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Volumn 8, Issue 3, 2011, Pages

Caught in self-interaction: Evolutionary and functional mechanisms of protein homooligomerization

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EID: 79956188298     PISSN: 14783967     EISSN: 14783975     Source Type: Journal    
DOI: 10.1088/1478-3975/8/3/035007     Document Type: Article
Times cited : (86)

References (89)
  • 1
    • 0015239530 scopus 로고
    • The quaternary structure of proteins composed of identical subunits
    • Cornish-Bowden A J and Koshland DE Jr 1971 The quaternary structure of proteins composed of identical subunits J. Biol. Chem. 246 3092-102
    • (1971) J. Biol. Chem. , vol.246 , pp. 3092-3102
    • Cornish-Bowden, A.J.1    Koshland Jr., D.E.2
  • 3
    • 22944475303 scopus 로고    scopus 로고
    • Protein oligomerization: How and why
    • DOI 10.1016/j.bmc.2005.05.037, PII S0968089605004748
    • Ali M H and Imperiali B 2005 Protein oligomerization: how and why Bioorg. Med. Chem. 13 5013-20 (Pubitemid 41043188)
    • (2005) Bioorganic and Medicinal Chemistry , vol.13 , Issue.17 , pp. 5013-5020
    • Ali, M.H.1    Imperiali, B.2
  • 6
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones S and Thornton J M 1995 Protein-protein interactions: a review of protein dimer structures Prog. Biophys. Mol. Biol. 63 31-65
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , Issue.1 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 7
    • 0345863907 scopus 로고    scopus 로고
    • BRENDA, the enzyme database: Updates and major new developments
    • Schomburg I et al 2004 BRENDA, the enzyme database: updates and major new developments Nucleic Acids Res. 32 D431-3
    • (2004) Nucleic Acids Res. , vol.32
    • Schomburg, I.1
  • 8
    • 21244464335 scopus 로고    scopus 로고
    • Binding properties and evolution of homodimers in protein-protein interaction networks
    • DOI 10.1093/nar/gki678
    • Ispolatov I, Yuryev A, Mazo I and Maslov S 2005 Binding properties and evolution of homodimers in protein-protein interaction networks Nucleic Acids Res. 33 3629-35 (Pubitemid 41430585)
    • (2005) Nucleic Acids Research , vol.33 , Issue.11 , pp. 3629-3635
    • Ispolatov, I.1    Yuryev, A.2    Mazo, I.3    Maslov, S.4
  • 9
    • 0141815677 scopus 로고    scopus 로고
    • The dimeric versus monomeric status of 14-3-3ζ is controlled by phosphorylation of Ser58 at the dimer interface
    • DOI 10.1074/jbc.M304689200
    • Woodcock J M, Murphy J, Stomski F C, Berndt M C and Lopez A F 2003 The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface J. Biol. Chem. 278 36323-7 (Pubitemid 37139958)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 36323-36327
    • Woodcock, J.M.1    Murphy, J.2    Stomski, F.C.3    Berndt, M.C.4    Lopez, A.F.5
  • 10
    • 23044500915 scopus 로고    scopus 로고
    • Pyruvate kinase type M2 and its role in tumor growth and spreading
    • DOI 10.1016/j.semcancer.2005.04.009, PII S1044579X0500026X, Tumor Metabolome
    • Mazurek S, Boschek C B, Hugo F and Eigenbrodt E 2005 Pyruvate kinase type M2 and its role in tumor growth and spreading Semin. Cancer Biol. 15 300-8 (Pubitemid 41058775)
    • (2005) Seminars in Cancer Biology , vol.15 , Issue.4 , pp. 300-308
    • Mazurek, S.1    Boschek, C.B.2    Hugo, F.3    Eigenbrodt, E.4
  • 11
    • 70349452284 scopus 로고    scopus 로고
    • Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold
    • Koike R, Kidera A and Ota M 2009 Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold Protein Sci. 18 2060-6
    • (2009) Protein Sci. , vol.18 , pp. 2060-2066
    • Koike, R.1    Kidera, A.2    Ota, M.3
  • 12
    • 17644370061 scopus 로고    scopus 로고
    • Leucine zipper-mediated homo-oligomerization regulates the Rho-GEF activity of AKAP-Lbc
    • DOI 10.1074/jbc.M414440200
