Tyrosine sulfation in precursors of collagen V.
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Summary
The tyrosine sulfate is located in a noncollagenous domain, which is probably adjacent to the amino end of the collagen helix, and is retained throughout the physiological proteolytic processing of procollagens V.
- Type
- article
- Published
- 1986-04-15
- Cited by
- 33
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1511292826
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24917590
Keywords
Sulfation, Chemistry, Tyrosine, Ammonium sulfate precipitation, Sodium dodecyl sulfate
References
Cited by
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- Basement-membrane stromal relationships: interactions between collagen fibrils and the lamina densa.
- Sulfation of the choriogonadotropin alpha subunit in human placental explants.
- Progesterone effect on intracellular inorganic sulphate in uterine epithelial cells.
- Dermatopontin: A potential predictor for metastasis of human oral cancer
- Protein tyrosine sulfation, 1993--an update.
- ROLE OF TYROSINE-SULFATED PROTEINS IN RETINAL STRUCTURE AND FUNCTION
- Different splice variants of cartilage alpha1(XI) collagen chain undergo uniform amino-terminal processing.
- Chlorate inhibits tyrosine sulfation of human type III procollagen without affecting its secretion or processing.
- Characterization of the Six Zebrafish Clade B Fibrillar Procollagen Genes, with Evidence for Evolutionarily Conserved Alternative Splicing within the pro-α1(V) C-propeptide
- Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly.
- Minor fibrillar collagens; variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation
- Caracterização da resposta imune em modelo experimental de esclerodermia induzida por colágeno tipo V
- Extracellular Matrix Remodeling: The Common Denominator in Connective Tissue Diseases Possibilities for Evaluation and Current Understanding of the Matrix as More Than a Passive Architecture, but a Key Player in Tissue Failure
- Collagens--structure, function, and biosynthesis.
- Intracellular transport and tyrosine sulfation of procollagens V.
- Type V collagen: molecular structure and fibrillar organization of the chicken alpha 1(V) NH2-terminal domain, a putative regulator of corneal fibrillogenesis
- Tyrosine sulfation and the secretory pathway.
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