Characterization of Urinary Degradation Products Derived from Type I Collagen
Open Access
- 1 April 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (15) , 9755-9763
- https://doi.org/10.1074/jbc.272.15.9755
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Bone Marrow, Cytokines, and Bone Remodeling — Emerging Insights into the Pathophysiology of OsteoporosisNew England Journal of Medicine, 1995
- In vitro aging of calmodulin generates isoaspartate at multiple Asn–Gly and Asp–Gly sites in calcium‐binding domains II, III, and IVProtein Science, 1993
- Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues: Effects of the solvent dielectricProtein Science, 1993
- Amino acid analysis: Determination of cysteine plus half-cystine in proteins after hydrochloric acid hydrolysis with a disulfide compound as additiveAnalytical Biochemistry, 1989
- The unusual substrate specificity of eukaryotic protein carboxyl methyltransferasesTrends in Biochemical Sciences, 1987
- Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteinsInternational Journal of Peptide and Protein Research, 1987
- Characterisation of a type‐I collagen trimeric cross‐linked peptide from calf aorta and its cross‐linked structureEuropean Journal of Biochemistry, 1987
- An 'Affinity' Method for Preparing Polypeptides Enriched in the Collagen-Associated Ehrlich ChromogenThe Journal of Biochemistry, 1983
- A collagen-associated Ehrlich chromogen: a pyrrolic cross-link?Bioscience Reports, 1981
- The quantitative relationship of urinary peptide hydroxyproline excretion to collagen degradationJournal of Clinical Investigation, 1969