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Volumn 43, Issue 18, 2004, Pages 5314-5323

Severity of Osteogenesis Imperfecta and Structure of a Collagen-like Peptide Modeling a Lethal Mutation Site

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; COMPUTER SIMULATION; HYDROGEN BONDS; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE;

EID: 2442492118     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035676w     Document Type: Article
Times cited : (31)

References (29)
  • 5
    • 0030978854 scopus 로고    scopus 로고
    • Amino acid sequence environment modulates the disruption by osteogenesis imperfecta glycine substitutions in collagen-like peptides
    • Yang, W., Battineni, M. L., and Brodsky, B. (1997) Amino acid sequence environment modulates the disruption by osteogenesis imperfecta glycine substitutions in collagen-like peptides, Biochemistry 36, 6930-6935.
    • (1997) Biochemistry , vol.36 , pp. 6930-6935
    • Yang, W.1    Battineni, M.L.2    Brodsky, B.3
  • 6
    • 0032480755 scopus 로고    scopus 로고
    • Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease
    • Liu, X., Kim, S., Dai, Q. H., Brodsky, B., and Baum, J. (1998) Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease, Biochemistry 37, 15528-15533.
    • (1998) Biochemistry , vol.37 , pp. 15528-15533
    • Liu, X.1    Kim, S.2    Dai, Q.H.3    Brodsky, B.4    Baum, J.5
  • 7
    • 0037150135 scopus 로고    scopus 로고
    • Folding and conformational consequences of glycine to alanine replacements at different positions in a collagen model peptide
    • Bhate, M., Wang, X., Baum, J., and Brodsky, B. (2002) Folding and conformational consequences of glycine to alanine replacements at different positions in a collagen model peptide, Biochemistry 41, 6539-6547.
    • (2002) Biochemistry , vol.41 , pp. 6539-6547
    • Bhate, M.1    Wang, X.2    Baum, J.3    Brodsky, B.4
  • 8
    • 2342518375 scopus 로고    scopus 로고
    • Structural Models of Osteogenesis Imperfecta-associated Variants in the COL1A1 Gene
    • Mooney, S. D., and Klein, T. E. (2002) Structural Models of Osteogenesis Imperfecta-associated Variants in the COL1A1 Gene, Mol. Cell. Proteomics 1, 868-875.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 868-875
    • Mooney, S.D.1    Klein, T.E.2
  • 9
    • 0141833160 scopus 로고    scopus 로고
    • The functional importance of disease-associated mutation
    • Mooney, S. D., and Klein, T. E. (2002) The functional importance of disease-associated mutation, BMC Bioinf. 3, 24.
    • (2002) BMC Bioinf. , vol.3 , pp. 24
    • Mooney, S.D.1    Klein, T.E.2
  • 10
    • 0037025113 scopus 로고    scopus 로고
    • Conformational preferences of substituted prolines in the collagen triple helix
    • Mooney, S. D., Kollman, P. A., and Klein, T. E. (2002) Conformational preferences of substituted prolines in the collagen triple helix, Biopolymers 64, 63-71.
    • (2002) Biopolymers , vol.64 , pp. 63-71
    • Mooney, S.D.1    Kollman, P.A.2    Klein, T.E.3
  • 11
    • 0028904399 scopus 로고
    • Structure of the type I collagen molecule based on conformational energy computations: The triple-stranded helix and the N-terminal telopeptide
    • Vitagliano, L., Nemethy, G., Zagari, A., and Scheraga, H. A. (1995) Structure of the type I collagen molecule based on conformational energy computations: the triple-stranded helix and the N-terminal telopeptide, J. Mol. Biol. 247, 69-80.
    • (1995) J. Mol. Biol. , vol.247 , pp. 69-80
    • Vitagliano, L.1    Nemethy, G.2    Zagari, A.3    Scheraga, H.A.4
  • 12
    • 0027219734 scopus 로고
    • Stabilization of the triple-helical structure of natural collagen by side-chain interactions
    • Vitagliano, L., Nemethy, G., Zagari, A., and Scheraga, H. A. (1993) Stabilization of the triple-helical structure of natural collagen by side-chain interactions, Biochemistry 32, 7354-7359.
    • (1993) Biochemistry , vol.32 , pp. 7354-7359
    • Vitagliano, L.1    Nemethy, G.2    Zagari, A.3    Scheraga, H.A.4
  • 13
    • 0036300984 scopus 로고    scopus 로고
    • Localized unfolding of collagen explains collagenase cleavage near imino-poor sites
    • Stultz, C. M. (2002) Localized unfolding of collagen explains collagenase cleavage near imino-poor sites, J. Mol. Biol. 319, 997-1003.
    • (2002) J. Mol. Biol. , vol.319 , pp. 997-1003
