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Volumn , Issue , 2010, Pages 337-347

Loss of post-translational modification sites in disease

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS;

EID: 84873053429     PISSN: None     EISSN: None     Source Type: Conference Proceeding    
DOI: None     Document Type: Conference Paper
Times cited : (94)

References (41)
  • 2
    • 0027411585 scopus 로고
    • SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange
    • Felder, S., et al., SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol Cell Biol, 1993. 13(3): p. 1449-55.
    • (1993) Mol Cell Biol , vol.13 , Issue.3 , pp. 1449-1455
    • Felder, S.1
  • 3
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: A new partnership for signaling
    • Yang, X.J., Lysine acetylation and the bromodomain: a new partnership for signaling. Bioessays, 2004. 26(10): p. 1076-87.
    • (2004) Bioessays , vol.26 , Issue.10 , pp. 1076-1087
    • Yang, X.J.1
  • 4
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., O.N. Jensen, Proteomic analysis of post-translational modifications. Nat Biotechnol, 2003. 21(3): p. 255-61.
    • (2003) Nat Biotechnol , vol.21 , Issue.3 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 5
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning, G., et al., The protein kinase complement of the human genome. Science, 2002. 298(5600): p. 1912-34.
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1
  • 6
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander, D., et al., Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol, 2009. 10(8): p. 550-63.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.8 , pp. 550-563
    • Komander, D.1
  • 7
    • 0042510537 scopus 로고    scopus 로고
    • Systematic trans-genomic comparison of protein kinases between Arabidopsis and Saccharomyces cerevisiae
    • Wang, D., et al., Systematic trans-genomic comparison of protein kinases between Arabidopsis and Saccharomyces cerevisiae. Plant Physiol, 2003. 132(4): p. 2152-65.
    • (2003) Plant Physiol , vol.132 , Issue.4 , pp. 2152-2165
    • Wang, D.1
  • 8
    • 8844254727 scopus 로고    scopus 로고
    • Loss of glycosylation associated with the T183A mutation in human prion disease
    • Grasbon-Frodl, E., et al., Loss of glycosylation associated with the T183A mutation in human prion disease. Acta Neuropathol, 2004. 108(6): p. 476-84.
    • (2004) Acta Neuropathol , vol.108 , Issue.6 , pp. 476-484
    • Grasbon-Frodl, E.1
  • 9
    • 0025643347 scopus 로고
    • Intracellular accumulation of the cellular prion protein after mutagenesis of its Asn-linked glycosylation sites
    • Rogers, M., et al., Intracellular accumulation of the cellular prion protein after mutagenesis of its Asn-linked glycosylation sites. Glycobiology, 1990. 1(1): p. 101-9.
    • (1990) Glycobiology , vol.1 , Issue.1 , pp. 101-109
    • Rogers, M.1
  • 10
    • 1542319221 scopus 로고    scopus 로고
    • Androgen receptor acetylation site mutations cause trafficking defects, misfolding, and aggregation similar to expanded glutamine tracts
    • Thomas, M., et al., Androgen receptor acetylation site mutations cause trafficking defects, misfolding, and aggregation similar to expanded glutamine tracts. J Biol Chem, 2004. 279(9): p. 8389-95.
    • (2004) J Biol Chem , vol.279 , Issue.9 , pp. 8389-8395
    • Thomas, M.1
  • 11
    • 0035136677 scopus 로고    scopus 로고
    • An hPer2 phosphorylation site mutation in familial advanced sleep phase syndrome
    • Toh, K.L., et al., An hPer2 phosphorylation site mutation in familial advanced sleep phase syndrome. Science, 2001. 291(5506): p. 1040-3.
    • (2001) Science , vol.291 , Issue.5506 , pp. 1040-1043
    • Toh, K.L.1
  • 12
    • 0035065485 scopus 로고    scopus 로고
    • Moult, SNPs, protein structure, and disease
    • Wang, Z., J. Moult, SNPs, protein structure, and disease. Hum Mutat, 2001. 17(4): p. 263-70.
    • (2001) Hum Mutat , vol.17 , Issue.4 , pp. 263-270
    • Wang, Z.J.1
  • 13
    • 2342473198 scopus 로고    scopus 로고
    • The importance of intrinsic disorder for protein phosphorylation
    • Iakoucheva, L.M., et al., The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res, 2004. 32(3): p. 1037-1049.
    • (2004) Nucleic Acids Res , vol.32 , Issue.3 , pp. 1037-1049
    • Iakoucheva, L.M.1
  • 15
    • 70350663707 scopus 로고    scopus 로고
    • Identification, analysis and prediction of protein ubiquitination sites
    • Radivojac, P., et al., Identification, analysis and prediction of protein ubiquitination sites. Proteins, 2009.
