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Science (New York, N.Y.)|December 19, 1975
Retention of nonhelical procollagen containing cis-hydroxyproline in rough endoplasmic reticulumJ Uitto, H Hoffman, D J ProckopThe Journal of Biological Chemistry|January 25, 1985
Type I procollagen N-proteinase from whole chick embryos. Cleavage of a homotrimer of pro-alpha 1(I) chains and the requirement for procollagen with a triple-helical conformationK Tanzawa, J Berger, D J ProckopBiochemistry|June 10, 1980
Inhibitors of procollagen N-protease. Synthetic peptides with sequences similar to the cleavage site in the pro alpha 1(I) chainT Morikawa, L Tuderman, D J ProckopBiochimica Et Biophysica Acta|January 20, 1976
Effects of the stereo-configuration of the hydroxyl group in 4-hydroxyproline on the triple-helical structures formed by homogenous peptides resembling collagenK Inouye, S Sakakibara, D J ProckopProceedings of the National Academy of Sciences of the United States of America|October 1, 1980
A defect in the structure of type I procollagen in a patient who had osteogenesis imperfecta: excess mannose in the COOH-terminal propeptideL Peltonen, A Palotie, D J ProckopClinics in Plastic Surgery|July 1, 1994
Molecular basis of osteogenesis imperfecta and related disorders of boneD J Prockop, H Kuivaniemi, G TrompMatrix Biology : Journal of the International Society for Matrix Biology|July 1, 1995
The complete cDNA coding sequence for the mouse pro alpha 1(I) chain of type I procollagenS W Li, J Khillan, D J ProckopProceedings of the National Academy of Sciences of the United States of America|November 1, 1993
Conformation-sensitive gel electrophoresis for rapid detection of single-base differences in double-stranded PCR products and DNA fragments: evidence for solvent-induced bends in DNA heteroduplexesA Ganguly, M J Rock, D J ProckopEuropean Journal of Biochemistry|September 1, 1981
Formation of the triple helix of type I procollagen in cellulo. A kinetic model based on cis-trans isomerization of peptide bondsP Bruckner, E F Eikenberry, D J ProckopThe Journal of Biological Chemistry|July 25, 1988
Assembly of type I collagen fibrils de novo. Between 37 and 41 degrees C the process is limited by micro-unfolding of monomersK E Kadler, Y Hojima, D J ProckopPageof 27