8]]},"DOI":"10.1016\/s0955-0674(02)00358-7","type":"journal-article","created":{"date-parts":[[2002,10,7]],"date-time":"2002-10-07T15:24:03Z","timestamp":1034004243000},"page":"476-482","source":"Crossref","is-referenced-by-count":410,"title":["ER-associated degradation in protein quality control and cellular regulation"],"prefix":"10.1016","volume":"14","author":[{"given":"Randolph Y","family":"Hampton","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/S0955-0674(02)00358-7_BIB1","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1023\/A:1006913215484","article-title":"Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome","volume":"26","author":"Plemper","year":"1999","journal-title":"Mol Biol Rep"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB2","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1096\/fasebj.11.14.9409541","article-title":"Endoplasmic reticulum degradation: reverse protein flow of no return","volume":"11","author":"Sommer","year":"1997","journal-title":"FASEB J"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB3","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1146\/annurev.cellbio.14.1.19","article-title":"Ubiquitin and the control of protein fate in the secretory and endocytic pathways","volume":"14","author":"Bonifacino","year":"1998","journal-title":"Annu Rev Cell Dev Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB4","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1053\/jhep.2002.30316","article-title":"Ubiquitin-mediated degradation of cellular proteins in health and disease","volume":"35","author":"Ciechanover","year":"2002","journal-title":"Hepatology"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB5","doi-asserted-by":"crossref","first-page":"19107","DOI":"10.1074\/jbc.270.32.19107","article-title":"Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase","volume":"270","author":"Kumagai","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB6","doi-asserted-by":"crossref","first-page":"4236","DOI":"10.1016\/S0021-9258(19)50652-4","article-title":"The role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase","volume":"267","author":"Chun","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB7","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1083\/jcb.125.2.299","article-title":"Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast","volume":"125","author":"Hampton","year":"1994","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB8","doi-asserted-by":"crossref","first-page":"12944","DOI":"10.1073\/pnas.94.24.12944","article-title":"Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase","volume":"94","author":"Hampton","year":"1997","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB9","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.1091\/mbc.7.12.2029","article-title":"Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy 3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein","volume":"7","author":"Hampton","year":"1996","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB10","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/35050524","article-title":"Hrd1p\/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation","volume":"3","author":"Bays","year":"2001","journal-title":"Nat Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB11","doi-asserted-by":"crossref","first-page":"4114","DOI":"10.1091\/mbc.12.12.4114","article-title":"HRD4\/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins","volume":"12","author":"Bays","year":"2001","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB12","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1083\/jcb.151.1.69","article-title":"Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p","volume":"151","author":"Gardner","year":"2000","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB13","doi-asserted-by":"crossref","first-page":"4276","DOI":"10.1128\/MCB.21.13.4276-4291.2001","article-title":"In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation","volume":"21","author":"Gardner","year":"2001","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB14","doi-asserted-by":"crossref","first-page":"25630","DOI":"10.1074\/jbc.271.41.25630","article-title":"Degradation of 3-hydroxy 3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis","volume":"271","author":"McGee","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB15","doi-asserted-by":"crossref","first-page":"35840","DOI":"10.1074\/jbc.M004793200","article-title":"The ubiquitin proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase","volume":"275","author":"Ravid","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB16","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S0925-4773(98)00146-4","article-title":"Cloning and characterization of Sel-1l, a murine homolog of the C. elegans sel-1 gene","volume":"78","author":"Donoviel","year":"1998","journal-title":"Mech Dev"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB17","doi-asserted-by":"crossref","first-page":"14422","DOI":"10.1073\/pnas.251401598","article-title":"The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum","volume":"98","author":"Fang","year":"2001","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB18","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/s004390051032","article-title":"SEL1L, the human homolog of C. elegans sel-1: refined physical mapping, gene structure and identification of polymorphic markers","volume":"106","author":"Biunno","year":"2000","journal-title":"Hum Genet"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB19","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.1126\/science.273.5282.1725","article-title":"ER degradation of a misfolded luminal protein by the cytosolic ubiquitin\u2013proteasome