    • (2009) Proteins
    • Radivojac, P.1
  • 16
    • 22844449795 scopus 로고    scopus 로고
    • Gains of glycosylation comprise an unexpectedly large group of pathogenic mutations
    • Vogt, G., et al., Gains of glycosylation comprise an unexpectedly large group of pathogenic mutations. Nat Genet, 2005. 37(7): p. 692-700.
    • (2005) Nat Genet , vol.37 , Issue.7 , pp. 692-700
    • Vogt, G.1
  • 17
    • 34249699069 scopus 로고    scopus 로고
    • Gain-of-glycosylation mutations
    • Vogt, G., et al., Gain-of-glycosylation mutations. Curr Opin Genet Dev, 2007. 17(3): p. 245-51.
    • (2007) Curr Opin Genet Dev , vol.17 , Issue.3 , pp. 245-251
    • Vogt, G.1
  • 18
    • 33644876212 scopus 로고    scopus 로고
    • DbPTM: An information repository of protein post-translational modification
    • Database issue
    • Lee, T.Y., et al., dbPTM: an information repository of protein post-translational modification. Nucleic Acids Res, 2006. 34(Database issue): p. D622-7.
    • (2006) Nucleic Acids Res , vol.34
    • Lee, T.Y.1
  • 19
    • 49549121853 scopus 로고    scopus 로고
    • PhosphoPOINT: A comprehensive human kinase interactome and phospho-protein database
    • Yang, C.Y., et al., PhosphoPOINT: a comprehensive human kinase interactome and phospho-protein database. Bioinformatics, 2008. 24(16): p. i14-20.
    • (2008) Bioinformatics , vol.24 , Issue.16
    • Yang, C.Y.1
  • 20
    • 49549115123 scopus 로고    scopus 로고
    • Gain and loss of phosphorylation sites in human cancer
    • Radivojac, P., et al., Gain and loss of phosphorylation sites in human cancer. Bioinformatics, 2008. 24(16): p. i241-7.
    • (2008) Bioinformatics , vol.24 , Issue.16
    • Radivojac, P.1
  • 22
    • 70350671733 scopus 로고    scopus 로고
    • Automated inference of molecular mechanisms of disease from amino acid substitutions
    • Li, B., et al., Automated inference of molecular mechanisms of disease from amino acid substitutions. Bioinformatics, 2009.
    • (2009) Bioinformatics
    • Li, B.1
  • 23
    • 13444273448 scopus 로고    scopus 로고
    • The universal protein resource (UniProt)
    • Database Issue
    • Bairoch, A., et al., The Universal Protein Resource (UniProt). Nucleic Acids Res, 2005. 33 Database Issue: p. D154-9.
    • (2005) Nucleic Acids Res , vol.33
    • Bairoch, A.1
  • 24
    • 58149193222 scopus 로고    scopus 로고
    • Human protein reference database-2009 update
    • Database issue
    • Keshava Prasad, T.S., et al., Human Protein Reference Database-2009 update. Nucleic Acids Res, 2009. 37(Database issue): p. D767-72.
    • (2009) Nucleic Acids Res , vol.37
    • Prasad, K.T.S.1
  • 25
    • 13244289881 scopus 로고    scopus 로고
    • Phospho. ELM: A database of experimentally verified phosphorylation sites in eukaryotic proteins
    • Diella, F., et al., Phospho.ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins. BMC Bioinformatics, 2004. 5(1): p. 79.
    • (2004) BMC Bioinformatics , vol.5 , Issue.1 , pp. 79
    • Diella, F.1
  • 26
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H.M., et al., The protein data bank. Nucleic Acids Res, 2000. 28(1): p. 235-242.
    • (2000) Nucleic Acids Res , vol.28 , Issue.1 , pp. 235-242
    • Berman, H.M.1
  • 27
    • 0032919585 scopus 로고    scopus 로고
    • O-GLYCBASE version 4.0: A revised database of O-glycosylated proteins
    • Gupta, R., et al., O-GLYCBASE version 4.0: a revised database of O-glycosylated proteins. Nucleic Acids Res, 1999. 27(1): p. 370-2.
    • (1999) Nucleic Acids Res , vol.27 , Issue.1 , pp. 370-372
    • Gupta, R.1
  • 28
    • 1542286168 scopus 로고    scopus 로고
    • Phosphoinositide-dependent protein kinase 1, a sensor of protein conformation
    • Biondi, R.M., Phosphoinositide-dependent protein kinase 1, a sensor of protein conformation. Trends Biochem Sci, 2004. 29(3): p. 136-42.
    • (2004) Trends Biochem Sci , vol.29 , Issue.3 , pp. 136-142
    • Biondi, R.M.1
  • 29
    • 77953446523 scopus 로고    scopus 로고
    • The human gene mutation database: 2008 update
    • Stenson, P.D., et al., The Human Gene Mutation Database: 2008 update. Genome Med, 2009. 1(1): p. 13.
