Synthesis of type I procollagen: formation of interchain disulfide bonds before complete hydroxylation of the protein.

[1]  C. Clark The distribution and initial characterization of oligosaccharide units on the COOH-terminal propeptide extensions of the pro-alpha 1 and pro-alpha 2 chains of type I procollagen. , 1979, The Journal of biological chemistry.

[2]  C. Lapière,et al.  Amino acid sequence of the aminoterminal segment of dermatosparactic calf-skin procollagen type I. , 1979, European journal of biochemistry.

[3]  K. Kivirikko,et al.  [Biosynthesis of collagen and its disorders]. , 1979, Duodecim; laaketieteellinen aikakauskirja.

[4]  R. Crystal,et al.  Synthesis and degradation of collagen by skin fibroblasts from controls and from patients with osteogenesis imperfecta , 1979, FEBS letters.

[5]  W. Kao,et al.  Kinetics for the secretion of nonhelical procollagen by freshly isolated tendon cells. , 1979, The Journal of biological chemistry.

[6]  R. Crystal,et al.  Degradation of newly synthesized collagen. , 1978, The Journal of biological chemistry.

[7]  W. Kao,et al.  Procollagen polypeptides containing cis-4-hydroxy-L-proline are overglycosylated and secreted as nonhelical pro-gamma-chains. , 1978, Archives of biochemistry and biophysics.

[8]  K. Kivirikko,et al.  Further studies on the effect of the collagen triple-helix formation on the hydroxylation of lysine and the glycosylations of hydroxylysine in chick-embryo tendon and cartilage cells. , 1977, The Biochemical journal.

[9]  B. Olsen,et al.  Purification and characterization of a peptide from the carboxy-terminal region of chick tendon procollagen type I. , 1977, Biochemistry.

[10]  K. Kivirikko,et al.  Effect of L-azetidine-2-carboxylic acid on glycosylations of collagen in chick-embryo tendon cells. , 1976, The Biochemical journal.

[11]  B. Olsen,et al.  Interchain disulfide bonds at the COOH-terminal end of procollagen synthesized by matrix-free cells from chick embryonic tendon and cartilage. , 1976, Archives of biochemistry and biophysics.

[12]  R. Timpl,et al.  NH2-terminal extensions on skin collagen from sheep with a genetic defect in conversion of procollagen into collagen. , 1976, Biochemistry.

[13]  L. Lukens Time of occurrence of disulfide linking between procollagen chains. , 1976, The Journal of biological chemistry.

[14]  K. Kivirikko,et al.  Hydroxylation of lysine and glycosylation of hydroxylysine during collagen biosynthesis in isolated chick-embryo cartilage cells. , 1976, The Biochemical journal.

[15]  W. Kao,et al.  Primary and secondary effects of ascorbate on procollagen synthesis and protein synthesis by primary cultures of tendon fibroblasts. , 1976, Archives of biochemistry and biophysics.

[16]  J. Uitto,et al.  Synthesis of elastin and procallagen by cells from embryonic aorta. Differences in the role of hydroxyproline and the effects of proline analogs on the secretion of the two proteins. , 1976, Archives of biochemistry and biophysics.

[17]  S. Jimenez,et al.  Secretion of unhydroxylated chick tendon procollagen. , 1975, Biochemical and biophysical research communications.

[18]  K. Kivirikko,et al.  Glucosylation of galactosylhydroxylysyl residues in collagen in vitro by collagen glucosyltransferase. Inhibition by triple-helical conformation of the substrate. , 1975, European journal of biochemistry.

[19]  N. Morris,et al.  Procollagen assembly and secretion in embryonic chick bone. , 1975, The Journal of biological chemistry.

[20]  A. Veis,et al.  The intracellular location of the glycosylation of hydroxylysine of collagen. , 1975, Biochemical and Biophysical Research Communications - BBRC.