    • Baisamy L, Jurisch N and Diviani D 2005 Leucine zipper-mediated homooligomerization regulates the Rho-GEF activity of AKAP-Lbc J. Biol. Chem. 280 15405-12 (Pubitemid 40562898)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15405-15412
    • Baisamy, L.1    Jurisch, N.2    Diviani, D.3
  • 14
    • 0037422171 scopus 로고    scopus 로고
    • C/EBP family transcription factors are degraded by the proteasome but stabilized by forming dimer
    • DOI 10.1038/sj.onc.1206204
    • Hattori T, Ohoka N, Inoue Y, Hayashi H and Onozaki K 2003 C/EBP family transcription factors are degraded by the proteasome but stabilized by forming dimer Oncogene 22 1273-80 (Pubitemid 36384589)
    • (2003) Oncogene , vol.22 , Issue.9 , pp. 1273-1280
    • Hattori, T.1    Ohoka, N.2    Inoue, Y.3    Hayashi, H.4    Onozaki, K.5
  • 15
    • 67650886055 scopus 로고    scopus 로고
    • Linking molecular affinity and cellular specificity in cadherin-mediated adhesion
    • Katsamba P et al 2009 Linking molecular affinity and cellular specificity in cadherin-mediated adhesion Proc. Natl Acad. Sci. USA 106 11594-9
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 11594-11599
    • Katsamba, P.1
  • 16
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • DOI 10.1126/science.1108595
    • Changeux J P and Edelstein S J 2005 Allosteric mechanisms of signal transduction Science 308 1424-8 (Pubitemid 40791288)
    • (2005) Science , vol.308 , Issue.5727 , pp. 1424-1428
    • Changeux, J.-P.1    Edelstein, S.J.2
  • 17
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • DOI 10.1038/328834a0
    • Miller S, Lesk A M, Janin J and Chothia C 1987 The accessible surface area and stability of oligomeric proteins Nature 328 834-6 (Pubitemid 17125965)
    • (1987) Nature , vol.328 , Issue.6133 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 18
    • 33846427758 scopus 로고    scopus 로고
    • So how do you know you have a macromolecular complex?
    • Dafforn T R 2007 So how do you know you have a macromolecular complex? Acta Crystallogr. D Biol. Crystallogr. 63 17-25
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 17-25
    • Dafforn, T.R.1
  • 19
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • DOI 10.1016/S0968-0004(98)01253-5, PII S0968000498012535
    • Henrick K and Thornton J M 1998 PQS: a protein quaternary structure file server Trends Biochem. Sci. 23 358-61 (Pubitemid 28461869)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.9 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 20
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E and Henrick K 2007 Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 774-97 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 22
    • 35748959334 scopus 로고    scopus 로고
    • PiQSi: Protein Quaternary Structure Investigation
    • DOI 10.1016/j.str.2007.09.019, PII S0969212607003760
    • Levy E D 2007 PiQSi: protein quaternary structure investigation Structure 15 1364-7 (Pubitemid 350051933)
    • (2007) Structure , vol.15 , Issue.11 , pp. 1364-1367
    • Levy, E.D.1
  • 23
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • DOI 10.1002/1097-0134(20001001)41:1<47::AID-PROT80>3.0.CO;2-8
    • Ponstingl H, Henrick K and Thornton J M 2000 Discriminating between homodimeric and monomeric proteins in the crystalline state Proteins 41 47-57 (Pubitemid 30666912)
    • (2000) Proteins: Structure, Function and Genetics , vol.41 , Issue.1 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 26
    • 0030877077 scopus 로고    scopus 로고
    • Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers
    • DOI 10.1002/(SICI)1097-0134(199708)28:4<494::AID-PROT4>3.0.CO;2-A
    • Dasgupta S, Iyer G H, Bryant S H, Lawrence C E and Bell J A 1997 Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers Proteins 28 494-514 (Pubitemid 27328566)
    • (1997) Proteins: Structure, Function and Genetics , vol.28 , Issue.4 , pp. 494-514
