메뉴 건너뛰기




Volumn 23, Issue 5, 2004, Pages 464-470

The Swiss-Prot Variant Page and the ModSNP Database: A Resource for Sequence and Structure Information on Human Protein Variants

Author keywords

Homology modeling; Human protein variant; ModSNP database; Single amino acid polymorphism; Swiss Prot; Three dimensional structure

Indexed keywords

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; HUMAN; INFORMATION PROCESSING; INFORMATION RETRIEVAL; INTERNET; MISSENSE MUTATION; MOLECULAR MODEL; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DATABASE; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN VARIANT; REVIEW; SEQUENCE ANALYSIS; SEQUENCE DATABASE; SEQUENCE HOMOLOGY; SINGLE NUCLEOTIDE POLYMORPHISM; STRUCTURE ANALYSIS; SWISS-PROT;

EID: 2342596530     PISSN: 10597794     EISSN: None     Source Type: Journal    
DOI: 10.1002/humu.20021     Document Type: Review
Times cited : (123)

References (32)
  • 1
    • 2342603156 scopus 로고    scopus 로고
    • Mutations in human genetic disease
    • Cooper DN, editor. London: Nature Publishing Group
    • Antonarakis SE, Cooper DN. 2003. Mutations in human genetic disease. In: Cooper DN, editor. Encyclopedia of the human genome. London: Nature Publishing Group. p 227-253.
    • (2003) Encyclopedia of the Human Genome , pp. 227-253
    • Antonarakis, S.E.1    Cooper, D.N.2
  • 2
    • 0035812694 scopus 로고    scopus 로고
    • Protein structure prediction and structural genomics
    • Baker D, Sali A. 2001. Protein structure prediction and structural genomics. Science 294:93-96.
    • (2001) Science , vol.294 , pp. 93-96
    • Baker, D.1    Sali, A.2
  • 5
    • 0035937259 scopus 로고    scopus 로고
    • Predicting the functional consequences of non-synonymous single nucleotide polymorphisms: Structure-based assessment of amino acid variation
    • Chasman D, Adams RM. 2001. Predicting the functional consequences of non-synonymous single nucleotide polymorphisms: structure-based assessment of amino acid variation. J Mol Biol 307:683-706.
    • (2001) J Mol Biol , vol.307 , pp. 683-706
    • Chasman, D.1    Adams, R.M.2
  • 6
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C, Lesk AM. 1986. The relation between the divergence of sequence and structure in proteins. EMBO J 5:823-826.
    • (1986) EMBO J , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 7
    • 0037317334 scopus 로고    scopus 로고
    • Protein folding and disease: A view from the first Horizon Symposium
    • Dobson CM. 2003. Protein folding and disease: a view from the first Horizon Symposium. Nat Rev Drug Discov 2:154-160.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 154-160
    • Dobson, C.M.1
  • 8
    • 0032711431 scopus 로고    scopus 로고
    • The structural basis of phenylketonuria
    • Erlandsen H, Stevens RC. 1999. The structural basis of phenylketonuria. Mol Genet Metab 68:103-125.
    • (1999) Mol Genet Metab , vol.68 , pp. 103-125
    • Erlandsen, H.1    Stevens, R.C.2
  • 9
    • 0036300807 scopus 로고    scopus 로고
    • Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties
    • Ferrer-Costa C, Orozco M, de la Cruz X. 2002. Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties. J Mol Biol 315:771-786.
    • (2002) J Mol Biol , vol.315 , pp. 771-786
    • Ferrer-Costa, C.1    Orozco, M.2    De La Cruz, X.3
  • 10
    • 0036081484 scopus 로고    scopus 로고
    • HGVbase: A human sequence variation database emphasizing data quality and a broad spectrum of data sources
    • Fredman D, Siegfried M, Yuan YP, Bork P, Lehvaslaiho H, Brookes AJ. 2002. HGVbase: a human sequence variation database emphasizing data quality and a broad spectrum of data sources. Nucleic Acids Res 30:387-391.
    • (2002) Nucleic Acids Res , vol.30 , pp. 387-391
    • Fredman, D.1    Siegfried, M.2    Yuan, Y.P.3    Bork, P.4    Lehvaslaiho, H.5    Brookes, A.J.6
  • 12
    • 0019028066 scopus 로고
    • Model for haptoglobin heavy chain based upon structural homology
    • Greer J. 1980. Model for haptoglobin heavy chain based upon structural homology. Proc Natl Acad Sci USA 77:3393-3397.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 3393-3397
    • Greer, J.1
  • 13
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 15
    • 0038820376 scopus 로고    scopus 로고
    • AstexViewer: A visualisation aid for structure-based drug design
    • Hartshorn MJ. 2002. AstexViewer: a visualisation aid for structure-based drug design. J Comput Aided Mol Des 16:871-881.
    • (2002) J Comput Aided Mol Des , vol.16 , pp. 871-881
    • Hartshorn, M.J.1
  • 16
  • 22
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC. 2003. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31:3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 24
    • 0034671945 scopus 로고    scopus 로고
    • Oncogenic mutations of the p53 tumor suppressor: The demons of the guardian of the genome
    • Sigal A, Rotter V. 2000. Oncogenic mutations of the p53 tumor suppressor: the demons of the guardian of the genome. Cancer Res 60:6788-6793.
    • (2000) Cancer Res , vol.60 , pp. 6788-6793
    • Sigal, A.1    Rotter, V.2
  • 27
    • 0036321534 scopus 로고    scopus 로고
    • Assessing the relative importance of the biophysical properties of amino acid substitutions associated with human genetic disease
    • Terp BN, Cooper DN, Christensen IT, Jorgensen FS, Bross P, Gregersen N, Krawczak M. 2002. Assessing the relative importance of the biophysical properties of amino acid substitutions associated with human genetic disease. Hum Mutat 20:98-109.
    • (2002) Hum Mutat , vol.20 , pp. 98-109
    • Terp, B.N.1    Cooper, D.N.2    Christensen, I.T.3    Jorgensen, F.S.4    Bross, P.5    Gregersen, N.6    Krawczak, M.7
  • 28
    • 0031564640 scopus 로고    scopus 로고
    • PDB-based protein loop prediction: Parameters for selection and methods for optimization
    • van Vlijmen HW, Karplus M. 1997. PDB-based protein loop prediction: parameters for selection and methods for optimization. J Mol Biol 267:975-1001.
    • (1997) J Mol Biol , vol.267 , pp. 975-1001
    • Van Vlijmen, H.W.1    Karplus, M.2
  • 29
    • 0035748996 scopus 로고    scopus 로고
    • Comparison of performance in successive CASP experiments
    • Venclovas C, Zemla A, Fidelis K, Moult J. 2001. Comparison of performance in successive CASP experiments. Proteins Suppl 5:163-170.
    • (2001) Proteins Suppl , vol.5 , pp. 163-170
    • Venclovas, C.1    Zemla, A.2    Fidelis, K.3    Moult, J.4
  • 30
    • 0035065485 scopus 로고    scopus 로고
    • SNPs, protein structure, and disease
    • Wang Z, Moult J. 2001. SNPs, protein structure, and disease. Hum Mutat 17:263-70.
    • (2001) Hum Mutat , vol.17 , pp. 263-270
    • Wang, Z.1    Moult, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.