BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

128 related articles for article (PubMed ID: 8157695)

  • 1. Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotype.
    Romanic AM; Spotila LD; Adachi E; Engel J; Hojima Y; Prockop DJ
    J Biol Chem; 1994 Apr; 269(15):11614-9. PubMed ID: 8157695
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Copolymerization of normal type I collagen with three mutated type I collagens containing substitutions of cysteine at different glycine positions in the alpha 1 (I) chain.
    Torre-Blanco A; Adachi E; Romanic AM; Prockop DJ
    J Biol Chem; 1992 Mar; 267(7):4968-73. PubMed ID: 1537873
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Type I procollagens containing substitutions of aspartate, arginine, and cysteine for glycine in the pro alpha 1 (I) chain are cleaved slowly by N-proteinase, but only the cysteine substitution introduces a kink in the molecule.
    Lightfoot SJ; Holmes DF; Brass A; Grant ME; Byers PH; Kadler KE
    J Biol Chem; 1992 Dec; 267(35):25521-8. PubMed ID: 1460046
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase.
    Lightfoot SJ; Atkinson MS; Murphy G; Byers PH; Kadler KE
    J Biol Chem; 1994 Dec; 269(48):30352-7. PubMed ID: 7982948
    [TBL] [Abstract][Full Text] [Related]  

  • 5. A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structures.
    Kadler KE; Torre-Blanco A; Adachi E; Vogel BE; Hojima Y; Prockop DJ
    Biochemistry; 1991 May; 30(20):5081-8. PubMed ID: 2036375
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Self-assembly into fibrils of collagen II by enzymic cleavage of recombinant procollagen II. Lag period, critical concentration, and morphology of fibrils differ from collagen I.
    Fertala A; Sieron AL; Hojima Y; Ganguly A; Prockop DJ
    J Biol Chem; 1994 Apr; 269(15):11584-9. PubMed ID: 8157691
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks.
    Westerhausen A; Kishi J; Prockop DJ
    J Biol Chem; 1990 Aug; 265(23):13995-4000. PubMed ID: 2116413
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid specific.
    Pack M; Constantinou CD; Kalia K; Nielsen KB; Prockop DJ
    J Biol Chem; 1989 Nov; 264(33):19694-9. PubMed ID: 2511192
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Formation of collagen fibrils by enzymic cleavage of precursors of type I collagen in vitro.
    Miyahara M; Hayashi K; Berger J; Tanzawa K; Njieha FK; Trelstad RL; Prockop DJ
    J Biol Chem; 1984 Aug; 259(15):9891-8. PubMed ID: 6430905
    [TBL] [Abstract][Full Text] [Related]  

  • 10. A substitution of cysteine for glycine 748 of the alpha 1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away.
    Vogel BE; Doelz R; Kadler KE; Hojima Y; Engel J; Prockop DJ
    J Biol Chem; 1988 Dec; 263(35):19249-55. PubMed ID: 3198624
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Polymerization of pNcollagen I and copolymerization of pNcollagen I with collagen I. A kinetic, thermodynamic, and morphologic study.
    Romanic AM; Adachi E; Hojima Y; Engel J; Prockop DJ
    J Biol Chem; 1992 Nov; 267(31):22265-71. PubMed ID: 1331049
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Temperature-induced post-translational over-modification of type I procollagen. Effects of over-modification of the protein on the rate of cleavage by procollagen N-proteinase and on self-assembly of collagen into fibrils.
    Torre-Blanco A; Adachi E; Hojima Y; Wootton JA; Minor RR; Prockop DJ
    J Biol Chem; 1992 Feb; 267(4):2650-5. PubMed ID: 1733961
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Substitution of aspartic acid for glycine at position 310 in type II collagen produces achondrogenesis II, and substitution of serine at position 805 produces hypochondrogenesis: analysis of genotype-phenotype relationships.
    Bonaventure J; Cohen-Solal L; Ritvaniemi P; Van Maldergem L; Kadhom N; Delezoide AL; Maroteaux P; Prockop DJ; Ala-Kokko L
    Biochem J; 1995 May; 307 ( Pt 3)(Pt 3):823-30. PubMed ID: 7741714
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Formation of collagen fibrils in vitro by cleavage of procollagen with procollagen proteinases.
    Miyahara M; Njieha FK; Prockop DJ
    J Biol Chem; 1982 Jul; 257(14):8442-8. PubMed ID: 6806297
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Ehlers-Danlos syndrome type VIIB. Morphology of type I collagen fibrils formed in vivo and in vitro is determined by the conformation of the retained N-propeptide.
    Holmes DF; Watson RB; Steinmann B; Kadler KE
    J Biol Chem; 1993 Jul; 268(21):15758-65. PubMed ID: 8340401
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Mutations that alter the primary structure of type I procollagen have long-range effects on its cleavage by procollagen N-proteinase.
    Dombrowski KE; Vogel BE; Prockop DJ
    Biochemistry; 1989 Aug; 28(17):7107-12. PubMed ID: 2684272
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Two cysteine substitutions in procollagen I: a glycine replacement near the N-terminus of alpha 1(I) chain causes lethal osteogenesis imperfecta and a glycine replacement in the alpha 2(I) chain markedly destabilizes the triple helix.
    Fertala A; Westerhausen A; Morris G; Rooney JE; Prockop DJ
    Biochem J; 1993 Jan; 289 ( Pt 1)(Pt 1):195-9. PubMed ID: 8424758
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pNcollagen that are near circular in cross-section.
    Watson RB; Wallis GA; Holmes DF; Viljoen D; Byers PH; Kadler KE
    J Biol Chem; 1992 May; 267(13):9093-100. PubMed ID: 1577745
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process.
    Kadler KE; Hojima Y; Prockop DJ
    J Biol Chem; 1987 Nov; 262(32):15696-701. PubMed ID: 3316206
    [TBL] [Abstract][Full Text] [Related]  

  • 20. A single base mutation that substitutes serine for glycine 790 of the alpha 1 (III) chain of type III procollagen exposes an arginine and causes Ehlers-Danlos syndrome IV.
    Tromp G; Kuivaniemi H; Shikata H; Prockop DJ
    J Biol Chem; 1989 Jan; 264(3):1349-52. PubMed ID: 2492273
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 7.