    • Dasgupta, S.1    Iyer, G.H.2    Bryant, S.H.3    Lawrence, C.E.4    Bell, J.A.5
  • 27
    • 26844500695 scopus 로고    scopus 로고
    • Interresidue contacts in proteins and protein-protein interfaces and their use in characterizing the homodimeric interface
    • DOI 10.1021/pr050118k
    • Saha R P, Bahadur R P and Chakrabarti P 2005 Interresidue contacts in proteins and protein-protein interfaces and their use in characterizing the homodimeric interface J. Proteome Res. 4 1600-9 (Pubitemid 41464786)
    • (2005) Journal of Proteome Research , vol.4 , Issue.5 , pp. 1600-1609
    • Saha, R.P.1    Bahadur, R.P.2    Chakrabarti, P.3
  • 28
    • 31344459575 scopus 로고    scopus 로고
    • Finding biologically relevant protein domain interactions: Conserved binding mode analysis
    • DOI 10.1110/ps.051760806
    • Shoemaker B A, Panchenko A R and Bryant S H 2006 Finding biologically relevant protein domain interactions: conserved binding mode analysis Protein Sci. 15 352-61 (Pubitemid 43145007)
    • (2006) Protein Science , vol.15 , Issue.2 , pp. 352-361
    • Shoemaker, B.A.1    Panchenko, A.R.2    Bryant, S.H.3
  • 29
    • 78651306870 scopus 로고    scopus 로고
    • The protein common interface database (ProtCID)-a comprehensive database of interactions of homologous proteins in multiple crystal forms
    • Xu Q and Dunbrack R L Jr 2011 The protein common interface database (ProtCID)-a comprehensive database of interactions of homologous proteins in multiple crystal forms Nucleic Acids Res. 39 D761-70
    • (2011) Nucleic Acids Res. , vol.39
    • Xu, Q.1    Dunbrack, R.L.2
  • 30
    • 20844454090 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions by combining structure and sequence conservation in protein interfaces
    • DOI 10.1093/bioinformatics/bti443
    • Aytuna A S, Gursoy A and Keskin O 2005 Prediction of protein-protein interactions by combining structure and sequence conservation in protein interfaces Bioinformatics 21 2850-5 (Pubitemid 40862283)
    • (2005) Bioinformatics , vol.21 , Issue.12 , pp. 2850-2855
    • Selim Aytuna, S.1    Gursoy, A.2    Keskin, O.3
  • 32
    • 75549083885 scopus 로고    scopus 로고
    • Inferred Biomolecular Interaction Server-a web server to analyze and predict protein interacting partners and binding sites
    • Shoemaker B A et al 2009 Inferred Biomolecular Interaction Server-a web server to analyze and predict protein interacting partners and binding sites Nucleic Acids Res. 38 D518-24
    • (2009) Nucleic Acids Res. , vol.38
    • Shoemaker, B.A.1
  • 33
    • 51649094321 scopus 로고    scopus 로고
    • Built-in loops allow versatility in domain-domain interactions: Lessons from self-interacting domains
    • Akiva E, Itzhaki Z and Margalit H 2008 Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains Proc. Natl Acad. Sci. USA 105 13292-7
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 13292-13297
    • Akiva, E.1    Itzhaki, Z.2    Margalit, H.3
  • 34
    • 78650537920 scopus 로고    scopus 로고
    • Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states
    • Hashimoto K and Panchenko A R 2010 Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states Proc. Natl Acad. Sci. USA 107 20352-7
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 20352-20357
    • Hashimoto, K.1    Panchenko, A.R.2
  • 35
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • DOI 10.1016/S0022-2836(02)01223-8
    • Ofran Y and Rost B 2003 Analysing six types of protein-protein interfaces J. Mol. Biol. 325 377-87 (Pubitemid 36062695)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.2 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 37
    • 34248532098 scopus 로고    scopus 로고
    • Comprehensive statistical analysis of residues interaction specificity at protein-protein interfaces
    • DOI 10.1002/prot.21363
