{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T17:26:31Z","timestamp":1791912391832,"version":"4.3.4"},"reference-count":99,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,2,1]],"date-time":"2017-02-01T00:00:00Z","timestamp":1485907200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science (JSPS)","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science (JSPS)","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Seminars in Cell & Developmental Biology"],"published-print":{"date-parts":[[2017,2]]},"DOI":"10.1016\/j.semcdb.2016.11.005","type":"journal-article","created":{"date-parts":[[2016,11,9]],"date-time":"2016-11-09T22:02:15Z","timestamp":1478728935000},"page":"142-151","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":250,"special_numbering":"C","title":["Biology of Hsp47 (Serpin H1), a collagen-specific molecular chaperone"],"prefix":"10.1016","volume":"62","author":[{"given":"Shinya","family":"Ito","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuhiro","family":"Nagata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.semcdb.2016.11.005_bib0005","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1146\/annurev-biochem-060208-092442","article-title":"Molecular chaperone functions in protein folding and proteostasis","volume":"82","author":"Kim","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0010","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a004507","article-title":"Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis","volume":"3","author":"Lindquist","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0015","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.molcel.2010.10.001","article-title":"Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms","volume":"40","author":"Buchberger","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0020","doi-asserted-by":"crossref","first-page":"a007526","DOI":"10.1101\/cshperspect.a007526","article-title":"Protein folding and quality control in the ER","volume":"3","author":"Araki","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0025","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.1016\/j.jmb.2015.02.011","article-title":"BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions","volume":"427","author":"Behnke","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0030","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1093\/jb\/mvp166","article-title":"Signalling pathways in the unfolded protein response: development from yeast to mammals","volume":"146","author":"Mori","year":"2009","journal-title":"J. Biochem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0035","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1126\/science.1209038","article-title":"The unfolded protein response: from stress pathway to homeostatic regulation","volume":"334","author":"Walter","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0040","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/B978-0-12-386471-0.00009-2","article-title":"Hsp47 as a collagen-specific molecular chaperone","volume":"499","author":"Ishida","year":"2011","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0045","doi-asserted-by":"crossref","first-page":"8937","DOI":"10.1073\/pnas.1201380109","article-title":"Global analysis of chaperone effects using a reconstituted cell-free translation system","volume":"109","author":"Niwa","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0050","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.semcdb.2003.09.020","article-title":"HSP47 as a collagen-specific molecular chaperone: function and expression in normal mouse development","volume":"14","author":"Nagata","year":"2003","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0055","doi-asserted-by":"crossref","first-page":"e242","DOI":"10.1371\/journal.pbio.0050242","article-title":"Variants in a novel epidermal collagen gene (COL29A1) are associated with atopic dermatitis","volume":"5","author":"S\u00f6derh\u00e4ll","year":"2007","journal-title":"PLoS Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0060","doi-asserted-by":"crossref","first-page":"aad4395","DOI":"10.1126\/science.aad4395","article-title":"Hair follicle aging is driven by transepidermal elimination of stem cells via COL17A1 proteolysis","volume":"351","author":"Matsumura","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0065","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1038\/nature14021","article-title":"Dauer-independent insulin\/IGF-1-signalling implicates collagen remodelling in longevity","volume":"519","author":"Ewald","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0070","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1038\/nsmb.2389","article-title":"Structural basis of fibrillar collagen trimerization and related genetic disorders","volume":"19","author":"Bourhis","year":"2012","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0075","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1146\/annurev.bb.20.060191.001033","article-title":"The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper","volume":"20","author":"Engel","year":"1991","journal-title":"Annu. Rev. Biophys. Biophys. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0080","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1016\/S0092-8674(00)81723-7","article-title":"Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation","volume":"95","author":"Bonfanti","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0085","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.ceb.2013.04.005","article-title":"COPII \u2013 a flexible vesicle formation system","volume":"25","author":"Miller","year":"2013","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0090","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1083\/jcb.201007162","article-title":"Global defects in collagen secretion in a Mia3\/TANGO1 knockout mouse","volume":"193","author":"Wilson","year":"2011","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0095","doi-asserted-by":"crossref","first-page":"3709","DOI":"10.1007\/s00018-015-1952-9","article-title":"Mechanisms for exporting large-sized cargoes from the