About: The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen

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About: The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen Goto Sponge NotDistinct Permalink

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 1978 (ast) vědecký článek publikovaný v roce 1978 (cs) 1978 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած (hyw) 1978 թվականի հոտեմբերին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в жовтні 1978 (uk) scientific journal article (en) im Oktober 1978 veröffentlichter wissenschaftlicher Artikel (de) مقالة علمية (نشرت في 16-10-1978) (ar) vedecký článok (publikovaný 1978/10/16) (sk) wetenschappelijk artikel (gepubliceerd op 1978/10/16) (nl)
publication date	wds:Q28608934-C5741090-81E5-4D4C-A3CD-84A099F4FB6A
publication date	1978-10-16 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28608934-D9112CAD-10BB-4D37-9868-5B8A0BCF1B7C
language of work or name	English
author name string	wds:Q28608934-38F39F9D-6857-4916-83F1-AC7FCDAFA052 wds:Q28608934-74F47CB8-DD8A-4BDA-BD89-6388814A6636 wds:Q28608934-78E7878B-F338-41D5-A72E-C60CCBC2A77A wds:Q28608934-BFA846BA-391E-45E8-9294-85760489C1D6
author name string	J. Engel R. Timpl H. P. Bächinger P. Bruckner
rdfs:label	The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (en) The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (nl) The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (ast)
skos:prefLabel	The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (en) The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (nl) The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (ast)
name	The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (en) The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (nl) The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (ast)
title	wds:Q28608934-44202997-6970-4687-A8BD-2FA559BE943F
title	The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen (en)
page(s)	wds:Q28608934-E8E18789-F7A0-4F02-9D5C-7EBAF85F9371
page(s)	605–613
instance of	wds:Q28608934-B0364BED-F0B6-413D-8521-99761C0362B9
instance of	scholarly article
PubMed ID	wds:Q28608934-7405F528-F0B6-4143-ADA1-6CFBD1F89B1E
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/710450
PubMed ID	710450
published in	wds:Q28608934-649236B9-D4B2-486E-858F-E05CBE281503
published in	FEBS Journal
issue	wds:Q28608934-77DADBA2-0CC4-4233-9232-15FAEE636CB7
volume	wds:Q28608934-BB2006FF-8558-4507-A3D4-2B35D4BB5941
issue	3
volume	90
DOI	wds:Q28608934-93766D4B-124F-4AF2-B3EB-62E4940FD9B9
DOI	http://dx.doi.org/10.1111/J.1432-1033.1978.TB12641.X
DOI	10.1111/J.1432-1033.1978.TB12641.X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28608934
is cites work of	Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes. Thermal stability of calf skin collagen type I in salt solutions Molecular structure and interaction of recombinant human type XVI collagen Homozygosity mapping approach identifies a missense mutation in equine cyclophilin B (PPIB) associated with HERDA in the American Quarter Horse Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier Prolyl isomerases: role in protein folding. Detection of cis and trans X-Pro peptide bonds in proteins by 13C NMR: application to collagen Transformation of the structure of collagen. A time-resolved analysis of mechanochemical processes using synchrotron radiation Assembly of type I collagen fibrils de novo. Between 37 and 41 degrees C the process is limited by micro-unfolding of monomers Lethal osteogenesis imperfecta resulting from a single nucleotide change in one human pro alpha 1(I) collagen allele Collagen fibril biosynthesis in tendon: a review and recent insights. Self-assembly of synthetic collagen triple helices Equilibrium thermal transitions of collagen model peptides pH effects on binding between the anthrax protective antigen and the host cellular receptor CMG2 Matrix metalloproteinase collagenolysis in health and disease Thermal stability of collagen triple helix Solution conformations of the gamma-carboxyglutamic acid domain of bovine prothrombin fragment 1, residues 1-65. The nature of the slow metal ion-dependent conformational transition in bovine prothrombin Procollagen propeptide release by procollagen peptidases and bacterial collagenase Protein disulphide-isomerase activity in chick-embryo tissues. Correlation with the biosynthesis of procollagen Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of alpha 1 (I)-chain glycine-to-arginine substitutions Real-time NMR investigations of triple-helix folding and collagen folding diseases Association of procollagen type V Association of procollagen type XII Association of procollagen type XIV Association of procollagen type XIX Collagen chain trimerization Association of procollagen type VIII Association of procollagen type XIII Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding. Processing of collagen based biomaterials and the resulting materials properties The chain register in heterotrimeric collagen peptides affects triple helix stability and folding kinetics A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis Association of procollagen type I Association of procollagen type VI Procollagen triple helix formation Association of procollagen type II Association of procollagen type III Association of procollagen type IV Association of procollagen type VII Association of procollagen type XI Association of procollagen type XV Association of procollagen type XVII Association of procollagen type XVIII Association of procollagen type XXII Association of procollagen type XXV Association of procollagen type XVIII Ziploc-ing the structure 2.0: Endoplasmic reticulum-resident peptidyl prolyl isomerases show different activities toward hydroxyproline. Trivalent soluble TNF Receptor, a potent TNF-α antagonist for the treatment collagen-induced arthritis.

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