(Q41058613)

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A recombinant homotrimer of type I procollagen that lacks the central two D-periods. The thermal stability of the triple helix is decreased by 2 to 4 degrees C.

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Europe PubMed Central

PubMed publication ID

26 September 2017

A recombinant homotrimer of type I procollagen that lacks the central two D-periods. The thermal stability of the triple helix is decreased by 2 to 4 degrees C. (English)

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

4

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26 September 2017

Aleksander Sieroń

2

object named as

Sieron AL

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26 September 2017

author name string

Zafarullah K

1

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26 September 2017

Fertala A

3

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26 September 2017

Kuivaniemi H

5

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26 September 2017

Prockop DJ

6

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26 September 2017

publication date

1 November 1997

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26 September 2017

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26 September 2017

16

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26 September 2017

5

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26 September 2017

245-253

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PubMed publication ID

26 September 2017

Sequence specific thermal stability of the collagen triple helix

1 reference

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Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen

1 reference

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NMR and CD studies of triple-helical peptides

1 reference

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Proteolytic enzymes as probes for the triple-helical conformation of procollagen

1 reference

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Presence of a thermostable domain in the helical part of the type I collagen molecule and its role in the mechanism of triple helix folding

1 reference

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7 January 2021

based on heuristic

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The A and B fragments of normal type I procollagen have a similar thermal stability to proteinase digestion but are selectively destabilized by structural mutations.

1 reference

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Altered helical structure of a homotrimer of alpha 1(I)chains synthesized by fibroblasts from a variant of osteogenesis imperfecta

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Influence of different tripeptides on the stability of the collagen triple helix. I. Analysis of the collagen sequence and identification of typical tripeptides

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Backbone dynamics of (Pro-Hyp-Gly)10 and a designed collagen-like triple-helical peptide by 15N NMR relaxation and hydrogen-exchange measurements

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Synthesis of recombinant human procollagen II in a stably transfected tumour cell line (HT1080).

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Expression of human COL1A1 gene in stably transfected HT1080 cells: the production of a thermostable homotrimer of type I collagen in a recombinant system.

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A synthetic model of collagen: an experimental investigation of the triple-helix stability

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Coordinate modulation of melanogenesis and type I trimer collagen secretion by type I collagen substratum during reversible conversion between melanotic and amelanotic cells in mouse B16 melanoma

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Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels

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Collagens: molecular biology, diseases, and potentials for therapy

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Influence of different tripeptides on the stability of the collagen triple helix. II. An experimental approach with appropriate variations of a trimer model oligotripeptide

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Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of human type I procollagen

1 reference

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based on heuristic

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Partial purification and characterization of a neutral protease which cleaves the N-terminal propeptides from procollagen

1 reference

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7 January 2021

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Collagen polymorphism: Isolation and partial characterization of α1(I)-trimer molecules in normal human skin

1 reference

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7 January 2021

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Identifiers

10.1016/S0945-053X(97)90013-5

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

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