endoplasmic reticulum","volume":"72","author":"Saito","year":"2015","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0100","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1126\/science.1224947","article-title":"Sedlin controls the ER export of procollagen by regulating the Sar1 cycle","volume":"337","author":"Venditti","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0105","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.matbio.2015.04.001","article-title":"The procollagen N-proteinases ADAMTS2 3 and 14 in pathophysiology","volume":"44\u201346","author":"Bekhouche","year":"2015","journal-title":"Matrix Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0110","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.matbio.2015.02.006","article-title":"BMP-1\/tolloid-like proteinases synchronize matrix assembly with growth factor activation to promote morphogenesis and tissue remodeling","volume":"44\u201346","author":"Vadon-Le Goff","year":"2015","journal-title":"Matrix Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0115","doi-asserted-by":"crossref","first-page":"e1006002","DOI":"10.1371\/journal.pgen.1006002","article-title":"Sc65-null mice provide evidence for a novel endoplasmic reticulum complex regulating collagen lysyl hydroxylation","volume":"12","author":"Heard","year":"2016","journal-title":"PLoS Genet."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0120","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1128\/MCB.02085-07","article-title":"Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases","volume":"29","author":"Schegg","year":"2009","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0125","doi-asserted-by":"crossref","first-page":"2479","DOI":"10.1016\/j.bbamcr.2013.04.008","article-title":"A molecular ensemble in the rER for procollagen maturation","volume":"1833","author":"Ishikawa","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0130","doi-asserted-by":"crossref","first-page":"7684","DOI":"10.1073\/pnas.79.24.7684","article-title":"Collagen structural microheterogeneity and a possible role for glycosylated hydroxylysine in type I collagen","volume":"79","author":"Yamauchi","year":"1982","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0135","doi-asserted-by":"crossref","first-page":"9637","DOI":"10.1074\/jbc.273.16.9637","article-title":"Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen","volume":"273","author":"Wilson","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0140","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1016\/S0960-9822(01)00317-7","article-title":"Quality control in the endoplasmic reticulum: PDI mediates the ER retention of unassembled procollagen C-propeptides","volume":"11","author":"Bottomley","year":"2001","journal-title":"Curr. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0145","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1083\/jcb.103.1.223","article-title":"A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein","volume":"103","author":"Nagata","year":"1986","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0150","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1016\/S0021-9258(18)61508-X","article-title":"Isolation of collagen binding proteins from embryonic chicken corneal epithelial cells","volume":"262","author":"Sugrue","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0155","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1139\/o87-100","article-title":"Differentiation defective mutants of skeletal myoblasts altered in a gelatin-binding glycoprotein","volume":"65","author":"Cates","year":"1987","journal-title":"Biochem. Cell Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0160","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1111\/j.1432-1033.1987.tb10736.x","article-title":"Distinct patterns of glycosylation of colligin, a collagen-binding glycoprotein, and SPARC (osteonectin), a secreted Ca2+-binding glycoprotein. Evidence for the localisation of colligin in the endoplasmic reticulum","volume":"163","author":"Hughes","year":"1987","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0165","doi-asserted-by":"crossref","first-page":"4036","DOI":"10.1128\/MCB.11.8.4036","article-title":"HSP47: a tissue-specific transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts","volume":"11","author":"Hirayoshi","year":"1991","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0170","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1083\/jcb.105.1.517","article-title":"pH-dependent function, purification, and intracellular location of a major collagen-binding glycoprotein","volume":"105","author":"Saga","year":"1987","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0175","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1083\/jcb.133.2.469","article-title":"Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen","volume":"133","author":"Satoh","year":"1996","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0180","doi-asserted-by":"crossref","first-page":"33293","DOI":"10.1074\/jbc.R100016200","article-title":"The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature","volume":"276","author":"Silverman","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0185","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/1479-7364-7-22","article-title":"Update of the human and mouse SERPIN gene superfamily","volume":"7","author":"Heit","year":"2013","journal-title":"Hum. Genom."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0190","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1083\/jcb.117.4.903","article-title":"Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum","volume":"117","author":"Nakai","year":"1992","journal-title":"J. Cell Biol."