Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

D J Prockop

Showing results (21-30 of 266) with videos related to

Pageof 27
Sort By:
Genomics|November 1, 1990
Completion of the intron-exon structure of the gene for human type II procollagen (COL2A1): variations in the nucleotide sequences of the alleles from three chromosomesL Ala-Kokko, D J Prockop
The Journal of Biological Chemistry|November 15, 1988
Cleavage of type I and type II procollagens by type I/II procollagen N-proteinase. Correlation of kinetic constants with the predicted conformations of procollagen substratesK E Dombrowski, D J Prockop
Biopolymers|January 1, 1996
Perspectives on the synthesis and application of triple-helical, collagen-model peptidesG B Fields, D J Prockop
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1974
Ferritin-conjugated antibodies used for labeling of organelles involved in the cellular synthesis and transport of procollagenB R Olsen, D J Prockop
Biotechniques|January 1, 1993
Use of an automated workstation to facilitate PCR amplification, loading agarose gels and sequencing of DNA templatesD Harrison, C Baldwin, D J Prockop
The Journal of Biological Chemistry|August 15, 1990
Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocksA Westerhausen, J Kishi, D J Prockop
Human Mutation|January 1, 1997
Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vesselsH Kuivaniemi, G Tromp, D J Prockop
The Journal of Biological Chemistry|November 25, 1984
A heterozygous defect for structurally altered pro-alpha 2 chain of type I procollagen in a mild variant of osteogenesis imperfecta. The altered structure decreases the thermal stability of procollagen and makes it resistant to procollagen N-proteinaseM Sippola, S Kaffe, D J Prockop
FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|April 1, 1991
Mutations in collagen genes: causes of rare and some common diseases in humansH Kuivaniemi, G Tromp, D J Prockop
Biochemistry|January 29, 1985
Sequential cleavage of type I procollagen by procollagen N-proteinase. An intermediate containing an uncleaved pro alpha 1(I) chainJ Berger, K Tanzawa, D J Prockop
Pageof 27

Showing results (21-30 of 266) with videos related to

Sort By:
Pageof 27
Genomics|November 1, 1990
Completion of the intron-exon structure of the gene for human type II procollagen (COL2A1): variations in the nucleotide sequences of the alleles from three chromosomesL Ala-Kokko, D J Prockop
The Journal of Biological Chemistry|November 15, 1988
Cleavage of type I and type II procollagens by type I/II procollagen N-proteinase. Correlation of kinetic constants with the predicted conformations of procollagen substratesK E Dombrowski, D J Prockop
Biopolymers|January 1, 1996
Perspectives on the synthesis and application of triple-helical, collagen-model peptidesG B Fields, D J Prockop
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1974
Ferritin-conjugated antibodies used for labeling of organelles involved in the cellular synthesis and transport of procollagenB R Olsen, D J Prockop
Biotechniques|January 1, 1993
Use of an automated workstation to facilitate PCR amplification, loading agarose gels and sequencing of DNA templatesD Harrison, C Baldwin, D J Prockop
The Journal of Biological Chemistry|August 15, 1990
Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocksA Westerhausen, J Kishi, D J Prockop
Human Mutation|January 1, 1997
Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vesselsH Kuivaniemi, G Tromp, D J Prockop
The Journal of Biological Chemistry|November 25, 1984
A heterozygous defect for structurally altered pro-alpha 2 chain of type I procollagen in a mild variant of osteogenesis imperfecta. The altered structure decreases the thermal stability of procollagen and makes it resistant to procollagen N-proteinaseM Sippola, S Kaffe, D J Prockop
FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|April 1, 1991
Mutations in collagen genes: causes of rare and some common diseases in humansH Kuivaniemi, G Tromp, D J Prockop
Biochemistry|January 29, 1985
Sequential cleavage of type I procollagen by procollagen N-proteinase. An intermediate containing an uncleaved pro alpha 1(I) chainJ Berger, K Tanzawa, D J Prockop
Pageof 27