    • Anashkina A, Kuznetsov E, Esipova N and Tumanyan V 2007 Comprehensive statistical analysis of residues interaction specificity at protein-protein interfaces Proteins 67 1060-77 (Pubitemid 46753951)
    • (2007) Proteins: Structure, Function and Genetics , vol.67 , Issue.4 , pp. 1060-1077
    • Anashkina, A.1    Kuznetsov, E.2    Esipova, N.3    Tumanyan, V.4
  • 38
    • 36549009679 scopus 로고    scopus 로고
    • Optimization of electrostatic interactions in protein-protein complexes
    • DOI 10.1529/biophysj.107.112367
    • Brock K, Talley K, Coley K, Kundrotas P and Alexov E 2007 Optimization of electrostatic interactions in protein-protein complexes Biophys. J. 93 3340-52 (Pubitemid 350190799)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3340-3352
    • Brock, K.1    Talley, K.2    Coley, K.3    Kundrotas, P.4    Alexov, E.5
  • 39
    • 77950867698 scopus 로고    scopus 로고
    • The subunit interfaces of weakly associated homodimeric proteins
    • Dey S, Pal A, Chakrabarti P and Janin J 2010 The subunit interfaces of weakly associated homodimeric proteins J. Mol. Biol. 398 146-60
    • (2010) J. Mol. Biol. , vol.398 , pp. 146-160
    • Dey, S.1    Pal, A.2    Chakrabarti, P.3    Janin, J.4
  • 40
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • DOI 10.1016/j.jmb.2004.07.002, PII S0022283604008010
    • Gunasekaran K, Tsai C J and Nussinov R 2004 Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers J. Mol. Biol. 341 1327-41 (Pubitemid 39092318)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1327-1341
    • Gunasekaran, K.1    Tsai, C.-J.2    Nussinov, R.3
  • 41
    • 46249083761 scopus 로고    scopus 로고
    • Assembly reflects evolution of protein complexes
    • DOI 10.1038/nature06942, PII NATURE06942
    • Levy E D, Boeri Erba E, Robinson C V and Teichmann S A 2008 Assembly reflects evolution of protein complexes Nature 453 1262-5 (Pubitemid 351913589)
    • (2008) Nature , vol.453 , Issue.7199 , pp. 1262-1265
    • Levy, E.D.1    Erba, E.B.2    Robinson, C.V.3    Teichmann, S.A.4
  • 43
    • 33845989816 scopus 로고    scopus 로고
    • Structural Similarity Enhances Interaction Propensity of Proteins
    • DOI 10.1016/j.jmb.2006.11.020, PII S002228360601549X
    • Lukatsky D B, Shakhnovich B E, Mintseris J and Shakhnovich E I 2007 Structural similarity enhances interaction propensity of proteins J. Mol. Biol. 365 1596-606 (Pubitemid 46048849)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1596-1606
    • Lukatsky, D.B.1    Shakhnovich, B.E.2    Mintseris, J.3    Shakhnovich, E.I.4
  • 45
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • DOI 10.1038/nature04195
    • Wright C F, Teichmann S A, Clarke J and Dobson C M 2005 The importance of sequence diversity in the aggregation and evolution of proteins Nature 438 878-81 (Pubitemid 41753072)
    • (2005) Nature , vol.438 , Issue.7069 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 48
    • 63549102895 scopus 로고    scopus 로고
    • Intrinsic disorder in protein interactions: Insights from a comprehensive structural analysis
    • Fong J H et al 2009 Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis PLoS Comput. Biol. 5 e1000316
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1000316
    • Fong, J.H.1
  • 49
    • 0031913197 scopus 로고    scopus 로고
    • Mechanism and evolution of protein dimerization
    • Xu D, Tsai C J and Nussinov R 1998 Mechanism and evolution of protein dimerization Protein Sci. 7 533-44 (Pubitemid 28130874)
    • (1998) Protein Science , vol.7 , Issue.3 , pp. 533-544
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 51
    • 63149089900 scopus 로고    scopus 로고
    • Self-assembly and evolution of homomeric protein complexes
    • Villar G et al 2009 Self-assembly and evolution of homomeric protein complexes Phys. Rev. Lett. 102 118106
    • (2009) Phys. Rev. Lett. , vol.102 , pp. 118106
    • Villar, G.1
  • 52
    • 17844390103 scopus 로고    scopus 로고