},{"issue":"Pt. 3","key":"10.1016\/j.semcdb.2016.11.005_bib0195","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1042\/bj3490877","article-title":"Structure-function studies on hsp47: pH-dependent inhibition of collagen fibril formation in vitro","volume":"349","author":"Thomson","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0200","doi-asserted-by":"crossref","first-page":"e1029","DOI":"10.1371\/journal.pone.0001029","article-title":"Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm","volume":"2","author":"Makareeva","year":"2007","journal-title":"PLoS One"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0205","doi-asserted-by":"crossref","first-page":"25399","DOI":"10.1074\/jbc.M102471200","article-title":"HSP47 binds cooperatively to triple helical type I collagen but has little effect on the thermal stability or rate of refolding","volume":"276","author":"Macdonald","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0210","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1083\/jcb.150.6.1499","article-title":"Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis","volume":"150","author":"Nagai","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0215","doi-asserted-by":"crossref","first-page":"31224","DOI":"10.1016\/S0021-9258(18)47412-1","article-title":"Interactions between collagen-binding stress protein HSP47 and collagen. Analysis of kinetic parameters by surface plasmon resonance biosensor","volume":"269","author":"Natsume","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0220","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.bbamcr.2011.10.013","article-title":"GRP94: an HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum","volume":"1823","author":"Marzec","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0225","doi-asserted-by":"crossref","first-page":"34523","DOI":"10.1074\/jbc.274.49.34523","article-title":"Substrate recognition of collagen-specific molecular chaperone HSP47. Structural requirements and binding regulation","volume":"274","author":"Koide","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0230","doi-asserted-by":"crossref","first-page":"19343","DOI":"10.1074\/jbc.M501657200","article-title":"Prediction of collagen stability from amino acid sequence","volume":"280","author":"Persikov","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0235","doi-asserted-by":"crossref","first-page":"6178","DOI":"10.1074\/jbc.M106497200","article-title":"Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47","volume":"277","author":"Koide","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0240","doi-asserted-by":"crossref","first-page":"2204","DOI":"10.1093\/emboj\/19.10.2204","article-title":"Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen","volume":"19","author":"Tasab","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0245","doi-asserted-by":"crossref","first-page":"35007","DOI":"10.1074\/jbc.M202782200","article-title":"Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47","volume":"277","author":"Tasab","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0250","doi-asserted-by":"crossref","first-page":"11177","DOI":"10.1074\/jbc.M601369200","article-title":"Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins","volume":"281","author":"Koide","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0255","doi-asserted-by":"crossref","first-page":"6810","DOI":"10.1074\/jbc.M111.280248","article-title":"Direct in vitro and in vivo evidence for interaction between Hsp47 protein and collagen triple helix","volume":"287","author":"Ono","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0260","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/S0969-2126(03)00025-X","article-title":"Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon","volume":"11","author":"Stetefeld","year":"2003","journal-title":"Structure"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0265","doi-asserted-by":"crossref","first-page":"e45930","DOI":"10.1371\/journal.pone.0045930","article-title":"NMR and mutational identification of the collagen-binding site of the chaperone Hsp47","volume":"7","author":"Yagi-Utsumi","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0270","doi-asserted-by":"crossref","first-page":"13243","DOI":"10.1073\/pnas.1208072109","article-title":"Molecular basis for the action of the collagen-specific chaperone Hsp47\/SERPINH1 and its structure-specific client recognition","volume":"109","author":"Widmer","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0275","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1242\/dev.01037","article-title":"Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development","volume":"131","author":"P\u00f6schl","year":"2004","journal-title":"Development"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0280","doi-asserted-by":"crossref","first-page":"4467","DOI":"10.1091\/mbc.E04-01-0050","article-title":"Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cells","volume":"15","author":"Matsuoka","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0285","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1242\/jcs.089748","article-title":"The molecular chaperone Hsp47 is essential for cartilage and endochondral bone formation","volume":"125","author":"Masago","year":"2012","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0290","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1038\/nm879","article-title":"Dynamic imaging of collagen and its modulation in tumors in vivo using second-harmonic generation","volume":"9","author":"Brown","year":"2003","journal-title":"Nat. Med."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0295","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.joca.2004.12.007","article-title":"Nonlinear optical microscopy of articular cartilage","volume":"13","author":"Yeh","year":"2005","journal-title":"Osteoarthr. Cartil."