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Volumn 25, Issue 5, 2009, Pages 193-197

Weak functional constraints on phosphoproteomes

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOME;

EID: 65349155149     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2009.03.003     Document Type: Short Survey
Times cited : (243)

References (23)
  • 1
    • 54549123613 scopus 로고    scopus 로고
    • Comparative phosphoproteomics reveals evolutionary and functional conservation of phosphorylation across eukaryotes
    • Boekhorst J., et al. Comparative phosphoproteomics reveals evolutionary and functional conservation of phosphorylation across eukaryotes. Genome Biol. 9 (2008) R144
    • (2008) Genome Biol. , vol.9
    • Boekhorst, J.1
  • 2
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites
    • Gnad F., et al. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol. 8 (2007) R250
    • (2007) Genome Biol. , vol.8
    • Gnad, F.1
  • 3
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax J.A., and Ferrell Jr. J.E. Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 8 (2007) 530-541
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell Jr., J.E.2
  • 4
    • 48149087568 scopus 로고    scopus 로고
    • Non-functional phosphorylations?
    • Lienhard G.E. Non-functional phosphorylations?. Trends Biochem. Sci. 33 (2008) 351-352
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 351-352
    • Lienhard, G.E.1
  • 5
    • 45449101679 scopus 로고    scopus 로고
    • Comparative conservation analysis of the human mitotic phosphoproteome
    • Malik R., et al. Comparative conservation analysis of the human mitotic phosphoproteome. Bioinformatics 24 (2008) 1426-1432
    • (2008) Bioinformatics , vol.24 , pp. 1426-1432
    • Malik, R.1
  • 6
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4: phylogenetic analysis by maximum likelihood
    • Yang Z. PAML 4: phylogenetic analysis by maximum likelihood. Mol. Biol. Evol 24 (2007) 1586-1591
    • (2007) Mol. Biol. Evol , vol.24 , pp. 1586-1591
    • Yang, Z.1
  • 7
    • 4143051195 scopus 로고    scopus 로고
    • Comparison of site-specific rate-inference methods for protein sequences: empirical Bayesian methods are superior
    • Mayrose I., et al. Comparison of site-specific rate-inference methods for protein sequences: empirical Bayesian methods are superior. Mol. Biol. Evol. 21 (2004) 1781-1791
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1781-1791
    • Mayrose, I.1
  • 8
    • 47849089500 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder
    • Collins M.O., et al. Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder. Mol. Cell. Proteomics 7 (2008) 1331-1348
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1331-1348
    • Collins, M.O.1
  • 9
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database
    • Nuhse T.S., et al. Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 16 (2004) 2394-2405
    • (2004) Plant Cell , vol.16 , pp. 2394-2405
    • Nuhse, T.S.1
  • 10
    • 0036017388 scopus 로고    scopus 로고
    • Evolutionary rate heterogeneity in proteins with long disordered regions
    • Brown C.J., et al. Evolutionary rate heterogeneity in proteins with long disordered regions. J. Mol. Evol. 55 (2002) 104-110
    • (2002) J. Mol. Evol. , vol.55 , pp. 104-110
    • Brown, C.J.1
  • 11
    • 50849102293 scopus 로고    scopus 로고
    • A catalog of neutral and deleterious polymorphism in yeast
    • Doniger S.W., et al. A catalog of neutral and deleterious polymorphism in yeast. PLoS Genet. 4 (2008) e1000183
    • (2008) PLoS Genet. , vol.4
    • Doniger, S.W.1
  • 12
    • 55749111058 scopus 로고    scopus 로고
    • Linear motif atlas for phosphorylation-dependent signaling
    • Miller M.L., et al. Linear motif atlas for phosphorylation-dependent signaling. Sci. Signal. 1 (2008) ra2
    • (2008) Sci. Signal. , vol.1
    • Miller, M.L.1
  • 13
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 579 (2005) 3346-3354
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 14
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: from transcript synthesis to protein degradation
    • Gsponer J., et al. Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 322 (2008) 1365-1368
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1
  • 15
    • 65349149138 scopus 로고    scopus 로고
    • How perfect can protein interactomes be?
    • Levy E.D., et al. How perfect can protein interactomes be?. Sci. Signal. 2 (2009) pe11
    • (2009) Sci. Signal. , vol.2
    • Levy, E.D.1
  • 16
    • 33846671062 scopus 로고    scopus 로고
    • Tuning bulk electrostatics to regulate protein function
    • Serber Z., and Ferrell Jr. J.E. Tuning bulk electrostatics to regulate protein function. Cell 128 (2007) 441-444
    • (2007) Cell , vol.128 , pp. 441-444
    • Serber, Z.1    Ferrell Jr., J.E.2
  • 17
    • 0036806311 scopus 로고    scopus 로고
    • Evolution of protein kinase signaling from yeast to man
    • Manning G., et al. Evolution of protein kinase signaling from yeast to man. Trends Biochem. Sci. 27 (2002) 514-520
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 514-520
    • Manning, G.1
  • 18
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation-a 25 year update
    • Cohen P. The regulation of protein function by multisite phosphorylation-a 25 year update. Trends Biochem. Sci. 25 (2000) 596-601
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 596-601
    • Cohen, P.1
  • 19
    • 48249142418 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations
    • Wenta N., et al. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 9238-9243
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 9238-9243
    • Wenta, N.1
  • 20
    • 0030070466 scopus 로고    scopus 로고
    • Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex
    • O'Neill E.M., et al. Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex. Science 271 (1996) 209-212
    • (1996) Science , vol.271 , pp. 209-212
    • O'Neill, E.M.1
  • 21
    • 26244442243 scopus 로고    scopus 로고
    • Protein phosphatases in MAPK signalling: we keep learning from yeast
    • Martin H., et al. Protein phosphatases in MAPK signalling: we keep learning from yeast. Mol. Microbiol. 58 (2005) 6-16
    • (2005) Mol. Microbiol. , vol.58 , pp. 6-16
    • Martin, H.1
  • 22
    • 0026721953 scopus 로고
    • The two forms of bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase result from alternative splicing
    • Rider M.H., et al. The two forms of bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase result from alternative splicing. Biochem. J 285 (1992) 405-411
    • (1992) Biochem. J , vol.285 , pp. 405-411
    • Rider, M.H.1
  • 23
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller B., et al. Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat. Methods 4 (2007) 231-237
    • (2007) Nat. Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.