메뉴 건너뛰기




Volumn 10, Issue 9, 2003, Pages 718-724

Cooperative organization in a macromolecular complex

Author keywords

[No Author keywords available]

Indexed keywords

CKS PROTEIN; CKS1 PROTEIN; CYCLIN DEPENDENT KINASE 2; FUNGAL PROTEIN; PHOSPHOPEPTIDE; PROTEIN; PROTEIN P27; RNA; RNA POLYMERASE II; S PHASE KINASE ASSOCIATED PROTEIN 2; SKP1 PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0042821546     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb962     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander, E.S. et al. Initial sequencing and analysis of the human genome. Nature 409, 860-921 (2001).
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1
  • 2
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P. et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403, 623-627 (2000).
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1
  • 3
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito, T. et al. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl. Acad. Sci. USA 98, 4569-4574 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4569-4574
    • Ito, T.1
  • 4
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin, A.C. et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141-147 (2002).
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1
  • 5
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho, Y. et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415, 180-183 (2002).
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1
  • 6
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 Å resolution
    • Cramer, P., Bushnell, D.A. & Kornberg, R.D. Structural basis of transcription: RNA polymerase II at 2.8 Å resolution. Science 292, 1863-1876 (2001).
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 7
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution
    • Gnatt, A.L., Cramer, P., Fu, J., Bushnell, D.A. & Kornberg, R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 Å resolution. Science 292, 1876-1882 (2001).
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 8
    • 0036082654 scopus 로고    scopus 로고
    • The search and its outcome: High-resolution structures of ribosomal particles from mesophilic, thermophilic, and halophilic bacteria at various functional states
    • Yonath, A. The search and its outcome: high-resolution structures of ribosomal particles from mesophilic, thermophilic, and halophilic bacteria at various functional states. Annu. Rev. Biophys. Biomol. Struct. 31, 257-273 (2002).
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 257-273
    • Yonath, A.1
  • 9
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan, V. Ribosome structure and the mechanism of translation. Cell 108, 557-572 (2002).
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 10
    • 0032529162 scopus 로고    scopus 로고
    • Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase-promoting complex at mitosis
    • Patra, D. & Dunphy, W.G. Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase-promoting complex at mitosis. Genes Dev. 12, 2549-2559 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2549-2559
    • Patra, D.1    Dunphy, W.G.2
  • 12
  • 13
    • 0035092687 scopus 로고    scopus 로고
    • The cell-cycle regulatory protein Cks1 is required for SCF(Skp2) -mediated ubiquitinylation of p27
    • Ganoth, D. et al. The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27. Nat. Cell Biol. 3, 321-324 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 321-324
    • Ganoth, D.1
  • 14
    • 0035810976 scopus 로고    scopus 로고
    • Protein destruction: Adapting roles for Cks proteins
    • Harper, J.W. Protein destruction: adapting roles for Cks proteins. Curr. Biol. 11, R431-R435 (2001).
    • (2001) Curr. Biol. , vol.11
    • Harper, J.W.1
  • 15
    • 0035067387 scopus 로고    scopus 로고
    • p27 destruction: Cks1 pulls the trigger
    • Bartek, J. & Lukas, J. p27 destruction: Cks1 pulls the trigger. Nat. Cell Biol. 3, E95-E98 (2001).
    • (2001) Nat. Cell Biol. , vol.3
    • Bartek, J.1    Lukas, J.2
  • 16
    • 0029918062 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the human Cdk2 kinase complex with cell cycle-regulatory protein CksHs1
    • Bourne, Y. et al. Crystal structure and mutational analysis of the human Cdk2 kinase complex with cell cycle-regulatory protein CksHs1. Cell 84, 863-874 (1996).
    • (1996) Cell , vol.84 , pp. 863-874
    • Bourne, Y.1
  • 17
    • 0036829681 scopus 로고    scopus 로고