[21]  J. Uitto,et al.  Biosynthesis of cartilage procollagen. Influence of chain association and hydroxylation of prolyl residues on the folding of the polypeptides into the triple-helical conformation. , 1974, Biochemistry.

[22]  J. Uitto,et al.  Synthesis and secretion of under-hydroxylated procollagen at various temperatures by cells subject to temporary anoxia. , 1974, Biochemical and Biophysical Research Communications - BBRC.

[23]  J. Uitto,et al.  Hydroxylation of peptide-bound proline and lysine before and after chain completion of the polypeptide chains of procollagen. , 1974, Archives of biochemistry and biophysics.

[24]  W. Bonner,et al.  A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. , 1974, European journal of biochemistry.

[25]  J. Uitto,et al.  Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cells. , 1974, Biochemistry.

[26]  J. Uitto,et al.  Intracellular hydroxylation of non-helical protocollagen to form triple-helical procollagen and subsequent secretion of the molecule. , 1974, European journal of biochemistry.

[27]  C. Levene,et al.  The activation of protocollagen proline hydroxylase by ascorbic acid in cultured 3T6 fibroblasts , 1974 .

[28]  D. Jackson,et al.  The sub-cellular location of inter-chain disulfide bond formation during procollagen biosynthesis by embryonic chick tendon cells. , 1973, Biochemical and biophysical research communications.

[29]  P. Bornstein,et al.  Further hydroxylation of lysyl residues in collagen by protocollagen lysyl hydroxylase in vitro. , 1973, Biochemistry.

[30]  D. Prockop,et al.  The biosynthesis of basement membrane collagen in embryonic chick lens. 3. Intracellular formation of the triple helix and the formation of aggregates through disulfide bonds. , 1973, The Journal of biological chemistry.

[31]  F. Studier,et al.  Analysis of bacteriophage T7 early RNAs and proteins on slab gels. , 1973, Journal of molecular biology.

[32]  D. Prockop,et al.  Purification of (14C) protocollagen and its hydroxylation by prolyl-hydroxylase. , 1973, Biochemistry.

[33]  B. Peterkofsky,et al.  The effect of ascorbic acid on collagen polypeptide synthesis and proline hydroxylation during the growth of cultured fibroblasts. , 1972, Archives of biochemistry and biophysics.

[34]  N. A. Kefalides,et al.  Simple chromatographic method for determination of 14 C-labeled lysine, hydroxylysine, and hydroxylysine glycosides. , 1972, Analytical biochemistry.

[35]  D. Prockop,et al.  Time lag in the secretion of collagen by matrix-free tendon cells and inhibition of the secretory process by colchicine and vinblastine. , 1972, Biochimica et biophysica acta.

[36]  J. King,et al.  Polypeptides of the tail fibres of bacteriophage T4. , 1971, Journal of molecular biology.

[37]  S. Jimenez,et al.  Further evidence for a transport form of collagen. Its extrusion and extracellular conversion to tropocollagen in embryonic tendon. , 1971, FEBS letters.

[38]  L. Lukens,et al.  Collagen polysomes: site of hydroxylation of proline residues. , 1971, Journal of molecular biology.

[39]  S. Udenfriend,et al.  Hydroxylation of proline residues in collagen nascent chains. , 1970, Archives of biochemistry and biophysics.

[40]  D. Prockop,et al.  Modified procedure for the assay of H-3-or C-14-labeled hydroxyproline. , 1966, Analytical biochemistry.

[41]  S. Udenfriend,et al.  CONVERSION OF PROLINE TO COLLAGEN HYDROXYPROLINE IN A CELL-FREE SYSTEM FROM CHICK EMBRYO. , 1963, The Journal of biological chemistry.

[42]  P. Bornstein,et al.  Structurally distinct collagen types. , 1980, Annual review of biochemistry.

[43]  K. Kivirikko,et al.  Urinary excretion of hydroxyproline in health and disease. , 1970, International review of connective tissue research.