    • (2009) Genome Med , vol.1 , Issue.1 , pp. 13
    • Stenson, P.D.1
  • 30
    • 70350154645 scopus 로고    scopus 로고
    • Analytical methods for inferring functional effects of single base pair substitutions in human cancers
    • Lee, W., et al., Analytical methods for inferring functional effects of single base pair substitutions in human cancers. Hum Genet, 2009.
    • (2009) Hum Genet
    • Lee, W.1
  • 31
    • 0028540405 scopus 로고
    • Use of an oriented peptide library to determine the optimal substrates of protein kinases
    • Songyang, Z., et al., Use of an oriented peptide library to determine the optimal substrates of protein kinases. Curr Biol, 1994. 4(11): p. 973-982.
    • (1994) Curr Biol , vol.4 , Issue.11 , pp. 973-982
    • Songyang, Z.1
  • 32
    • 0029639819 scopus 로고
    • Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activity
    • Oppliger, T., et al., Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activity. J Biol Chem, 1995. 270(49): p. 29498-506.
    • (1995) J Biol Chem , vol.270 , Issue.49 , pp. 29498-29506
    • Oppliger, T.1
  • 33
    • 0033615638 scopus 로고    scopus 로고
    • Serine 19 of human 6-pyruvoyltetrahydropterin synthase is phosphorylated by cGMP protein kinase II
    • Scherer-Oppliger, T., et al., Serine 19 of human 6- pyruvoyltetrahydropterin synthase is phosphorylated by cGMP protein kinase II. J Biol Chem, 1999. 274(44): p. 31341-8.
    • (1999) J Biol Chem , vol.274 , Issue.44 , pp. 31341-31348
    • Scherer-Oppliger, T.1
  • 34
    • 0028280353 scopus 로고
    • Hyperphenylalaninemia due to defects in tetrahydrobiopterin metabolism: Molecular characterization of mutations in 6-pyruvoyl-tetrahydropterin synthase
    • Thony, B., et al., Hyperphenylalaninemia due to defects in tetrahydrobiopterin metabolism: molecular characterization of mutations in 6-pyruvoyl-tetrahydropterin synthase. Am J Hum Genet, 1994. 54(5): p. 782-92.
    • (1994) Am J Hum Genet , vol.54 , Issue.5 , pp. 782-792
    • Thony, B.1
  • 35
    • 0034843597 scopus 로고    scopus 로고
    • Grishin, AL2CO: Calculation of positional conservation in a protein sequence alignment
    • Pei, J. and N.V. Grishin, AL2CO: calculation of positional conservation in a protein sequence alignment. Bioinformatics, 2001. 17(8): p. 700-12.
    • (2001) Bioinformatics , vol.17 , Issue.8 , pp. 700-712
    • Pei, J.N.V.1
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., et al., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res, 1994. 22(22): p. 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1
  • 37
    • 0028043552 scopus 로고
    • Henikoff, Position-based sequence weights
    • Henikoff, S., J.G. Henikoff, Position-based sequence weights. J Mol Biol, 1994. 243(4): p. 574-8.
    • (1994) J Mol Biol , vol.243 , Issue.4 , pp. 574-578
    • Henikoff, S.J.G.1
  • 38
    • 0035026704 scopus 로고    scopus 로고
    • Henikoff, Predicting deleterious amino acid substitutions
    • Ng, P.C., S. Henikoff, Predicting deleterious amino acid substitutions. Genome Res, 2001. 11(5): p. 863-74.
    • (2001) Genome Res , vol.11 , Issue.5 , pp. 863-874
    • Ng, P.C.S.1
  • 39
    • 3142665525 scopus 로고    scopus 로고
    • Speed, GOstat: Find statistically overrepresented Gene Ontologies within a group of genes
    • Beissbarth, T. and T.P. Speed, GOstat: find statistically overrepresented Gene Ontologies within a group of genes. Bioinformatics, 2004. 20(9): p. 1464-5.
    • (2004) Bioinformatics , vol.20 , Issue.9 , pp. 1464-1465
    • Beissbarth, T.T.P.1
  • 40
    • 42949160024 scopus 로고    scopus 로고
    • From protein-disease associations to disease informatics
    • Dalkilic, M.M., et al., From protein-disease associations to disease informatics. Front Biosci, 2008. 13: p. 3391-407.
    • (2008) Front Biosci , vol.13 , pp. 3391-3407
    • Dalkilic, M.M.1
  • 41
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology. The gene ontology consortium
    • Ashburner, M., et al., Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat Genet, 2000. 25(1): p. 25-29.
    • (2000) Nat Genet , vol.25 , Issue.1 , pp. 25-29
    • Ashburner, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.