Type I collagen is thermally unstable at body temperature - Wikidata - awgldk - TriplyDB

Type I collagen is thermally unstable at body temperature

Type I collagen is thermally unstable at body temperature

http://www.wikidata.org/entity/Q34009096

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Aegyptin displays high-affinity for the von Willebrand factor binding site (RGQOGVMGF) in collagen and inhibits carotid thrombus formation in vivo Collagen structure and stability Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis Always cleave up your mess: targeting collagen degradation to treat tissue fibrosis Matrix metalloproteinase interactions with collagen and elastin Development and characterization of a eukaryotic expression system for human type II procollagen Internal strain drives spontaneous periodic buckling in collagen and regulates remodeling.Mechanical strain stabilizes reconstituted collagen fibrils against enzymatic degradation by mammalian collagenase matrix metalloproteinase 8 (MMP-8)Implications for Collagen Binding from the Crystallographic Structure of Fibronectin 6FnI1-2FnII7FnI Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1 Structural Analysis of Collagen Type I Interactions with Human Fibronectin Reveals a Cooperative Binding Mode A Unique Set of the Burkholderia Collagen-Like Proteins Provides Insight into Pathogenesis, Genome Evolution and Niche Adaptation, and Infection Detection The cysteine-rich region of type VII collagen is a cystine knot with a new topology Thermal denaturation studies of collagen by microthermal analysis and atomic force microscopy Triple-helical collagen hydrogels via covalent aromatic functionalization with 1,3-Phenylenediacetic acid Collagen-like proteins of pathogenic streptococci Early emphysema in the tight skin and pallid mice: roles of microfibril-associated glycoproteins, collagen, and mechanical forces.Real Time FRET Based Detection of Mechanical Stress in Cytoskeletal and Extracellular Matrix Proteins Collagen unfolding accelerates water influx, determining hydration in the interstitial matrix.Interstitial-matrix edema in burns: mechanistic insights from subatmospheric pressure treatment in vivo.Hydroxylation-induced stabilization of the collagen triple helix. Acetyl-(glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)(10)-NH(2) forms a highly stable triple helix.Cleavage of fibromodulin in cartilage explants involves removal of the N-terminal tyrosine sulfate-rich region by proteolysis at a site that is sensitive to matrix metalloproteinase-13.Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges.Strain-induced alignment in collagen gels.Segregation of type I collagen homo- and heterotrimers in fibrils Mechanical strain enhances survivability of collagen micronetworks in the presence of collagenase: implications for load-bearing matrix growth and stability Increased C-telopeptide cross-linking of tendon type I collagen in fibromodulin-deficient mice.The local pathology of interstitial edema: surface tension increases hydration potential in heat-damaged skin.Unstable molecules form stable tissues Diffusion of MMPs on the surface of collagen fibrils: the mobile cell surface-collagen substratum interface.Methacrylation induces rapid, temperature-dependent, reversible self-assembly of type-I collagen A Mechanistic study of Plasma Treatment Effects on Demineralized Dentin Surfaces for Improved Adhesive/Dentin Interface Bonding Collagen-like proteins in pathogenic E. coli strains.Double thermal transitions of type I collagen in acidic solution.Nanomechanical mapping of hydrated rat tail tendon collagen I fibrils.Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.Fibronectin: functional character and role in alcoholic liver disease.Chaperoning osteogenesis: new protein-folding disease paradigms.

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Type I collagen is thermally unstable at body temperature

http://www.wikidata.org/entity/Q34009096

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2002 nî lūn-bûn

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2002 թուականի Յունուարին հրատարակուած գիտական յօդուած

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Type I collagen is thermally unstable at body temperature

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Type I collagen is thermally unstable at body temperature

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Type I collagen is thermally unstable at body temperature

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Type I collagen is thermally unstable at body temperature

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Type I collagen is thermally unstable at body temperature

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Type I collagen is thermally unstable at body temperature

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Type I collagen is thermally unstable at body temperature

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Type I collagen is thermally unstable at body temperature

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Type I collagen is thermally unstable at body temperature

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Proceedings of the National Academy of Sciences of the United States of America

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Type I collagen is thermally unstable at body temperature

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E Leikina

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M V Mertts

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P2860

Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen

Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis

Structural bases of collagen stabilization induced by proline hydroxylation

Mutations in collagen genes: causes of rare and some common diseases in humans

Procollagen folding and assembly: the role of endoplasmic reticulum enzymes and molecular chaperones.

Polymer-in-a-box mechanism for the thermal stabilization of collagen molecules in fibers.

Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine

Synthesis and turnover of collagen precursors in rabbit skin.

Stability of proteins. Proteins which do not present a single cooperative system.

A new approach to assessing collagen turnover by using a micro-assay. A highly efficient and rapid turnover of collagen in rat periodontal tissues

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