{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T22:23:54Z","timestamp":1778624634885,"version":"3.51.4"},"reference-count":47,"publisher":"The Royal Society","issue":"1406","license":[{"start":{"date-parts":[[2001,2,28]],"date-time":"2001-02-28T00:00:00Z","timestamp":983318400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/royalsociety.org\/journals\/ethics-policies\/data-sharing-mining\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Phil. Trans. R. Soc. Lond. B"],"published-print":{"date-parts":[[2001,2,28]]},"abstract":"<jats:p>\n                    Misfolding of the triple helix has been shown to play a critical role in collagen diseases. The substitution of a single Gly by another amino acid breaks the characteristic repeating (Gly\u2013X\u2013Y)\n                    <jats:sub>n<\/jats:sub>\n                    sequence pattern and results in connective tissue disease such as osteogenesis imperfecta. Nuclear magnetic resonance (NMR) studies of normal and mutated collagen triple\u2013helical peptides offer an opportunity to characterize folding and conformational alterations at the substitution site, as well as at positions upstream and downstream of a Gly mutation. The NMR studies suggest that the local sequences surrounding the substitution site, and the renucleation sequences N\u2013terminal to and adjacent to the substitution site, may be critical in defining the clinical phenotype of osteogenesis imperfecta. These studies may pave the way to understanding the mechanism by which a single Gly substitution in collagen can lead to pathological conditions.\n                  <\/jats:p>","DOI":"10.1098\/rstb.2000.0761","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T19:58:30Z","timestamp":1027713510000},"page":"159-168","source":"Crossref","is-referenced-by-count":24,"title":["Nuclear magnetic resonance characterization of peptide models of collagen\u2013folding diseases"],"prefix":"10.1098","volume":"356","author":[{"given":"Alexei","family":"Buevich","sequence":"first","affiliation":[{"name":"Department of Chemistry, Rutgers University, Piscataway, NJ 08855\u20130939, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean","family":"Baum","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Rutgers University, Piscataway, NJ 08855\u20130939, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"175","published-online":{"date-parts":[[2001,2,28]]},"reference":[{"key":"p_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.12.7668"},{"key":"p_2","article-title":"The in\u00a3uence of peptidyl-prolyl cis^trans isomerase on the in vitro folding of type III collagen","volume":"262","author":"B\u00ccchinger H. P.","year":"1987","journal-title":"J. Biol. Chem."},{"key":"p_3","article-title":"The role of cis^trans isomerization of peptide bonds in the coil\/ triple helix conversion of collagen","volume":"90","author":"B\u00ccchinger H. P.","year":"1978","journal-title":"Eur. J. Biochem."},{"key":"p_4","article-title":"Folding mechanism of the triple helix in type-III collagen and type-II pN-collagen. Role of disul\u00a2de bridges and peptide bond isomerization","volume":"106","author":"B\u00ccchinger H. P.","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"p_5","doi-asserted-by":"crossref","unstructured":"Baum J. & Brodsky B. 1997 Real-time NMR investigations of triple helix folding and collagen folding diseases. Fold. Design 2 R53^ R60.","DOI":"10.1016\/S1359-0278(97)00028-X"},{"key":"p_6","doi-asserted-by":"crossref","unstructured":"Baum J. & Brodsky B. 1999 Folding of peptide models of collagen and misfolding in disease. Curr. Opin. Struct. Biol. 9 122^128.","DOI":"10.1016\/S0959-440X(99)80016-5"},{"key":"p_7","doi-asserted-by":"crossref","unstructured":"Baum J. & Brodsky B. 2000 Folding of the collagen triple helix and its naturally occurring mutants (ed. R. H. Pain pp. 330^347. Oxford University Press.","DOI":"10.1093\/oso\/9780199637898.003.0012"},{"key":"p_8","doi-asserted-by":"crossref","unstructured":"Beck K. Chan V. C. Shenoy N. Kirkpatrick A. Ramshaw J. A. M. & Brodsky B. 2000 Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine. Proc. Natl Acad. Sci. USA 97 4273^4278.","DOI":"10.1073\/pnas.070050097"},{"key":"p_9","doi-asserted-by":"publisher","DOI":"10.1126\/science.7695699"},{"key":"p_10","doi-asserted-by":"crossref","unstructured":"Bonadio