The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
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Hydroxylation of COLLs prolyl residues is essential for proper assembly and thermal stabilization of COLLs triple helices through intramolecular hydrogen bonding.
“Hydroxylation of COLLs prolyl residues is essential for proper assembly and thermal stabilization of COLLs triple helices through intramolecular hydrogen bonding [40], since under-hydroxylation results in abnormal assembly, and reduced thermal stability of newly synthesized procollagen chains [39].”
Cites
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The Chemistry and Structure of Collagen
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Isolation and characterization of a chick cartilage collagen containing three identical chains
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Self-citationDehm, P., & Prockop, D. J. (1972) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(72)90302-9 · Cited by 198 · see citing works
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Self-citationThe Function of Hydroxyproline in Collagens
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Chemical, biochemical, functional, and nutritional characteristics of collagen in food systems
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Molecular insights into prolyl and lysyl hydroxylation of fibrillar collagens in health and disease
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Hsp47 as a Collagen-Specific Molecular Chaperone
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Topically applied vitamin C increases the density of dermal papillae in aged human skin
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Collagen Prolyl 4-Hydroxylase as a Therapeutic Target: Miniperspective
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Vitamins and photoaging: Do scientific data support their use?
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Amino Acids, Peptides, and Proteins
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- Authors
- Berg, R. A., & Prockop, D. J.
- Affiliations
- Rutgers, The State University of New Jersey (US)
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1973-05
- Volume
- 52
- Issue
- 1
- Pages
- 115-120
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2003292237
- Cited by
- 582
- References
- 10
- Citations by year
- 2026: 13 · 2025: 12 · 2024: 9 · 2023: 11 · 2022: 13 · 2021: 8 · 2020: 12 · 2019: 15 · 2018: 15 · 2017: 11 · 2016: 16 · 2015: 15 · 2014: 8 · 2013: 15 · 2012: 13
- FWCI
- 22.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- collagen, hydroxyproline, hydroxylation, thermal stability, triple helix, melting point, alpha chain, alpha,alpha'-dipyridyl, optical rotation
- MeSH terms
- Animals, Carbon Isotopes, Chick Embryo, Chromatography, Gel, Chymotrypsin, Collagen, Drug Stability, Electrophoresis, Polyacrylamide Gel, Hot Temperature, Hydroxyproline, Kinetics, Protein Conformation, Protein Denaturation, Protein Precursors, Skin, Sodium Dodecyl Sulfate, Tendons, Culture Techniques
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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