pathway","volume":"273","author":"Hiller","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB20","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/S0014-5793(98)01724-4","article-title":"Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species","volume":"443","author":"Plemper","year":"1999","journal-title":"FEBS Lett"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB21","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1091\/mbc.9.1.209","article-title":"Der3p\/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins","volume":"9","author":"Bordallo","year":"1998","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB22","doi-asserted-by":"crossref","first-page":"4123","DOI":"10.1242\/jcs.112.22.4123","article-title":"Genetic interactions of Hrd3p and Der3p\/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation","volume":"112","author":"Plemper","year":"1999","journal-title":"J Cell Sci"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB23","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1038\/35017001","article-title":"A regulatory link between ER-associated protein degradation and the unfolded-protein response","volume":"2","author":"Friedlander","year":"2000","journal-title":"Nat Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB24","doi-asserted-by":"crossref","first-page":"32848","DOI":"10.1074\/jbc.273.49.32848","article-title":"Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome","volume":"273","author":"Plemper","year":"1998","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB25","doi-asserted-by":"crossref","first-page":"1697","DOI":"10.1091\/mbc.11.5.1697","article-title":"HRD gene dependence of endoplasmic reticulum-associated degradation","volume":"11","author":"Wilhovsky","year":"2000","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB26","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1083\/jcb.200106123","article-title":"Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding","volume":"155","author":"Vashist","year":"2001","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB27","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0092-8674(00)80835-1","article-title":"Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation","volume":"101","author":"Travers","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB28","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1093\/emboj\/21.4.615","article-title":"Role of the ubiquitin-selective CDC48(UFD1\/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates","volume":"21","author":"Braun","year":"2002","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB29","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1128\/MCB.22.2.626-634.2002","article-title":"AAA-ATPase p97\/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation","volume":"22","author":"Rabinovich","year":"2002","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB30","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1038\/414652a","article-title":"The AAA ATPase Cdc48\/p97 and its partners transport proteins from the ER into the cytosol","volume":"414","author":"Ye","year":"2001","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB31","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/S0092-8674(01)00595-5","article-title":"Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1\/NPL4), a ubiquitin-selective chaperone","volume":"107","author":"Rape","year":"2001","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB32","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1038\/ncb746","article-title":"Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48","volume":"4","author":"Jarosch","year":"2002","journal-title":"Nat Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB33","doi-asserted-by":"crossref","first-page":"3226","DOI":"10.1091\/mbc.12.10.3226","article-title":"The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation","volume":"12","author":"Hitchcock","year":"2001","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB34","doi-asserted-by":"crossref","first-page":"R366","DOI":"10.1016\/S0960-9822(02)00862-X","article-title":"Cdc48p\/Npl4p\/Ufd1p: stuck in the middle with Ub","volume":"12","author":"Bays","year":"2002","journal-title":"Curr Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB35","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1038\/42276","article-title":"Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation","volume":"388","author":"Plemper","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB36","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1016\/S1097-2765(00)80222-1","article-title":"The engagement of Sec61p in the ER dislocation process","volume":"4","author":"Zhou","year":"1999","journal-title":"Mol Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB37","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1038\/384432a0","article-title":"Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction","volume":"384","author":"Wiertz","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB38","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1093\/emboj\/19.4.550","article-title":"Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system","volume":"19","author":"Hill","year":"2000","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB39","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1091\/mbc.12.5.1303","article-title":"Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast","volume":"12","author":"Zhang","year":"2001","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB40","doi-asserted-by":"crossref","first-page":"2660","DOI":"10.1101\/gad.933301","article-title":"A conserved ubiquitin ligase of the nuclear envelope\/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation","volume":"15","author":"Swanson","year":"2001","journal-title":"Genes