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0300","doi-asserted-by":"crossref","first-page":"2346","DOI":"10.1091\/mbc.E05-11-1065","article-title":"Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis","volume":"17","author":"Ishida","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0305","doi-asserted-by":"crossref","first-page":"5913","DOI":"10.1242\/jcs.01514","article-title":"Accumulation of type IV collagen in dilated ER leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP","volume":"117","author":"Marutani","year":"2004","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0310","doi-asserted-by":"crossref","first-page":"2744","DOI":"10.1091\/mbc.E08-11-1092","article-title":"Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection","volume":"20","author":"Ishida","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0315","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1146\/annurev-cellbio-092910-154005","article-title":"The role of Atg proteins in autophagosome formation","volume":"27","author":"Mizushima","year":"2011","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0320","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1038\/nrm3696","article-title":"The autophagosome: origins unknown biogenesis complex","volume":"14","author":"Lamb","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0325","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/j.yexcr.2004.01.029","article-title":"Intracellular trafficking and degradation of unassociated proalpha2 chains of collagen type I","volume":"296","author":"Gotkin","year":"2004","journal-title":"Exp. Cell Res."},{"issue":"Pt. 2","key":"10.1016\/j.semcdb.2016.11.005_bib0330","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1042\/bj2930387","article-title":"A type I collagen reporter gene construct for protein engineering studies. Functional equivalence of transfected reporter COL1A1 and endogenous gene products during biosynthesis and in vitro extracellular matrix accumulation","volume":"293","author":"Lamand\u00e9","year":"1993","journal-title":"Biochem. J."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0335","doi-asserted-by":"crossref","first-page":"27392","DOI":"10.1074\/jbc.274.39.27392","article-title":"Proteasomal degradation of unassembled mutant type I collagen pro-alpha1(I) chains","volume":"274","author":"Fitzgerald","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0340","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/nature16063","article-title":"FGF signalling regulates bone growth through autophagy","volume":"528","author":"Cinque","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0345","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.4161\/auto.5.8.10168","article-title":"Autophagy eliminates a specific species of misfolded procollagen and plays a protective role in cell survival against ER stress","volume":"5","author":"Ishida","year":"2009","journal-title":"Autophagy"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0350","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.molcel.2014.03.037","article-title":"ERQC autophagy: yet another way to die","volume":"54","author":"Buchberger","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0355","doi-asserted-by":"crossref","first-page":"E6166","DOI":"10.1073\/pnas.1519384112","article-title":"Basal autophagy maintains pancreatic acinar cell homeostasis and protein synthesis and prevents ER stress","volume":"112","author":"Antonucci","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0360","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1038\/nature14498","article-title":"Regulation of endoplasmic reticulum turnover by selective autophagy","volume":"522","author":"Khaminets","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0365","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1111\/j.1432-1033.1992.tb16930.x","article-title":"Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells","volume":"206","author":"Takechi","year":"1992","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0370","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0378-1119(93)90366-B","article-title":"Structure of the gene encoding the mouse 47-kDa heat-shock protein (HSP47)","volume":"126","author":"Hosokawa","year":"1993","journal-title":"Gene"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0375","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1101\/sqb.2012.76.010637","article-title":"The heat shock response: systems biology of proteotoxic stress in aging and disease","volume":"76","author":"Morimoto","year":"2011","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0380","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1146\/annurev-biochem-060809-095203","article-title":"Regulation of HSF1 function in the heat stress response: implications in aging and disease","volume":"80","author":"Anckar","year":"2011","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0385","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/S0968-0004(06)80023-X","article-title":"Hsp47: a collagen-specific molecular chaperone","volume":"21","author":"Nagata","year":"1996","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0390","doi-asserted-by":"crossref","first-page":"7531","DOI":"10.1016\/S0021-9258(17)38424-7","article-title":"Phosphorylation and transformation sensitivity of a major collagen-binding protein of fibroblasts","volume":"261","author":"Nagata","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0395","doi-asserted-by":"crossref","first-page":"9500","DOI":"10.1073\/pnas.95.16.9500","article-title":"Zf9, a kruppel-like transcription factor up-regulated in vivo during early hepatic fibrosis","volume":"95","author":"Ratziu","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0400","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1111\/j.1365-2443.2006.01021.x","article-title":"The molecular chaperone HSP47 rapidly senses gravitational changes in myoblasts","volume":"11","author":"Oguro","year":"2006","journal-title":"Genes Cells"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0405","doi-asserted-by":"crossref","first-page":"1580","DOI":"10.1158\/0008-5472.CAN-14-1027","article-title":"Chaperone Hsp47 drives malignant growth and invasion by modulating an ECM gene network","volume":"75","author":"Zhu","year":"2015","journal-title":"Cancer Res."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0410","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1309\/3PAM-P5WL-2LV0-R4EG","article-title":"Immunohistochemical validation of a novel epithelial and a novel stromal marker of pancreatic ductal adenocarcinoma identified by global expression microarrays: sea urchin fascin homolog and heat shock protein 47","volume":"118","author":"Maitra","year":"2002","journal-title":"Am. J. Clin. Pathol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0415","first-page":"71","article-title":"Immunohistochemical distribution of heat shock protein 47 (HSP47) in scirrhous carcinoma of the stomach","volume":"26","author":"Hirai","year":"2006","journal-title":"Anticancer Res."