Rate of helix formation by intracellular procollagen and protocollagen. Evidence for a role for disulfide bons
Authors:
- Jouni UittoJUJouni Uitto
- Darwin J. ProckopDPDarwin J. Prockop
- 1 December 1973
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 55 (3) , 904-911
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Procollagen-A Precursor Form of CollagenClinical Orthopaedics and Related Research, 1973
- Purification of carbon-14-labeled protocollagen and its hydroxylation by prolyl-hydroxylaseBiochemistry, 1973
- The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagenBiochemical and Biophysical Research Communications, 1973
- Hydroxyproline stabilizes the triple helix of chick tendon collagenBiochemical and Biophysical Research Communications, 1973
- Time lag in the secretion of collagen by matrix-free tendon cells and inhibition of the secretory process by colchicine and vinblastineBiochimica et Biophysica Acta (BBA) - General Subjects, 1972
- Procollagen: Conversion of the Precursor to Collagen by a Neutral ProteaseScience, 1972
- Electronoptical studies of procollagen from the skin of dermatosparaxic calvesFEBS Letters, 1971
- Further evidence for a transport form of collagen. Its extrusion and extracellular conversion to tropocollagen in embryonic tendonFEBS Letters, 1971
- The Chemistry and Structure of Collagen1971
- The Renaturation of Soluble Collagen. Products Formed at Different Temperatures*Biochemistry, 1966