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Matrix Biology : Journal of the International Society for Matrix Biology|April 3, 1998
Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signalingD J Prockop, A L Sieron, S W Li
Biochemistry|July 29, 1986
Iron-containing metallocenes as active site directed inhibitors of the proteinase that cleaves the NH2-terminal propeptides from type I procollagenK E Dombrowski, J E Sheats, D J Prockop
The Journal of Biological Chemistry|December 15, 1985
Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterizationY Hojima, M van der Rest, D J Prockop
Biochemistry|April 19, 1977
Hydroxylation of (Pro-Pro-Gly)5 and (Pro-Pro-Gly)10 by prolyl hydroxylase. Evidence for an asymmetric active site in the enzymeR A Berg, Y Kishida, S Sakakibara, et al.
American Journal of Medical Genetics|January 15, 1993
Somatic cell mosaicism: another source of phenotypic heterogeneity in nuclear families with osteogenesis imperfectaC D Constantinou-Deltas, R L Ladda, D J Prockop
The Journal of Biological Chemistry|March 7, 1997
Collagen II containing a Cys substitution for arg-alpha1-519. Homotrimeric monomers containing the mutation do not assemble into fibrils but alter the self-assembly of the normal proteinA Fertala, L Ala-Kokko, R Wiaderkiewicz, et al.
Matrix Biology : Journal of the International Society for Matrix Biology|March 1, 1994
Cadmium ions inhibit procollagen C-proteinase and cupric ions inhibit procollagen N-proteinaseY Hojima, B Behta, A M Romanic, et al.
DNA Sequence : the Journal of DNA Sequencing and Mapping|January 1, 1993
Efficient DNA sequencing on microtiter plates using dried reagents and Bst DNA polymeraseJ J Earley, H Kuivaniemi, D J Prockop, et al.
The Journal of Biological Chemistry|August 25, 1991
Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helixT Tsuneyoshi, A Westerhausen, C D Constantinou, et al.
Biochemistry|September 13, 1994
Specific inhibition of expression of a human collagen gene (COL1A1) with modified antisense oligonucleotides. The most effective target sites are clustered in double-stranded regions of the predicted secondary structure for the mRNAA V Laptev, Z Lu, A Colige, et al.
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