Dev"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB41","doi-asserted-by":"crossref","first-page":"42938","DOI":"10.1074\/jbc.M101968200","article-title":"CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation","volume":"276","author":"Jiang","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB42","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\/S0955-0674(02)00358-7_BIB43","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1093\/embo-reports\/kve246","article-title":"CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein","volume":"2","author":"Murata","year":"2001","journal-title":"EMBO Rep"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB44","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1038\/35050509","article-title":"The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation","volume":"3","author":"Meacham","year":"2001","journal-title":"Nat Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB45","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1042\/0264-6021:3510527","article-title":"Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction","volume":"351","author":"Ponting","year":"2000","journal-title":"Biochem J"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB46","doi-asserted-by":"crossref","first-page":"23296","DOI":"10.1074\/jbc.M102962200","article-title":"Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi","volume":"276","author":"Caldwell","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB47","doi-asserted-by":"crossref","unstructured":"Taxis C, Vogel F, Wolf D. ER\u2013Golgi-traffic is a prerequisite for efficient ER degradation, Mol Biol Cell 2002, in press. See annotation Vashist et al. (2001) [26\u2022].","DOI":"10.1091\/mbc.01-08-0399"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB48","doi-asserted-by":"crossref","first-page":"31671","DOI":"10.1074\/jbc.274.44.31671","article-title":"A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes","volume":"274","author":"Gardner","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB49","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1083\/jcb.148.5.915","article-title":"Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p\/Spf1p","volume":"148","author":"Cronin","year":"2000","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB50","doi-asserted-by":"crossref","unstructured":"Cronin S, Rao R, Hampton RY. Cod1p\/Spf1 is an ER P-type ATPase required for ER function and calcium homeostasis. J Cell Biol 2002, in press.","DOI":"10.1083\/jcb.200203052"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB51","doi-asserted-by":"crossref","first-page":"8681","DOI":"10.1074\/jbc.M007888200","article-title":"An oxysterol-derived positive signal for 3-hydroxy-3-methylglutaryl-CoA reductase degradation in yeast","volume":"276","author":"Gardner","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB52","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/abbi.1997.0200","article-title":"Farnesol as a regulator of HMG-CoA reductase degradation: characterization and role of farnesyl pyrophosphatase","volume":"345","author":"Meigs","year":"1997","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB53","doi-asserted-by":"crossref","first-page":"17390","DOI":"10.1016\/S0021-9258(17)32450-X","article-title":"Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase","volume":"269","author":"Correll","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB54","doi-asserted-by":"crossref","first-page":"5994","DOI":"10.1093\/emboj\/18.21.5994","article-title":"A \u2018distributed degron\u2019 allows regulated entry into the ER degradation pathway","volume":"18","author":"Gardner","year":"1999","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB55","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1074\/jbc.271.2.635","article-title":"Glycerol reverses the misfolding phenotype of the most common Cystic fibrosis mutation","volume":"271","author":"Sato","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB56","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1379\/1466-1268(1996)001<0117:CCCTMP>2.3.CO;2","article-title":"Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein","volume":"1","author":"Brown","year":"1996","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB57","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1379\/1466-1268(1996)001<0109:IOMACC>2.3.CO;2","article-title":"Influence of molecular and chemical chaperones on protein folding","volume":"1","author":"Welch","year":"1996","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB58","doi-asserted-by":"crossref","first-page":"17171","DOI":"10.1074\/jbc.274.24.17171","article-title":"Oligomerization state influences the degradation rate of 3-hydroxy 3-methylglutaryl-CoA reductase","volume":"274","author":"Cheng","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(02)00358-7_BIB59","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/S0092-8674(00)00037-4","article-title":"Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes","volume":"102","author":"Nohturfft","year":"2000","journal-title":"Cell"}],"container-title":["Current Opinion in Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067402003587?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067402003587?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,28]],"date-time":"2021-05-28T11:12:45Z","timestamp":1622200365000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0955067402003587"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,8]]},"references-count":59,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2002,8]]}},"alternative-id":["S0955067402003587"],"URL":"https:\/\/doi.org\/10.1016\/s0955-0674(02)00358-7","relation":{},"ISSN":["0955-0674"],"issn-type":[{"value":"0955-0674","type":"print"}],"subject":[],"published":{"date-parts":[[2002,8]]}}}