    • Novel specificities emerge by stepwise duplication of functional modules
    • DOI 10.1101/gr.3102105
    • Pereira-Leal J B and Teichmann S A 2005 Novel specificities emerge by stepwise duplication of functional modules Genome Res. 15 552-9 (Pubitemid 41057817)
    • (2005) Genome Research , vol.15 , Issue.4 , pp. 552-559
    • Pereira-Leal, J.B.1    Teichmann, S.A.2
  • 53
    • 77949902801 scopus 로고    scopus 로고
    • Comparative evolutionary analysis of protein complexes in E. coli and yeast
    • Reid A J, Ranea J A and Orengo C A 2010 Comparative evolutionary analysis of protein complexes in E. coli and yeast BMC Genomics 11 79
    • (2010) BMC Genomics , vol.11 , pp. 79
    • Reid, A.J.1    Ranea, J.A.2    Orengo, C.A.3
  • 54
    • 77953081364 scopus 로고    scopus 로고
    • Functional states of homooligomers: Insights from the evolution of glycosyltransferases
    • Hashimoto K, Madej T, Bryant S H and Panchenko A R 2010 Functional states of homooligomers: insights from the evolution of glycosyltransferases J. Mol. Biol. 399 196-206
    • (2010) J. Mol. Biol. , vol.399 , pp. 196-206
    • Hashimoto, K.1    Madej, T.2    Bryant, S.H.3    Panchenko, A.R.4
  • 55
    • 34848913963 scopus 로고    scopus 로고
    • Evolution of protein complexes by duplication of homomeric interactions
    • Pereira-Leal J B, Levy E D, Kamp C and Teichmann S A 2007 Evolution of protein complexes by duplication of homomeric interactions Genome Biol. 8 R51
    • (2007) Genome Biol. , vol.8 , pp. 51
    • Pereira-Leal, J.B.1    Levy, E.D.2    Kamp, C.3    Teichmann, S.A.4
  • 58
    • 60449090411 scopus 로고    scopus 로고
    • Protein acrobatics in pairs-dimerization via domain swapping
    • Gronenborn A M 2009 Protein acrobatics in pairs-dimerization via domain swapping Curr. Opin. Struct. Biol. 19 39-49
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 39-49
    • Gronenborn, A.M.1
  • 59
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • DOI 10.1110/ps.0201402
    • Liu Y and Eisenberg D 2002 3D domain swapping: as domains continue to swap Protein Sci. 11 1285-99 (Pubitemid 34547201)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 60
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase A dimer with implications for amyloid formation
    • DOI 10.1038/84941
    • Liu Y, Gotte G, Libonati M and Eisenberg D 2001 A domain-swapped RNase A dimer with implications for amyloid formation Nat. Struct. Biol. 8 211-4 (Pubitemid 32180044)
    • (2001) Nature Structural Biology , vol.8 , Issue.3 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 63
    • 0030062246 scopus 로고    scopus 로고
    • Creation of a biologically active interleukin-5 monomer
    • DOI 10.1038/379652a0
    • Dickason R R and Huston D P 1996 Creation of a biologically active interleukin-5 monomer Nature 379 652-5 (Pubitemid 26053454)
    • (1996) Nature , vol.379 , Issue.6566 , pp. 652-655
    • Dickason, R.R.1    Huston, D.P.2
  • 64
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: Stability, specificity, and biological implications
    • DOI 10.1002/cbic.200300781
    • Mason J M and Arndt K M 2004 Coiled coil domains: stability, specificity, and biological implications ChemBioChem 5 170-6 (Pubitemid 39256232)
    • (2004) ChemBioChem , vol.5 , Issue.2 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 65
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'shea E K, Rutkowski R and Kim P S 1989 Evidence that the leucine zipper is a coiled coil Science 243 538-42 (Pubitemid 19048755)
    • (1989) Science , vol.243 , Issue.4890 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 66
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P B, Zhang T, Kim P S and Alber T 1993 A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants Science 262 1401-7
    • (1993) Science , vol.262 , Issue.5138 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 67
