메뉴 건너뛰기




Volumn 22, Issue 5, 2003, Pages 385-391

Covalent cross-links in collagen: A personal account of their discovery

Author keywords

Collagen; Covalent cross links; Cyanogen bromide; Lysyl aldehydes

Indexed keywords

AMINO ACID; COLLAGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 2; CYANOGEN BROMIDE; GUANIDINE; HYDROXYLAMINE; PROTEIN SUBUNIT;

EID: 0242606868     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(03)00061-1     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0033514449 scopus 로고    scopus 로고
    • Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: Indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17
    • Bank R.A., Robins S.P., Wijmenga C., et al. Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17. Proc. Natl. Acad. Sci. USA. 96:1999;1054-1058.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1054-1058
    • Bank, R.A.1    Robins, S.P.2    Wijmenga, C.3
  • 2
    • 0242485143 scopus 로고
    • The participation of aspartyl residues in the hydroxylamine- or hydrazine-sensitive bonds of collagen
    • Blumenfeld O.O., Gallop P.M. The participation of aspartyl residues in the hydroxylamine- or hydrazine-sensitive bonds of collagen. Biochemistry. 1:1962;947-959.
    • (1962) Biochemistry , vol.1 , pp. 947-959
    • Blumenfeld, O.O.1    Gallop, P.M.2
  • 3
    • 0013958521 scopus 로고
    • Amino aldehydes in tropocollagen: The nature of a probable cross-link
    • Blumenfeld O.O., Gallop P.M. Amino aldehydes in tropocollagen: the nature of a probable cross-link. Proc. Natl. Acad. Sci. USA. 56:1966;1260-1267.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.56 , pp. 1260-1267
    • Blumenfeld, O.O.1    Gallop, P.M.2
  • 4
    • 0242401812 scopus 로고
    • Subunits of hydroxylamine-treated tropocollagen
    • Blumenfeld O.O., Rojkind M., Gallop P.M. Subunits of hydroxylamine- treated tropocollagen. Biochemistry. 4:1965;1780-1788.
    • (1965) Biochemistry , vol.4 , pp. 1780-1788
    • Blumenfeld, O.O.1    Rojkind, M.2    Gallop, P.M.3
  • 5
    • 0014670518 scopus 로고
    • The nature of a hydroxylamine-sensitive bond in collagen
    • Bornstein P. The nature of a hydroxylamine-sensitive bond in collagen. Biochem. Biophys. Res. Commun. 36:1969;957-964.
    • (1969) Biochem. Biophys. Res. Commun. , vol.36 , pp. 957-964
    • Bornstein, P.1
  • 6
    • 0014938141 scopus 로고
    • Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine- sensitive bond and composition of tryptic peptides
    • Bornstein P. Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides. Biochemistry. 9:1970;2408-2421.
    • (1970) Biochemistry , vol.9 , pp. 2408-2421
    • Bornstein, P.1
  • 7
    • 0014962696 scopus 로고
    • The specific nonenzymatic cleavage of bovine ribonuclease with hydroxylamine
    • Bornstein P., Balian G. The specific nonenzymatic cleavage of bovine ribonuclease with hydroxylamine. J. Biol. Chem. 245:1970;4854-4856.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4854-4856
    • Bornstein, P.1    Balian, G.2
  • 8
    • 0013881733 scopus 로고
    • The nature and location of intramolecular cross-links in collagen
    • Bornstein P., Kang A.H., Piez K.A. The nature and location of intramolecular cross-links in collagen. Proc. Natl. Acad. Sci. USA. 55:1966a;417-424.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 417-424
    • Bornstein, P.1    Kang, A.H.2    Piez, K.A.3
  • 9
    • 0007916704 scopus 로고
    • The limited cleavage of native collagen with chymotrypsin, trypsin, and cyanogen bromide
    • Bornstein P., Kang A.H., Piez K.A. The limited cleavage of native collagen with chymotrypsin, trypsin, and cyanogen bromide. Biochemistry. 5:1966b;3803-3812.
    • (1966) Biochemistry , vol.5 , pp. 3803-3812
    • Bornstein, P.1    Kang, A.H.2    Piez, K.A.3
  • 10
    • 0242485139 scopus 로고
    • A biochemical study of human skin collagen and the relation between intra- and intermolecular cross-linking
    • Bornstein P., Piez K.A. A biochemical study of human skin collagen and the relation between intra- and intermolecular cross-linking. J. Clin. Invest. 43:1964;1813-1823.
    • (1964) J. Clin. Invest. , vol.43 , pp. 1813-1823
    • Bornstein, P.1    Piez, K.A.2
  • 11
    • 0011970761 scopus 로고
    • Collagen: Structural studies based on the cleavage of methionyl bonds
    • Bornstein P., Piez K.A. Collagen: structural studies based on the cleavage of methionyl bonds. Science. 148:1965;1353-1355.
    • (1965) Science , vol.148 , pp. 1353-1355
