Tonndorf R, Aibibu D, Cherif C
Int J Mol Sci. 2021; 22(17).
PMID: 34502469
PMC: 8431235.
DOI: 10.3390/ijms22179561.
Perdivara I, Yamauchi M, Tomer K
Aust J Chem. 2014; 66(7):760-769.
PMID: 25414518
PMC: 4235766.
DOI: 10.1071/CH13174.
Light N, Bailey A
Biochem J. 1980; 189(1):111-24.
PMID: 7458897
PMC: 1161923.
DOI: 10.1042/bj1890111.
Glanville R, Breitkreutz D, Meitinger M, Fietzek P
Biochem J. 1983; 215(1):183-9.
PMID: 6354180
PMC: 1152379.
DOI: 10.1042/bj2150183.
Light N, Bailey A
Biochem J. 1980; 185(2):373-81.
PMID: 6249253
PMC: 1161363.
DOI: 10.1042/bj1850373.
Hydroxylysine in the N-terminal telopeptides of skin collagen from chick embryo and newborn rat.
Barnes M, Constable B, Morton L, KODICEK E
Biochem J. 1971; 125(3):925-8.
PMID: 5145913
PMC: 1178201.
DOI: 10.1042/bj1250925.
Hydroxylysine in the N-terminal regions of the 1 - and 2 -chains of various collagens.
Barnes M, Constable B, Morton L, KODICEK E
Biochem J. 1971; 125(2):433-7.
PMID: 5144746
PMC: 1178077.
DOI: 10.1042/bj1250433.
Studies on the hydroxylation of lysine occurring in the non-helical region at the N-terminal end of the collagen molecule.
Barnes M, Constable B, Morton L, KODICEK E
Biochem J. 1971; 125(2):16P-17P.
PMID: 5144717
PMC: 1178122.
DOI: 10.1042/bj1250016pb.
The chemistry of the collagen cross-links. Age-related changes in the reducible components of intact bovine collagen fibres.
Robins S, Shimokomaki M, Bailey A
Biochem J. 1973; 131(4):771-80.
PMID: 4722452
PMC: 1177537.
DOI: 10.1042/bj1310771.
The purification of bovine cathepsin B1 and its mode of action on bovine collagens.
Etherington D
Biochem J. 1974; 137(3):547-57.
PMID: 4423493
PMC: 1166156.
DOI: 10.1042/bj1370547.
Procollagen: intermediate forms containing several types of peptide chains and non-collagen peptide extensions at NH2 and COOH ends.
Tanzer M, Church R, YAEGER J, WAMPLER D, Park E
Proc Natl Acad Sci U S A. 1974; 71(8):3009-13.
PMID: 4370290
PMC: 388609.
DOI: 10.1073/pnas.71.8.3009.
Collagen cross-linking. Isolation of cross-linked peptides from collagen of chicken bone.
Eyre D, Glimcher M
Biochem J. 1973; 135(3):393-403.
PMID: 4359017
PMC: 1165841.
DOI: 10.1042/bj1350393.
Characterization of conformation independent antigenic determinants in the triple-helical part of calf and rat collagen.
Timpl R, Beil W, Furthmayr H, Meigel W, Pontz B
Immunology. 1971; 21(6):1017-30.
PMID: 4108594
PMC: 1408260.
[Stimulating effect of collagen and collagen derivatives on the propregation and adhesion of thrombocytes in defibrinogenated human citrate plasma and in animal citrate plasma].
Balleisen L, Marx R, Kuhn K
Blut. 1975; 31(2):95-106.
PMID: 1164570
DOI: 10.1007/BF01633725.
Biochemical characteristics and biological significance of the genetically-distinct collagens.
Miller E
Mol Cell Biochem. 1976; 13(3):165-92.
PMID: 1004502
DOI: 10.1007/BF01731779.
Proteins of the periodontium. Characterization of the insoluble collagens of bovine dental cementum.
Birkedal-Hansen H, Butler W, Taylor R
Calcif Tissue Res. 1977; 23(1):39-44.
PMID: 890542
DOI: 10.1007/BF02012764.
Amino acid sequence of the N-terminal non-collagenous segment of dermatosparactic sheep procollagen type I.
Rohde H, Wachter E, Richter W, Bruckner P, Helles O, Timpl R
Biochem J. 1979; 179(3):631-42.
PMID: 475772
PMC: 1186672.
DOI: 10.1042/bj1790631.
Isolation and tissue localization of type AB2 collagen from normal lung parenchyma.
Madri J, Furthmayr H
Am J Pathol. 1979; 94(2):323-31.
PMID: 371411
PMC: 2042247.
