J D Schofield|D J Prockop - JoVE Visualize

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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.

Collagen and Related Research|September 1, 1985

Altered helical structure of a homotrimer of alpha 1(I)chains synthesized by fibroblasts from a variant of osteogenesis imperfectaS B Deak, M van der Rest, D J Prockop

The Journal of Biological Chemistry|December 10, 1983

The mRNAs for the pro-alpha 1(I) and pro-alpha 2(I) chains of type I procollagen are translated at the same rate in normal human fibroblasts and in fibroblasts from two variants of osteogenesis imperfecta with altered steady state ratios of the two mRNAsW J de Wet, M L Chu, D J Prockop

Biochemistry|February 16, 1982

Partial purification of a procollagen C-proteinase. Inhibition by synthetic peptides and sequential cleavage of type I procollagenF K Njieha, T Morikawa, L Tuderman, et al.

Analytical Biochemistry|December 1, 1994

Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycolY Hojima, B Behta, A M Romanic, et al.

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Showing results (71-80 of 270) with videos related to

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Pageof 27

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.

Collagen and Related Research|September 1, 1985

Altered helical structure of a homotrimer of alpha 1(I)chains synthesized by fibroblasts from a variant of osteogenesis imperfectaS B Deak, M van der Rest, D J Prockop

The Journal of Biological Chemistry|December 10, 1983

The mRNAs for the pro-alpha 1(I) and pro-alpha 2(I) chains of type I procollagen are translated at the same rate in normal human fibroblasts and in fibroblasts from two variants of osteogenesis imperfecta with altered steady state ratios of the two mRNAsW J de Wet, M L Chu, D J Prockop

Biochemistry|February 16, 1982

Partial purification of a procollagen C-proteinase. Inhibition by synthetic peptides and sequential cleavage of type I procollagenF K Njieha, T Morikawa, L Tuderman, et al.

Analytical Biochemistry|December 1, 1994

Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycolY Hojima, B Behta, A M Romanic, et al.

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