    • Bornstein, P.1    Piez, K.A.2
  • 12
    • 0013970797 scopus 로고
    • The nature of the intramolecular cross-links in collagen. The separation and characterization of peptides from the cross-link region of rat skin collagen
    • Bornstein P., Piez K.A. The nature of the intramolecular cross-links in collagen. The separation and characterization of peptides from the cross-link region of rat skin collagen. Biochemistry. 5:1966;3460-3473.
    • (1966) Biochemistry , vol.5 , pp. 3460-3473
    • Bornstein, P.1    Piez, K.A.2
  • 13
    • 0035374511 scopus 로고    scopus 로고
    • Structural characterization of pyrrolic cross-links in collagen using a biotinylated Ehrlich's reagent
    • Brady J.D., Robins S.P. Structural characterization of pyrrolic cross-links in collagen using a biotinylated Ehrlich's reagent. J. Biol. Chem. 276:2001;18812-18818.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18812-18818
    • Brady, J.D.1    Robins, S.P.2
  • 14
    • 0014690561 scopus 로고
    • The identity of a hydroxylamine-sensitive bond in the α1 chain of rat skin collagen
    • Butler W.T. The identity of a hydroxylamine-sensitive bond in the α1 chain of rat skin collagen. J. Biol. Chem. 244:1969;3415-3422.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3415-3422
    • Butler, W.T.1
  • 15
    • 0014180887 scopus 로고
    • Isolation and characterization of the cyanogen bromide peptides from the α1 chain of rat skin collagen
    • Butler W.T., Piez K.A., Bornstein P. Isolation and characterization of the cyanogen bromide peptides from the α1 chain of rat skin collagen. Biochemistry. 6:1967;3771-3780.
    • (1967) Biochemistry , vol.6 , pp. 3771-3780
    • Butler, W.T.1    Piez, K.A.2    Bornstein, P.3
  • 17
    • 0013875072 scopus 로고
    • 3,2,1:A,B,C sub-unit hypothesis for the α-chains of tropocollagen
    • Gallop P.M. 3,2,1:A,B,C sub-unit hypothesis for the α-chains of tropocollagen. Nature. 209:1966;73-74.
    • (1966) Nature , vol.209 , pp. 73-74
    • Gallop, P.M.1
  • 18
    • 73049160443 scopus 로고
    • Nonenzymatic cleavage of peptide bonds: The methionine residues in bovine pancreatic ribonuclease
    • Gross E., Witkop B. Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease. J. Biol. Chem. 237:1962;1856-1860.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1856-1860
    • Gross, E.1    Witkop, B.2
  • 20
    • 0013821052 scopus 로고
    • The unusual links and crosslinks of collagen
    • Harding J.J. The unusual links and crosslinks of collagen. Adv. Prot. Chem. 20:1965;109-190.
    • (1965) Adv. Prot. Chem. , vol.20 , pp. 109-190
    • Harding, J.J.1
  • 21
    • 0002846317 scopus 로고    scopus 로고
    • The collagen family: Structure, assembly, and organization of the extracellular matrix
    • P.M. Royce, & B. Steinmann. New York, NY: Wiley-Liss, Inc
    • Kielty C.M., Grant M.E. The collagen family: structure, assembly, and organization of the extracellular matrix. Royce P.M., Steinmann B. Connective Tissue and its Heritable Disorders. 2002;159-221 Wiley-Liss, Inc, New York, NY.
    • (2002) Connective Tissue and its Heritable Disorders , pp. 159-221
    • Kielty, C.M.1    Grant, M.E.2
  • 22
    • 0037759702 scopus 로고
    • Studies on the mode of action of lathyrogenic compounds
    • Levene C.I. Studies on the mode of action of lathyrogenic compounds. J. Exp. Med. 116:1962;119-130.
    • (1962) J. Exp. Med. , vol.116 , pp. 119-130
    • Levene, C.I.1
  • 23
    • 0000830030 scopus 로고
    • Alterations in state of molecular aggregation of collagen induced in chick embryos by β-amino-propionitrile (lathyrus factor)
    • Levene C.I., Gross J. Alterations in state of molecular aggregation of collagen induced in chick embryos by β-amino-propionitrile (lathyrus factor). J. Exp. Med. 110:1959;771.
    • (1959) J. Exp. Med. , vol.110 , pp. 771
    • Levene, C.I.1    Gross, J.2
  • 24
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand L., Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nature Rev. 4:2003;140-156.
    • (2003) Nature Rev. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 25
    • 0242653595 scopus 로고
    • 14C] glycine into the subunits of collagens from normal and lathyritic animals
    • 14C] glycine into the subunits of collagens from normal and lathyritic animals. Biochem. Biophys. Acta. 69:1963;472-479.
    • (1963) Biochem. Biophys. Acta , vol.69 , pp. 472-479
    • Martin, G.R.1    Piez, K.A.2    Lewis, M.S.3
