These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

120 related articles for article (PubMed ID: 8223589)

  • 1. Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion.
    Valli M; Zolezzi F; Mottes M; Antoniazzi F; Stanzial F; Tenni R; Pignatti P; Cetta G
    Eur J Biochem; 1993 Oct; 217(1):77-82. PubMed ID: 8223589
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix.
    Tsuneyoshi T; Westerhausen A; Constantinou CD; Prockop DJ
    J Biol Chem; 1991 Aug; 266(24):15608-13. PubMed ID: 1874719
    [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 de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a moderate case of osteogenesis imperfecta. Substitution of cysteine for glycine 178 in the triple helical domain.
    Valli M; Mottes M; Tenni R; Sangalli A; Gomez Lira M; Rossi A; Antoniazzi F; Cetta G; Pignatti PF
    J Biol Chem; 1991 Jan; 266(3):1872-8. PubMed ID: 1988452
    [TBL] [Abstract][Full Text] [Related]  

  • 6. The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen.
    Deak SB; Scholz PM; Amenta PS; Constantinou CD; Levi-Minzi SA; Gonzalez-Lavin L; Mackenzie JW
    J Biol Chem; 1991 Nov; 266(32):21827-32. PubMed ID: 1718984
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I procollagen causes lethal osteogenesis imperfecta.
    Kurosaka D; Hattori S; Hori H; Yamaguchi N; Hasegawa T; Akimoto H; Nagai Y
    J Biochem; 1994 May; 115(5):853-7. PubMed ID: 7961597
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 270(15):8642-9. PubMed ID: 7721766
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution.
    Steinmann B; Westerhausen A; Constantinou CD; Superti-Furga A; Prockop DJ
    Biochem J; 1991 Nov; 279 ( Pt 3)(Pt 3):747-52. PubMed ID: 1953667
    [TBL] [Abstract][Full Text] [Related]  

  • 10. G76E substitution in type I collagen is the first nonlethal glutamic acid substitution in the alpha1(I) chain and alters folding of the N-terminal end of the helix.
    Cabral WA; Chernoff EJ; Marini JC
    Mol Genet Metab; 2001 Apr; 72(4):326-35. PubMed ID: 11286507
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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]  

  • 12. 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; 261(19):9056-64. PubMed ID: 3722186
    [TBL] [Abstract][Full Text] [Related]  

  • 13. The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen.
    Cole WG; Patterson E; Bonadio J; Campbell PE; Fortune DW
    J Med Genet; 1992 Feb; 29(2):112-8. PubMed ID: 1613761
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Osteogenesis imperfecta and type-I collagen mutations. A lethal variant caused by a Gly910-->Ala substitution in the alpha 1 (I) chain.
    Valli M; Sangalli A; Rossi A; Mottes M; Forlino A; Tenni R; Pignatti PF; Cetta G
    Eur J Biochem; 1993 Feb; 211(3):415-9. PubMed ID: 7679635
    [TBL] [Abstract][Full Text] [Related]  

  • 15. A point mutation in a type I procollagen gene converts glycine 748 of the alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta.
    Vogel BE; Minor RR; Freund M; Prockop DJ
    J Biol Chem; 1987 Oct; 262(30):14737-44. PubMed ID: 3667599
    [TBL] [Abstract][Full Text] [Related]  

  • 16. SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen chain resulting in osteogenesis imperfecta type II.
    Mackay K; Lund AM; Raghunath M; Steinmann B; Dalgleish R
    Hum Genet; 1993 Jun; 91(5):439-44. PubMed ID: 8100209
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Altered helical structure of a homotrimer of alpha 1(I)chains synthesized by fibroblasts from a variant of osteogenesis imperfecta.
    Deak SB; van der Rest M; Prockop DJ
    Coll Relat Res; 1985 Sep; 5(4):305-13. PubMed ID: 4053561
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Characterization of a type I collagen alpha 2(I) glycine-586 to valine substitution in osteogenesis imperfecta type IV. Detection of the mutation and prenatal diagnosis by a chemical cleavage method.
    Bateman JF; Hannagan M; Chan D; Cole WG
    Biochem J; 1991 Jun; 276 ( Pt 3)(Pt 3):765-70. PubMed ID: 2064612
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Altered triple helical structure of type I procollagen in lethal perinatal osteogenesis imperfecta.
    Bonadio J; Holbrook KA; Gelinas RE; Jacob J; Byers PH
    J Biol Chem; 1985 Feb; 260(3):1734-42. PubMed ID: 2981871
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Osteogenesis imperfecta type IV: evidence of abnormal triple helical structure of type I collagen.
    Wenstrup RJ; Hunter AG; Byers PH
    Hum Genet; 1986 Sep; 74(1):47-53. PubMed ID: 3759085
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 6.