    • Three different binding sites of Cks1 are required for p27-ubiquitin ligation
    • Sitry, D. et al. Three different binding sites of Cks1 are required for p27-ubiquitin ligation. J. Biol. Chem. 277, 42233-42240 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 42233-42240
    • Sitry, D.1
  • 18
    • 0037023719 scopus 로고    scopus 로고
    • suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate
    • suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate. J. Biol. Chem. 277, 12375-12381 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12375-12381
    • Odaert, B.1
  • 20
    • 0034710976 scopus 로고    scopus 로고
    • Can allosteric regulation be predicted from structure?
    • Freire, E. Can allosteric regulation be predicted from structure? Proc. Natl. Acad. Sci. USA 97, 11680-11682 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11680-11682
    • Freire, E.1
  • 21
    • 0033621118 scopus 로고    scopus 로고
    • The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme
    • Freire, E. The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozyme. Proc. Natl. Acad. Sci. USA 96, 10118-10122 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10118-10122
    • Freire, E.1
  • 22
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel, G.M., Lockless, S.W., Wall, M.A. & Ranganathan, R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat. Struct. Biol. 10, 59-69 (2003)
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 23
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless, S.W, & Ranganathan, R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286, 295-299 (1999).
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 24
    • 0037192131 scopus 로고    scopus 로고
    • Folding and association of the human cell cycle regulatory proteins CksHs1 and CksHs2
    • Seeliger, M.A., Schymkowitz, J.W., Rousseau, F., Wilkinson, H.R. & Itzhaki, L.S. Folding and association of the human cell cycle regulatory proteins CksHs1 and CksHs2. Biochemistry 41, 1202-1210 (2002).
    • (2002) Biochemistry , vol.41 , pp. 1202-1210
    • Seeliger, M.A.1    Schymkowitz, J.W.2    Rousseau, F.3    Wilkinson, H.R.4    Itzhaki, L.S.5
  • 25
    • 0036443972 scopus 로고    scopus 로고
    • The constraints protein-protein interactions place on sequence divergence
    • Teichmann, S.A. The constraints protein-protein interactions place on sequence divergence. J. Mol. Biol. 324, 399-407 (2002).
    • (2002) J. Mol. Biol. , vol.324 , pp. 399-407
    • Teichmann, S.A.1
  • 27
    • 0033605643 scopus 로고    scopus 로고
    • Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity
    • Brown, N.R. et al. Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity. J. Biol. Chem. 274, 8746-8756 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8746-8756
    • Brown, N.R.1
  • 28
    • 0034676443 scopus 로고    scopus 로고
    • Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex
    • Schulman, B.A. et al. Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature 408, 381-386 (2000).
    • (2000) Nature , vol.408 , pp. 381-386
    • Schulman, B.A.1
  • 29
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng, N. et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 416, 703-709 (2002).
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 30
    • 0037154149 scopus 로고    scopus 로고
    • A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants
    • Friedler, A. et al. A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants. Proc. Natl. Acad. Sci. USA 99, 937-942 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 937-942
    • Friedler, A.1
  • 31
    • 0029034120 scopus 로고
    • Crystal structure of the human cell cycle protein CksHs1: Single domain fold with similarity to kinase N-lobe domain
    • Arvai, A.S., Bourne, Y., Hickey, M.J. & Tainer, J.A. Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain. J. Mol. Biol. 249, 835-842 (1995).
    • (1995) J. Mol. Biol. , vol.249 , pp. 835-842
    • Arvai, A.S.1    Bourne, Y.2    Hickey, M.J.3    Tainer, J.A.4
  • 32
    • 0037414650 scopus 로고    scopus 로고
    • Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the Cks family
    • Seeliger, M.A., Breward, S.E. & Itzhaki, L.S. Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the Cks family. J. Mol. Biol. 325, 189-199 (2003).
    • (2003) J. Mol. Biol. , vol.325 , pp. 189-199
    • Seeliger, M.A.1    Breward, S.E.2    Itzhaki, L.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.