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0420","doi-asserted-by":"crossref","first-page":"1855","DOI":"10.3892\/ijo.2013.2145","article-title":"Tumor-suppressive microRNA-29a inhibits cancer cell migration and invasion via targeting HSP47 in cervical squamous cell carcinoma","volume":"43","author":"Yamamoto","year":"2013","journal-title":"Int. J. Oncol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0425","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1097\/MOP.0000000000000117","article-title":"Osteogenesis imperfecta due to mutations in non-collagenous genes: lessons in the biology of bone formation","volume":"26","author":"Marini","year":"2014","journal-title":"Curr. Opin. Pediatr."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0430","doi-asserted-by":"crossref","first-page":"e1000579","DOI":"10.1371\/journal.pgen.1000579","article-title":"A missense mutation in the SERPINH1 gene in dachshunds with osteogenesis imperfecta","volume":"5","author":"Dr\u00f6gem\u00fcller","year":"2009","journal-title":"PLoS Genet."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0435","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/j.ajhg.2010.01.034","article-title":"Homozygosity for a missense mutation in SERPINH1 which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta","volume":"86","author":"Christiansen","year":"2010","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0440","doi-asserted-by":"crossref","first-page":"1918","DOI":"10.1093\/hmg\/ddu608","article-title":"HSP47 and FKBP65 cooperate in the synthesis of type I procollagen","volume":"24","author":"Duran","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0445","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/j.bbrc.2015.12.028","article-title":"Mutants of collagen-specific molecular chaperone Hsp47 causing osteogenesis imperfecta are structurally unstable with weak binding affinity to collagen","volume":"469","author":"Ito","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0450","doi-asserted-by":"crossref","first-page":"17679","DOI":"10.1074\/jbc.M115.661025","article-title":"Molecular consequences of the SERPINH1\/HSP47 mutation in the dachshund natural model of osteogenesis imperfecta","volume":"290","author":"Lindert","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0455","doi-asserted-by":"crossref","first-page":"1796","DOI":"10.1073\/pnas.97.4.1796","article-title":"Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: a potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency","volume":"97","author":"Burrows","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0460","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1053\/j.gastro.2008.03.003","article-title":"Mechanisms of hepatic fibrogenesis","volume":"134","author":"Friedman","year":"2008","journal-title":"Gastroenterology"},{"key":"10.1016\/j.semcdb.2016.11.005_bib0465","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1038\/nm.2807","article-title":"Mechanisms of fibrosis: therapeutic translation for fibrotic disease","volume":"18","author":"Wynn","year":"2012","journal-title":"Nat. Med."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0470","doi-asserted-by":"crossref","first-page":"167sr161","DOI":"10.1126\/scitranslmed.3004700","article-title":"Therapy for fibrotic diseases: nearing the starting line","volume":"5","author":"Friedman","year":"2013","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0475","first-page":"967","article-title":"Antisense oligonucleotides against collagen-binding stress protein HSP47 suppress collagen accumulation in experimental glomerulonephritis","volume":"78","author":"Sunamoto","year":"1998","journal-title":"Lab. Invest."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0480","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1038\/nbt1396","article-title":"Resolution of liver cirrhosis using vitamin A-coupled liposomes to deliver siRNA against a collagen-specific chaperone","volume":"26","author":"Sato","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0485","article-title":"Deletion of the collagen-specific molecular chaperone hsp47 causes endoplasmic reticulum stress-mediated apoptosis of hepatic stellate cells","author":"Kawasaki","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0490","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.bbrc.2014.12.051","article-title":"De novo design based pharmacophore query generation and virtual screening for the discovery of Hsp-47 inhibitors","volume":"456","author":"Katarkar","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.semcdb.2016.11.005_bib0495","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1021\/jm049148+","article-title":"Identification of small molecule chemical inhibitors of the collagen-specific chaperone Hsp47","volume":"48","author":"Thomson","year":"2005","journal-title":"J. Med. Chem."}],"container-title":["Seminars in Cell & Developmental Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1084952116303846?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1084952116303846?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,7,12]],"date-time":"2022-07-12T23:55:53Z","timestamp":1657670153000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1084952116303846"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,2]]},"references-count":99,"alternative-id":["S1084952116303846"],"URL":"https:\/\/doi.org\/10.1016\/j.semcdb.2016.11.005","relation":{},"ISSN":["1084-9521"],"issn-type":[{"value":"1084-9521","type":"print"}],"subject":[],"published":{"date-parts":[[2017,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Biology of Hsp47 (Serpin H1), a collagen-specific molecular chaperone","name":"articletitle","label":"Article Title"},{"value":"Seminars in Cell & Developmental Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.semcdb.2016.11.005","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}