  • 26
    • 0015232048 scopus 로고
    • Identification of three genetically distinct collagens by cyanogen bromide cleavage of insoluble human skin and cartilage collagen
    • Miller E.J., Epstein E.H., Piez K.A. Identification of three genetically distinct collagens by cyanogen bromide cleavage of insoluble human skin and cartilage collagen. Biochem. Biophys. Res. Commun. 42:1971;1024-1029.
    • (1971) Biochem. Biophys. Res. Commun. , vol.42 , pp. 1024-1029
    • Miller, E.J.1    Epstein, E.H.2    Piez, K.A.3
  • 27
    • 0013773681 scopus 로고
    • The utilization of lysine in the biosynthesis of elastin crosslinks
    • Miller E.J., Martin G.R., Piez K.A. The utilization of lysine in the biosynthesis of elastin crosslinks. Biochem. Biophys. Res. Commun. 17:1964;248-253.
    • (1964) Biochem. Biophys. Res. Commun. , vol.17 , pp. 248-253
    • Miller, E.J.1    Martin, G.R.2    Piez, K.A.3
  • 28
    • 25044454369 scopus 로고
    • Cleavage with cyanogen bromide of methionyl bonds in collagen
    • Nordwig A., Dick Y.P. Cleavage with cyanogen bromide of methionyl bonds in collagen. Biochim. Biophys. Acta. 97:1965;179-182.
    • (1965) Biochim. Biophys. Acta , vol.97 , pp. 179-182
    • Nordwig, A.1    Dick, Y.P.2
  • 29
    • 0013834388 scopus 로고
    • Characterization of a collagen from codfish skin containing three chromatographically different α chains
    • Piez K.A. Characterization of a collagen from codfish skin containing three chromatographically different α chains. Biochemistry. 4:1965;2590-2596.
    • (1965) Biochemistry , vol.4 , pp. 2590-2596
    • Piez, K.A.1
  • 30
    • 0014228848 scopus 로고
    • Cross-linking of collagen and elastin
    • Piez K.A. Cross-linking of collagen and elastin. Ann. Rev. Biochem. 37:1968;547-570.
    • (1968) Ann. Rev. Biochem. , vol.37 , pp. 547-570
    • Piez, K.A.1
  • 31
    • 0002955886 scopus 로고    scopus 로고
    • Research on collagen in the author's laboratory, 1952-1982
    • P.M. Royce, & B. Steinmann. New York, NY: Wiley-Liss, Inc
    • Piez K.A. Research on collagen in the author's laboratory, 1952-1982. Royce P.M., Steinmann B. Connective Tissue and its Heritable Disorders. 2002;1-11 Wiley-Liss, Inc, New York, NY.
    • (2002) Connective Tissue and its Heritable Disorders , pp. 1-11
    • Piez, K.A.1
  • 32
    • 0348155268 scopus 로고
    • The chromatographic separation and amino acid composition of the subunits of several collagens
    • Piez K.A., Eigner E.A., Lewis M.S. The chromatographic separation and amino acid composition of the subunits of several collagens. Biochemistry. 2:1963;58-66.
    • (1963) Biochemistry , vol.2 , pp. 58-66
    • Piez, K.A.1    Eigner, E.A.2    Lewis, M.S.3
  • 33
    • 0014348347 scopus 로고
    • The cross-linking of collagen and elastin: Enzymatic conversion of lysine in peptide linkage to α-aminoadipic-δ-semialdehyde (allysine) by an extract from bone
    • Pinnell S.R., Martin G.R. The cross-linking of collagen and elastin: enzymatic conversion of lysine in peptide linkage to α-aminoadipic- δ-semialdehyde (allysine) by an extract from bone. Proc. Natl. Acad. Sci. USA. 61:1968;708-716.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 708-716
    • Pinnell, S.R.1    Martin, G.R.2
  • 34
    • 0014010451 scopus 로고
    • Localization and partial characterization of an aldehydic component in tropocollagen
    • Rojkind M., Blumenfeld O.O., Gallop P.M. Localization and partial characterization of an aldehydic component in tropocollagen. J. Biol. Chem. 241:1966;1530-1536.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1530-1536
    • Rojkind, M.1    Blumenfeld, O.O.2    Gallop, P.M.3
  • 35
    • 0001371421 scopus 로고
    • Degradation products from elastin
    • Thomas J., Elsden D.F., Partridge S.M. Degradation products from elastin. Nature. 200:1963;651-652.
    • (1963) Nature , vol.200 , pp. 651-652
    • Thomas, J.1    Elsden, D.F.2    Partridge, S.M.3
  • 36
    • 0023664834 scopus 로고
    • Structure and formation of a stable histidine based trifunctional cross-link in skin collagen
    • Yamauchi M., London R.E., Guenat C., Hashimoto F., Mechanic G.L. Structure and formation of a stable histidine based trifunctional cross-link in skin collagen. J. Biol. Chem. 262:1987;11428-11434.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11428-11434
    • Yamauchi, M.1    London, R.E.2    Guenat, C.3    Hashimoto, F.4    Mechanic, G.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.