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • DOI 10.1038/371080a0
    • Harbury P B, Kim P S and Alber T 1994 Crystal structure of an isoleucine-zipper trimer Nature 371 80-3 (Pubitemid 24277468)
    • (1994) Nature , vol.371 , Issue.6492 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 68
    • 77951243441 scopus 로고    scopus 로고
    • Amino acid substitutions at protein-protein interfaces that modulate the oligomeric state
    • Nishi H and Ota M 2010 Amino acid substitutions at protein-protein interfaces that modulate the oligomeric state Proteins 78 1563-74
    • (2010) Proteins , vol.78 , pp. 1563-1574
    • Nishi, H.1    Ota, M.2
  • 69
    • 38149037823 scopus 로고    scopus 로고
    • Designed protein-protein association
    • Grueninger D et al 2008 Designed protein-protein association Science 319 206-9
    • (2008) Science , vol.319 , Issue.5860 , pp. 206-209
    • Grueninger, D.1
  • 70
    • 14144250670 scopus 로고    scopus 로고
    • Structure of the thermolabile mutant aldolase B, A149P: Molecular basis of hereditary fructose intolerance
    • DOI 10.1016/j.jmb.2005.01.008
    • Malay A D, Allen K N and Tolan D R 2005 Structure of the thermolabile mutant aldolase B, A149P: molecular basis of hereditary fructose intolerance J. Mol. Biol. 347 135-44 (Pubitemid 40283634)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.1 , pp. 135-144
    • Malay, A.D.1    Allen, K.N.2    Tolan, D.R.3
  • 73
    • 0033603494 scopus 로고    scopus 로고
    • P73 and p63 are homotetramers capable of weak heterotypic interactions with each other but not with p53
    • Davison T S et al 1999 p73 and p63 are homotetramers capable of weak heterotypic interactions with each other but not with p53 J. Biol. Chem. 274 18709-14
    • (1999) J. Biol. Chem. , vol.274 , pp. 18709-18714
    • Davison, T.S.1
  • 74
    • 70449588702 scopus 로고    scopus 로고
    • Structural evolution of p53, p63, and p73: Implication for heterotetramer formation
    • Joerger A C et al 2009 Structural evolution of p53, p63, and p73: implication for heterotetramer formation Proc. Natl Acad. Sci. USA 106 17705-10
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 17705-17710
    • Joerger, A.C.1
  • 75
    • 0347093483 scopus 로고    scopus 로고
    • LIM-domain-binding protein 1: A multifunctional cofactor that interacts with diverse proteins
    • DOI 10.1038/sj.embor.7400030
    • Matthews J M and Visvader J E 2003 LIM-domain-binding protein 1: a multifunctional cofactor that interacts with diverse proteins EMBO Rep. 4 1132-7 (Pubitemid 38088407)
    • (2003) EMBO Reports , vol.4 , Issue.12 , pp. 1132-1137
    • Matthews, J.M.1    Visvader, J.E.2
  • 76
    • 59149084489 scopus 로고    scopus 로고
    • Competition between LIM-binding domains
    • Matthews J M et al 2008 Competition between LIM-binding domains Biochem. Soc. Trans. 36 1393-7
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1393-1397
    • Matthews, J.M.1
  • 78
    • 77953082257 scopus 로고    scopus 로고
    • LIM domain binding proteins 1 and 2 have different oligomeric states
    • Cross A J, Jeffries C M, Trewhella J and Matthews J M 2010 LIM domain binding proteins 1 and 2 have different oligomeric states J. Mol. Biol. 399 133-44
    • (2010) J. Mol. Biol. , vol.399 , pp. 133-144
    • Cross, A.J.1    Jeffries, C.M.2    Trewhella, J.3    Matthews, J.M.4
  • 79
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • DOI 10.1016/S0022-2836(02)01281-0
    • Nooren I M and Thornton J M 2003 Structural characterisation and functional significance of transient protein-protein interactions J. Mol. Biol. 325 991-1018 (Pubitemid 36263408)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 80
    • 60749098410 scopus 로고    scopus 로고
    • The role of quaternary structure in (beta/alpha)(8)-barrel proteins: Evolutionary happenstance or a higher level of structure-function relationships?
