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128 related items for PubMed ID: 7929094

  • 1. The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and III procollagen.
    Lees JF, Bulleid NJ.
    J Biol Chem; 1994 Sep 30; 269(39):24354-60. PubMed ID: 7929094
    [Abstract] [Full Text] [Related]

  • 2. Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation.
    Bulleid NJ, Wilson R, Lees JF.
    Biochem J; 1996 Jul 01; 317 ( Pt 1)(Pt 1):195-202. PubMed ID: 8694764
    [Abstract] [Full Text] [Related]

  • 3. Role of the pro-alpha2(I) COOH-terminal region in assembly of type I collagen: disruption of two intramolecular disulfide bonds in pro-alpha2(I) blocks assembly of type I collagen.
    Doyle SA, Smith BD.
    J Cell Biochem; 1998 Nov 01; 71(2):233-42. PubMed ID: 9779821
    [Abstract] [Full Text] [Related]

  • 4. Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen.
    Lees JF, Tasab M, Bulleid NJ.
    EMBO J; 1997 Mar 03; 16(5):908-16. PubMed ID: 9118952
    [Abstract] [Full Text] [Related]

  • 5. The molecular defect in an autosomal dominant form of osteogenesis imperfecta. Synthesis of type I procollagen containing cysteine in the triple-helical domain of pro-alpha 1(I) chains.
    de Vries WN, de Wet WJ.
    J Biol Chem; 1986 Jul 05; 261(19):9056-64. PubMed ID: 3722186
    [Abstract] [Full Text] [Related]

  • 6. Endoplasmic reticulum protein Hsp47 binds specifically to the N-terminal globular domain of the amino-propeptide of the procollagen I alpha 1 (I)-chain.
    Hu G, Gura T, Sabsay B, Sauk J, Dixit SN, Veis A.
    J Cell Biochem; 1995 Nov 05; 59(3):350-67. PubMed ID: 8567753
    [Abstract] [Full Text] [Related]

  • 7. Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly.
    Lamandé SR, Chessler SD, Golub SB, Byers PH, Chan D, Cole WG, Sillence DO, Bateman JF.
    J Biol Chem; 1995 Apr 14; 270(15):8642-9. PubMed ID: 7721766
    [Abstract] [Full Text] [Related]

  • 8. Assembly of the type 1 procollagen molecule: selectivity of the interactions between the alpha 1(I)- and alpha 2(I)-carboxyl propeptides.
    Alvares K, Siddiqui F, Malone J, Veis A.
    Biochemistry; 1999 Apr 27; 38(17):5401-11. PubMed ID: 10220327
    [Abstract] [Full Text] [Related]

  • 9. Disruption of one intra-chain disulphide bond in the carboxyl-terminal propeptide of the proalpha1(I) chain of type I procollagen permits slow assembly and secretion of overmodified, but stable procollagen trimers and results in mild osteogenesis imperfecta.
    Pace JM, Kuslich CD, Willing MC, Byers PH.
    J Med Genet; 2001 Jul 27; 38(7):443-9. PubMed ID: 11432962
    [Abstract] [Full Text] [Related]

  • 10. Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta.
    Chessler SD, Wallis GA, Byers PH.
    J Biol Chem; 1993 Aug 25; 268(24):18218-25. PubMed ID: 8349697
    [Abstract] [Full Text] [Related]

  • 11. Chain assembly intermediate in the biosynthesis of type III procollagen in chick embryo blood vessels.
    Bächinger HP, Fessler LI, Timpl R, Fessler JH.
    J Biol Chem; 1981 Dec 25; 256(24):13193-9. PubMed ID: 6273419
    [Abstract] [Full Text] [Related]

  • 12. Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding.
    Oliver JE, Thompson EM, Pope FM, Nicholls AC.
    Hum Mutat; 1996 Dec 25; 7(4):318-26. PubMed ID: 8723681
    [Abstract] [Full Text] [Related]

  • 13. Structure and assembly of the heterotrimeric and homotrimeric C-propeptides of type I collagen: significance of the alpha2(I) chain.
    Malone JP, Alvares K, Veis A.
    Biochemistry; 2005 Nov 22; 44(46):15269-79. PubMed ID: 16285730
    [Abstract] [Full Text] [Related]

  • 14. Cysteine residues required for the attachment of the light chain in human IgA2.
    Chintalacharuvu KR, Yu LJ, Bhola N, Kobayashi K, Fernandez CZ, Morrison SL.
    J Immunol; 2002 Nov 01; 169(9):5072-7. PubMed ID: 12391223
    [Abstract] [Full Text] [Related]

  • 15. Interchain disulfide bond formation in types I and II procollagen. Evidence for a protein disulfide isomerase catalyzing bond formation.
    Koivu J, Myllylä R.
    J Biol Chem; 1987 May 05; 262(13):6159-64. PubMed ID: 3571251
    [Abstract] [Full Text] [Related]

  • 16. The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis.
    Bulleid NJ, Dalley JA, Lees JF.
    EMBO J; 1997 Nov 17; 16(22):6694-701. PubMed ID: 9362484
    [Abstract] [Full Text] [Related]

  • 17. Complete primary structure of the human alpha 2 type V procollagen COOH-terminal propeptide.
    Myers JC, Loidl HR, Seyer JM, Dion AS.
    J Biol Chem; 1985 Sep 15; 260(20):11216-22. PubMed ID: 2411731
    [Abstract] [Full Text] [Related]

  • 18. Distinct cysteine sulfhydryl environments detected by analysis of Raman S-hh markers of Cys-->Ser mutant proteins.
    Raso SW, Clark PL, Haase-Pettingell C, King J, Thomas GJ.
    J Mol Biol; 2001 Mar 30; 307(3):899-911. PubMed ID: 11273709
    [Abstract] [Full Text] [Related]

  • 19. Prolyl 4-hydroxylase: defective assembly of alpha-subunit mutants indicates that assembled alpha-subunits are intramolecularly disulfide bonded.
    John DC, Bulleid NJ.
    Biochemistry; 1994 Nov 29; 33(47):14018-25. PubMed ID: 7947811
    [Abstract] [Full Text] [Related]

  • 20. Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike.
    Haase-Pettingell C, Betts S, Raso SW, Stuart L, Robinson A, King J.
    Protein Sci; 2001 Feb 29; 10(2):397-410. PubMed ID: 11266625
    [Abstract] [Full Text] [Related]

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