J. & Byers P. 1985 Subtle structural alterations in the chains of type I procollagen produce osteogenesis imperfecta type II. Nature 316 363^366.","DOI":"10.1038\/316363a0"},{"key":"p_11","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(67)80066-4"},{"key":"p_12","doi-asserted-by":"crossref","unstructured":"Brodsky B. & Ramshaw J. A. 1997 The collagen triple-helix structure. Matrix Biol. 15 545^554.","DOI":"10.1016\/S0945-053X(97)90030-5"},{"key":"p_13","doi-asserted-by":"publisher","DOI":"10.1096\/fasebj.9.15.8529832"},{"key":"p_14","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1978.tb12640.x"},{"key":"p_15","doi-asserted-by":"crossref","unstructured":"Buevich A. V. Dai Q.-H. Liu X. Brodsky B. & Baum J. 2000 Site-speci\u00a2c NMR monitoring of cis^trans isomerization in the folding of the proline-rich collagen triple helix. Biochemistry 39 4299^4308.","DOI":"10.1021\/bi992584r"},{"key":"p_16","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/16.22.6694"},{"key":"p_17","unstructured":"Byers P. H. 1993 Osteogenesis imperfecta. In Connective tissue and its heritable disorders: molecular genetic and medical aspects (ed. P. M. Royce & B. Steinmann pp. 317^350. New York: Wiley Liss."},{"key":"p_18","first-page":"19","article-title":"From Levinthal to pathways to funnels","volume":"4","author":"Dill K. A.","year":"1997","journal-title":"Nat. Struct. Biol."},{"key":"p_19","doi-asserted-by":"crossref","unstructured":"Dobson C. M. & Hore P. J. 1998 Kinetics studies of protein folding using NMR spectroscopy. Nat. Struct. Biol. 5(Suppl. 504^507.","DOI":"10.1038\/744"},{"key":"p_20","doi-asserted-by":"crossref","unstructured":"Dobson C. M. Sali A. & Karplus M. 1998 Protein folding: a perspective from theory and experiment. Angewante Chem. Int. Ed. 37 868^893.","DOI":"10.1002\/(SICI)1521-3773(19980420)37:7<868::AID-ANIE868>3.0.CO;2-H"},{"key":"p_21","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.physchem.47.1.369"},{"key":"p_22","doi-asserted-by":"crossref","unstructured":"Dyson H. J. & Wright P. E. 1998 Equilibrium NMR studies of unfolded and partially folded proteins. Nat. Struct. Biol. 5(Suppl. 499^503.","DOI":"10.1038\/739"},{"key":"p_23","unstructured":"Engel J. 1987 Folding and unfolding of collagen triple helices. In Advances in meat research vol. 4 (ed. A. M. Pearson T. R. Dutson & A. J. Bailey pp. 145^161. New York: Van Nostrand Reinhold."},{"key":"p_24","article-title":"The zipper-like folding of collagen triple-helices and the e\u00a1ects of mutations that disrupt the zipper","volume":"20","author":"Engel J.","year":"1991","journal-title":"A. Rev. Biophys. Biophys. Chem."},{"key":"p_25","doi-asserted-by":"crossref","unstructured":"Fields G. B. & Prockop D. J. 1996 Perspectives on synthesis and applications of triple-helical collagen model peptides. Biopolymers 40 345^357.","DOI":"10.1002\/(SICI)1097-0282(1996)40:4<345::AID-BIP1>3.0.CO;2-W"},{"key":"p_26","doi-asserted-by":"crossref","unstructured":"Goodman M. Bhumralkar M. Je\u00a1erson E. A. Kwak J. & Locardi E. 1998 Collagen mimetics. Biopolymers (Pept. Sci. 47 127^142.","DOI":"10.1002\/(SICI)1097-0282(1998)47:2<127::AID-BIP2>3.0.CO;2-W"},{"key":"p_27","doi-asserted-by":"crossref","unstructured":"Harrington W. & Von Hippel P. H. 1961 Formation and stabilization of the collagen-fold. Arch. Biochem. Biophys. 92 110^113.","DOI":"10.1016\/0003-9861(61)90224-7"},{"key":"p_28","doi-asserted-by":"crossref","unstructured":"Harrison R. K. & Stein R. L. 1990 Substrate speci\u00a2cities of the peptidyl prolyl cis^trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry 29 3813^3816.","DOI":"10.1021\/bi00468a001"},{"key":"p_29","doi-asserted-by":"crossref","unstructured":"Kelly J. W. Colon W. Lai Z. Lashuel H. A. McCulloch J. McCutchen S. L. Miroy G. J. & Peterson S. A. 1997 Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Adv. Protein Chem. 60 161^181.","DOI":"10.1016\/S0065-3233(08)60321-6"},{"key":"p_30","unstructured":"Kielty C. M. Hopkinson I. & Grant M. E. 1993 Connective tissue and its hereditable disorders molecular genetic and medical aspects. In The collagen family: structure assembly and organization in the extracellular matrix (ed. P. M. Royes & B. U. Steinmann pp. 103^147. New York: Wiley Liss."