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Volumn 34, Issue 1, 2009, Pages 3-

Fuzzy interactome: the limitations of models in molecular biology

Author keywords

[No Author keywords available]

Indexed keywords

CELL COMPARTMENTALIZATION; LETTER; MOLECULAR MODEL; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

EID: 58149215982     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.10.006     Document Type: Letter
Times cited : (9)

References (10)
  • 1
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    • The 'fuzzy' interactome
    • Welch R. The 'fuzzy' interactome. Trends Biochem Sci. 34 (2009) 1-2
    • (2009) Trends Biochem Sci. , vol.34 , pp. 1-2
    • Welch, R.1
  • 2
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92 (1998) 291-294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 3
    • 0034161474 scopus 로고    scopus 로고
    • Macromolecular interactions: tracing the roots
    • Srere P.A. Macromolecular interactions: tracing the roots. Trends Biochem. Sci. 25 (2000) 150-153
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 150-153
    • Srere, P.A.1
  • 4
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    • Tompa P., and Fuxreiter M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 33 (2008) 2-8
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 5
    • 0031633365 scopus 로고    scopus 로고
    • Thousands of proteins likely to have long disordered regions
    • Romero P., et al. Thousands of proteins likely to have long disordered regions. Pac. Symp. Biocomput. 3 (1998) 437-448
    • (1998) Pac. Symp. Biocomput. , vol.3 , pp. 437-448
    • Romero, P.1
  • 6
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 7
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem. Sci. 27 (2002) 527-533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 8
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa P., et al. Structural disorder throws new light on moonlighting. Trends Biochem. Sci. 30 (2005) 484-489
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 484-489
    • Tompa, P.1
  • 9
    • 3042625942 scopus 로고    scopus 로고
    • The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA
    • Savvides S.N., et al. The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA. Protein Sci. 13 (2004) 1942-1947
    • (2004) Protein Sci. , vol.13 , pp. 1942-1947
    • Savvides, S.N.1
  • 10
    • 39549118689 scopus 로고    scopus 로고
    • Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products
    • Simon S.M., et al. Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 1152-1157
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 1152-1157
    • Simon, S.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.