Collagen and elastin fibres

scientific article published on January 1, 1978

Collagen and elastin fibres is …
instance of (P31):
review articleQ7318358
scholarly articleQ13442814

External links are
P953full work available at URLhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/365893/?tool=EBI
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/365893/pdf/?tool=EBI
https://europepmc.org/articles/PMC1347123
https://europepmc.org/articles/PMC1347123?pdf=render
P932PMC publication ID1347123
P698PubMed publication ID365893

P2093author name stringA. J. Bailey
P2860cites workInterchain disulfide bonds in procollagen are located in a large nontriple-helical COOH-terminal domainQ27919705
New Molecular Model for the Long-range Elasticity of ElastinQ28252745
Comparative electron-microscope studies on type-III and type-I collagensQ32035573
Molecular mobility and structure of elastin deduced from the solvent and temperature dependence of carbon-13 magnetic resonance relaxation dataQ32068087
The Coacervate-Sol Transition Observed with α-Elastin and its N-Formyl O-Methyl DerivativeQ33271716
Molecular abnormalities of collagenQ33678955
Isolation and characterization of a fluorescent material in bovine achilles tendon collagenQ34414929
Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagenQ35039994
Kinetics of processing of type I and type III procollagens in fibroblast culturesQ35043507
Biosynthesis of Collagen Crosslinks: Increased Activity of Purified Lysyl Oxidase with Reconstituted Collagen FibrilsQ35119840
Procollagen: biological scission of amino and carboxyl extension peptidesQ37464680
Studies on the Action of Lysyl Oxidase on Soluble ElastinQ39149825
A High Molecular Weight Species of Soluble Elastin-ProelastinQ39439880
The chemistry and structure of collagenQ39867305
Structure and biosynthesis of basement membranesQ39879408
The Biosynthesis of CollagenQ39945276
Basement membrane procollagen is not converted to collagen in organ cultures of parietal yolk sac endodermQ39979405
Intermediates in the Conversion of Procollagen to Collagen. Evidence for Stepwise Limited Proteolysis of the COOH-Terminal Peptide ExtensionsQ40123096
The physical properties of elastic tissueQ40498630
Conformations of the repeat peptides of elastin in solution: an application of proton and carbon-13 magnetic resonance to the determination of polypeptide secondary structureQ40574786
Some Investigations of Elastin Biosynthesis In Vitro Using an ImmunoprecipitantQ40778013
Salt-soluble elastin from lathyritic chicksQ41842754
The chemistry of connective tissues. 2. Soluble proteins derived from partial hydrolysis of elastinQ41971505
Comparative studies of the cross-linked regions of elastin from bovine ligamentum nuchae and bovine, porcine and human aortaQ42555770
The chemistry of the collagen cross-links. The characterization of Fraction C, a possible artifact produced during the reduction of collagen fibres with borohydrideQ42558116
Structure of Two Histidine-containing Cross-Links from CollagenQ44534027
Studies on the location of intermolecular cross-links in collagen. Isolation of a CNBr peptide containing -hydroxylysinonorleucineQ44812368
Molecular Packing in CollagenQ47754977
The elastic properties of elastinQ47846673
The ultrastructural organization of elastinQ47889597
Molecular model for elastin structure and functionQ47936912
Isolation and structural identification of a labile intermolecular crosslink in collagenQ50335737
The stability of collagen cross-links when derived from hydroxylsyl residues.Q53795616
Degradation Products from Elastin: Partial Structure of Two Major Degradation Products from the Cross-linkages in ElastinQ59066837
Coacervation of Solubilized Elastin effects a Notable Conformational ChangeQ59069212
Biological significance of the intermolecular crosslinks of collagenQ59095967
Molecular Pattern in Native CollagenQ59097889
Type III procollagen and collagen in skinQ66897699
Isolation, Chemical and Electron Microscopical Characterization of Neutral-Salt-Soluble Type III Collagen and Procollagen from Fetal Bovine SkinQ66904796
Synthesis of elastin in aortas from chick embryos. Conversion of newly secreted elastin to cross-linked elastin without apparent proteolysis of the moleculeQ67010842
Isolation and structure of a cross linked tripeptide from calf bone collagenQ67313429
Crosslinkage of salt-soluble elastin in vitroQ67321020
Collagen crosslinking: Isolation of hydroxyaldol-histidine, a naturally-occurring crosslinkQ67348561
The synthesis of connective tissue protein in smooth muscle cellsQ67432141
The covalent structure of cartilage collagen. Amino acid sequence of the NH2-terminal helical portion of the alpha 1 (II) chainQ67487220
Biochemical characteristics and biological significance of the genetically-distinct collagensQ68217892
Relative stabilities of the intermediate reducible crosslinks present in collagen fibresQ68695799
Isolation and Characterization of CrossLinked Peptides from ElastinQ68925625
Coacervation of alpha-elastin results in fiber formationQ69999667
Preparation and properties of salt-soluble elastinQ70357120
Mechanism of formation of desmosine and isodesmosine cross-links of elastinQ71442097
Structural features of tropoelastin related to the sites of cross-links in aortic elastinQ71745791
Characterization of the aldehydes present on the cyanogen bromide peptides from mature rat skin collagenQ71850973
Studies on the reduction of bovine elastin: Evidence for the presence of Δ6,7-dehydrolysinonorleucineQ72232705
Biosynthesis and nature of elastin structuresQ72857401
P407language of work or nameEnglishQ1860
P921main subjectcollagenQ26868
P304page(s)49-58
P577publication date1978-01-01
P1433published inJournal of clinical pathology. Supplement (Royal College of Pathologists)Q27711444
P1476titleCollagen and elastin fibres
P478volume12

Reverse relations

cites work (P2860)
Q49484206Decellularization and Solubilization of Porcine Liver for Use as a Substrate for Porcine Hepatocyte Culture: Method Optimization and Comparison
Q50898933[Quantitative polarization microscopy demonstration of collagen type I and type III in histologic paraffin sections].

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