},{"key":"p_31","doi-asserted-by":"crossref","unstructured":"Kuivaniemi H. Tromp G. & Prockop D. 1997 Mutations in \u00a2brillar collagens (types I II II and IX \u00a2bril-associated collagen (type IX and network-forming collagen (type X cause a spectrum of diseases of bone cartilage and blood vessels. Hum. Mutat. 9 300^315.","DOI":"10.1002\/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9"},{"key":"p_32","doi-asserted-by":"crossref","unstructured":"Lansbury Jr P. T. 1997 Structural neurology: are seeds at the root of neuronal degeneration? Neuron 19 1151^1154.","DOI":"10.1016\/S0896-6273(00)80406-7"},{"key":"p_33","unstructured":"Liu X. 1997 Real-time NMR investigation of triple helical peptide folding and collagen folding diseases. New Brunswick NJ: Rutgers University."},{"key":"p_34","doi-asserted-by":"crossref","unstructured":"Liu X. Siegel D. L. Fan P. Brodsky B. & Baum J. 1996 Direct NMR measurement of the folding kinetics of a trimeric peptide. Biochemistry 35 4306^4313.","DOI":"10.1021\/bi952270d"},{"key":"p_35","unstructured":"Liu X. Kim S. Dai Q.-H. Brodsky B. & Baum J. 1998 NMR shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease. Biochemistry 33 15 528^15 533."},{"key":"p_36","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(92)91020-P"},{"key":"p_37","doi-asserted-by":"crossref","unstructured":"Long C. G. Braswell E. Zhu D. Apigo J. Baum J. & Brodsky B. 1993 Characterization of collagen-like peptides containing interruptions in the repeating Gly-X-Y sequence. Biochemistry 32 11688^11695.","DOI":"10.1021\/bi00094a027"},{"key":"p_38","doi-asserted-by":"crossref","unstructured":"McLaughlin S. H. & Bulleid N. J. 1997 Molecular recognition in procollagen chain assembly. Matrix Biol. 16 369^377.","DOI":"10.1016\/S0945-053X(98)90010-5"},{"key":"p_39","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.62.070193.003253"},{"key":"p_40","doi-asserted-by":"crossref","unstructured":"Mayo K. H. 1996 NMR and X-ray studies of collagen model peptides. Biopolymers 40 359^370.","DOI":"10.1002\/(SICI)1097-0282(1996)40:4<359::AID-BIP2>3.0.CO;2-V"},{"key":"p_41","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(79)90240-7"},{"key":"p_42","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.64.070195.002155"},{"key":"p_43","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1994.1199"},{"key":"p_44","article-title":"The molecular structure of collagen","volume":"3","author":"Rich A.","year":"1961","journal-title":"J. Mol. Biol."},{"key":"p_45","doi-asserted-by":"crossref","unstructured":"Roder H. & Shastry M. R. 1999 Methods for exploring early events in protein folding. Curr. Opin. Struct. Biol. 9 620^626.","DOI":"10.1016\/S0959-440X(99)00015-9"},{"key":"p_46","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(68)90237-4"},{"key":"p_47","doi-asserted-by":"crossref","unstructured":"Yang W. Battinenni M. & Brodsky B. 1997 Amino acid sequence environment modulates the disruption by osteogenesis imperfecta glycine substitutions in collagen-like peptides. Biochemistry 36 6930^6935.","DOI":"10.1021\/bi970051h"}],"container-title":["Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/royalsocietypublishing.org\/doi\/pdf\/10.1098\/rstb.2000.0761","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/royalsocietypublishing.org\/doi\/pdf\/10.1098\/rstb.2000.0761","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T21:26:26Z","timestamp":1778621186000},"score":1,"resource":{"primary":{"URL":"http:\/\/royalsocietypublishing.org\/rstb\/article\/356\/1406\/159-168\/19755"}},"subtitle":[],"editor":[{"given":"C. M.","family":"Dobson","sequence":"additional","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]},{"given":"R. J.","family":"Ellis","sequence":"additional","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]},{"given":"A. R.","family":"Fersht","sequence":"additional","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2001,2,28]]},"references-count":47,"journal-issue":{"issue":"1406","published-print":{"date-parts":[[2001,2,28]]}},"alternative-id":["10.1098\/rstb.2000.0761"],"URL":"https:\/\/doi.org\/10.1098\/rstb.2000.0761","relation":{},"ISSN":["0962-8436","1471-2970"],"issn-type":[{"value":"0962-8436","type":"print"},{"value":"1471-2970","type":"electronic"}],"subject":[],"published":{"date-parts":[[2001,2,28]]}}}