    • Stultz, C.M.1
  • 16
    • 0037110472 scopus 로고    scopus 로고
    • Effective Born radii in the generalized Born approximation: The importance of being perfect
    • Onufriev, A., Case, D. A., and Bashford, D. (2002) Effective Born radii in the generalized Born approximation: the importance of being perfect, J. Comput. Chem. 23, 1297-1304.
    • (2002) J. Comput. Chem. , vol.23 , pp. 1297-1304
    • Onufriev, A.1    Case, D.A.2    Bashford, D.3
  • 17
    • 20644449471 scopus 로고    scopus 로고
    • Modification of the Generalized Born Model Suitable for Macromolecules
    • Onufriev, A., Bashford, D., and Case, D. A. (2000) Modification of the Generalized Born Model Suitable for Macromolecules, J. Phys. Chem. B 104, 3712-3720.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3712-3720
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 18
    • 0031626860 scopus 로고    scopus 로고
    • The object technology framework: An object-oriented interface to molecular data and its application to collagen
    • Huang, C. C., Couch, G. S., Pettersen, E. F., Ferrin, T. E., Howard, A. E., and Klein, T. E. (1998) The object technology framework: an object-oriented interface to molecular data and its application to collagen, Pac. Symp. Biocomput. '98, 349-361.
    • (1998) Pac. Symp. Biocomput. '98 , pp. 349-361
    • Huang, C.C.1    Couch, G.S.2    Pettersen, E.F.3    Ferrin, T.E.4    Howard, A.E.5    Klein, T.E.6
  • 19
    • 0036007873 scopus 로고    scopus 로고
    • Insights on the conformational stability of collagen
    • Jenkins, C. L., and Raines, R. T. (2002) Insights on the conformational stability of collagen, Nat. Prod. Rep. 19, 49-59.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 49-59
    • Jenkins, C.L.1    Raines, R.T.2
  • 20
    • 0036298978 scopus 로고    scopus 로고
    • Peptide investigations of pairwise interactions in the collagen triple-helix
    • Persikov, A. V., Ramshaw, J. A., Kirkpatrick, A., and Brodsky, B. (2002) Peptide investigations of pairwise interactions in the collagen triple-helix, J. Mol. Biol. 316, 385-394.
    • (2002) J. Mol. Biol. , vol.316 , pp. 385-394
    • Persikov, A.V.1    Ramshaw, J.A.2    Kirkpatrick, A.3    Brodsky, B.4
  • 21
    • 0034442555 scopus 로고    scopus 로고
    • Collagen model peptides: Sequence dependence of triple-helix stability
    • Persikov, A. V., Ramshaw, J. A., and Brodsky, B. (2000) Collagen model peptides: Sequence dependence of triple-helix stability, Biopolymers 55, 436-450.
    • (2000) Biopolymers , vol.55 , pp. 436-450
    • Persikov, A.V.1    Ramshaw, J.A.2    Brodsky, B.3
  • 22
  • 24
    • 0035800664 scopus 로고    scopus 로고
    • The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence
    • Kramer, R. Z., Bella, J., Brodsky, B., and Berman, H. M. (2001) The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence, J. Mol. Biol. 311, 131-147.
    • (2001) J. Mol. Biol. , vol.311 , pp. 131-147
    • Kramer, R.Z.1    Bella, J.2    Brodsky, B.3    Berman, H.M.4
  • 25
    • 0036838777 scopus 로고    scopus 로고
    • A statistically derived parametrization for the collagen triple-helix
    • Rainey, J. K., and Goh, M. C. (2002) A statistically derived parametrization for the collagen triple-helix, Protein Sci. 11, 2748-2754.
    • (2002) Protein Sci. , vol.11 , pp. 2748-2754
    • Rainey, J.K.1    Goh, M.C.2
  • 26
    • 0031831307 scopus 로고    scopus 로고
    • The Human Collagen Mutation Database 1998
    • Dalgleish, R. (1998) The Human Collagen Mutation Database 1998, Nucleic Acids Res. 26, 253-255.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 253-255
    • Dalgleish, R.1
  • 27
    • 0030789557 scopus 로고    scopus 로고
    • The human type I collagen mutation database
    • Dalgleish, R. (1997) The human type I collagen mutation database, Nucleic Acids Res. 25, 181-187.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 181-187
    • Dalgleish, R.1
  • 29
    • 0037155282 scopus 로고    scopus 로고
    • Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47
    • Koide, T., Takahara, Y., Asada, S., and Nagata, K. (2002) Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47, J. Biol. Chem. 277, 6178-6182.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6178-6182
    • Koide, T.1    Takahara, Y.2    Asada, S.3    Nagata, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.