Interchain disulfide bonds at the COOH-terminal end of procollagen synthesized by matrix-free cells from chick embryonic tendon and cartilage.
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- Type
- article
- Published
- 1976-07-01
- Cited by
- 61
- References
- 18
- OpenAlex
- https://openalex.org/W2071820057
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:42029687
Keywords
Procollagen peptidase, Collagenase, Disulfide bond, Chemistry, Cartilage
References
- Protein assembly of procollagen and effects of hydroxylation.
- Characterization of the pro- 1 chain of procollagen.
- Isolation of a disulfide-stabilized, three-chain polypeptide fragment unique to the precursor of human collagen.
- Further characterization of embryonic tendon fibroblasts and the use of immunoferritin techniques to study collagen biosynthesis
- Location of procollagen in chick corneal and tendon fibroblasts with ferritin-conjugated antibodies
- Biosynthesis of cartilage procollagen. Influence of chain association and hydroxylation of prolyl residues on the folding of the polypeptides into the triple-helical conformation.
- Structural studies on cartilage collagen employing limited cleavage and solubilization with pepsin.
- Entrapment of collagen in a polyacrylamide matrix and its application in the purification of animal collagenases.
- Analysis of bacteriophage T7 early RNAs and proteins on slab gels.
- Time lag in the secretion of collagen by matrix-free tendon cells and inhibition of the secretory process by colchicine and vinblastine.
- A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels.
- Some properties of the products of reaction of tadpole collagenase with collagen.
- Biosynthesis of cartilage procollagen.
- Polypeptides of the tail fibres of bacteriophage T4.
- Use of a mixture of proteinase-free collagenases for the specific assay of radioactive collagen in the presence of other proteins.
- Isolation and partial characterization of procollagen fractions produced by a clonal strain of calf dermatosparactic cells.
- The biosynthesis of collagen.
Cited by
- Is newly-secreted elastin cleaved to a smaller molecule before being incorporated into crosslinked elastin fibers?
- Genotype-phenotype relations in patient-derived point mutations in collagen II
- Chemical reduction of disulfides.
- Intermediates in the conversion of procollagen to collagen. Evidence for stepwise limited proteolysis of the COOH-terminal peptide extensions.
- Propeptide-mediated regulation of procollagen synthesis in IMR-90 human lung fibroblast cell cultures. Evidence for transcriptional control.
- The role of glycosylation in the enzymatic conversion of procollagen to collagen: studies using tunicamycin and concanavalin A.
- Isolation and purification of human type I procollagen by adsorption to glass beads.
- Procollagen polypeptides containing cis-4-hydroxy-L-proline are overglycosylated and secreted as nonhelical pro-gamma-chains.
- Studies on structural relationship between two glycoproteins isolated from alveoli of patients with alveolar proteinosis.
- Comparison between avian and human prolyl 4‐hydroxylases: Studies on the holomeric enzymes and their constituent subunits
- Evidence for heterogeneous origin of glomerular basement membrane.
- Synthesis of type I procollagen: formation of interchain disulfide bonds before complete hydroxylation of the protein.
- Kinetics of the incorporation of tropoelastin into elastic fibers in embryonic chick aorta.
- Isolation of unhydroxylated type I procollagen folding of the protein in vitro.
- Purification of procollagen type II by covalent chromatography with activated thiol-sepharose 4B.
- Characterization of Tissue-Specific and Developmentally Regulated Alternative Splicing of Exon 64 in the COL5A1 Gene
- Addition of mannose to both the amino- and carboxy-terminal properties of type II procollagen occurs without formation of a triple helix.
- Synthesis of elastin in aortas from chick embryos. Conversion of newly secreted elastin to cross-linked elastin without apparent proteolysis of the molecule.
- Collagen synthesis by liver stellate cells is released from its normal feedback regulation by acetaldehyde-induced modification of the carboxyl-terminal propeptide of procollagen.
- Characterization of the amino‐terminal segment in procollagen pα2 chain from dermatosparactic sheep
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