    • Devenish S R and Gerrard J A 2009 The role of quaternary structure in (beta/alpha)(8)-barrel proteins: evolutionary happenstance or a higher level of structure-function relationships? Org. Biomol. Chem. 7 833-9
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 833-839
    • Devenish, S.R.1    Gerrard, J.A.2
  • 81
    • 0024261927 scopus 로고
    • Pyruvate kinase type M2 is phosphorylated at tyrosine residues in cells transformed by Rous sarcoma virus
    • DOI 10.1016/0014-5793(88)81014-7
    • Presek P, Reinacher M and Eigenbrodt E 1988 Pyruvate kinase type M2 is phosphorylated at tyrosine residues in cells transformed by Rous sarcoma virus FEBS Lett. 242 194-8 (Pubitemid 19012276)
    • (1988) FEBS Letters , vol.242 , Issue.1 , pp. 194-198
    • Presek, P.1    Reinacher, M.2    Eigenbrodt, E.3
  • 82
    • 42049091009 scopus 로고    scopus 로고
    • Regulation of the Rad53 protein kinase in signal amplification by oligomer assembly and disassembly
    • Jia-Lin Ma N and Stern D F 2008 Regulation of the Rad53 protein kinase in signal amplification by oligomer assembly and disassembly Cell Cycle 7 808-17 (Pubitemid 351520045)
    • (2008) Cell Cycle , vol.7 , Issue.6 , pp. 808-817
    • Ma, J.-L.1    Stern, D.F.2
  • 83
    • 0344875508 scopus 로고    scopus 로고
    • Role of cysteine amino acid residues on the RNA binding activity of human thymidylate synthase
    • DOI 10.1093/nar/gkg678
    • Lin X, Liu J, Maley F and Chu E 2003 Role of cysteine amino acid residues on the RNA binding activity of human thymidylate synthase Nucleic Acids Res. 31 4882-7 (Pubitemid 37441853)
    • (2003) Nucleic Acids Research , vol.31 , Issue.16 , pp. 4882-4887
    • Lin, X.1    Liu, J.2    Maley, F.3    Chu, E.4
  • 84
    • 77951528478 scopus 로고    scopus 로고
    • Dimer-monomer equilibrium of human thymidylate synthase monitored by fluorescence resonance energy transfer
    • Genovese F et al 2010 Dimer-monomer equilibrium of human thymidylate synthase monitored by fluorescence resonance energy transfer Protein Sci. 19 1023-30
    • (2010) Protein Sci. , vol.19 , pp. 1023-1030
    • Genovese, F.1
  • 85
    • 0029563173 scopus 로고
    • Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element
    • DOI 10.1074/jbc.270.50.30205
    • Arnold S F, Vorojeikina D P and Notides A C 1995 Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element J. Biol. Chem. 270 30205-12 (Pubitemid 26001698)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.50 , pp. 30205-30212
    • Arnold, S.F.1    Vorojeikina, D.P.2    Notides, A.C.3
  • 86
    • 0031897460 scopus 로고    scopus 로고
    • Carbon source-dependent phosphorylation of hexokinase PII and its role in the glucose-signaling response in yeast
    • Randez-Gil F, Sanz P, Entian K D and Prieto J A 1998 Carbon source-dependent phosphorylation of hexokinase PII and its role in the glucose-signaling response in yeast Mol. Cell Biol. 18 2940-8 (Pubitemid 28183463)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.5 , pp. 2940-2948
    • Randez-Gil, F.1    Sanz, P.2    Entian, K.-D.3    Prieto, J.A.4
  • 87
    • 0037023722 scopus 로고    scopus 로고
    • Phosphorylation and dimerization regulate nucleocytoplasmic shuttling of mammalian STE20-like kinase (MST)
    • DOI 10.1074/jbc.M108138200
    • Lee K K and Yonehara S 2002 Phosphorylation and dimerization regulate nucleocytoplasmic shuttling of mammalian STE20-like kinase (MST) J. Biol. Chem. 277 12351-8 (Pubitemid 34952806)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 12351-12358
    • Lee, K.-K.1    Yonehara, S.2
  • 89
    • 70449435684 scopus 로고    scopus 로고
    • The tyrosine kinase Csk dimerizes through its SH3 domain
    • Levinson N M, Visperas P R and Kuriyan J 2009 The tyrosine kinase Csk dimerizes through its SH3 domain PLoS One 4 e7683
    • (2009) PLoS One , vol.4 , pp. 7683
    • Levinson, N.M.1    Visperas, P.R.2    Kuriyan, J.3


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