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Volumn 49, Issue 2, 2013, Pages 222-231

From Systems to Structure: Bridging Networks and Mechanism

Author keywords

[No Author keywords available]

Indexed keywords

BRCA2 PROTEIN; CYCLINE; GUANOSINE TRIPHOSPHATASE; NUCLEIC ACID; PROTEIN KINASE R; RAS PROTEIN; VASCULOTROPIN;

EID: 84872784853     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2013.01.003     Document Type: Review
Times cited : (31)

References (106)
  • 4
    • 0041384254 scopus 로고    scopus 로고
    • Understanding and predicting protein assemblies with 3D structures
    • Aloy P., Russell R.B. Understanding and predicting protein assemblies with 3D structures. Comp. Funct. Genomics 2003, 4:410-415.
    • (2003) Comp. Funct. Genomics , vol.4 , pp. 410-415
    • Aloy, P.1    Russell, R.B.2
  • 6
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • Amberg D.C., Basart E., Botstein D. Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 1995, 2:28-35.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.C.1    Basart, E.2    Botstein, D.3
  • 7
    • 84867644046 scopus 로고    scopus 로고
    • A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function
    • Araya C.L., Fowler D.M., Chen W., Muniez I., Kelly J.W., Fields S. A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function. Proc. Natl. Acad. Sci. USA 2012, 109:16858-16863.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 16858-16863
    • Araya, C.L.1    Fowler, D.M.2    Chen, W.3    Muniez, I.4    Kelly, J.W.5    Fields, S.6
  • 10
    • 77950022453 scopus 로고    scopus 로고
    • Non-additivity of functional group contributions in protein-ligand binding: a comprehensive study by crystallography and isothermal titration calorimetry
    • Baum B., Muley L., Smolinski M., Heine A., Hangauer D., Klebe G. Non-additivity of functional group contributions in protein-ligand binding: a comprehensive study by crystallography and isothermal titration calorimetry. J. Mol. Biol. 2010, 397:1042-1054.
    • (2010) J. Mol. Biol. , vol.397 , pp. 1042-1054
    • Baum, B.1    Muley, L.2    Smolinski, M.3    Heine, A.4    Hangauer, D.5    Klebe, G.6
  • 11
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C., Sowa M.E., Gygi S.P., Harper J.W. Network organization of the human autophagy system. Nature 2010, 466:68-76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 12
    • 77953236579 scopus 로고    scopus 로고
    • Quantitative genetic interactions reveal biological modularity
    • Beltrao P., Cagney G., Krogan N.J. Quantitative genetic interactions reveal biological modularity. Cell 2010, 141:739-745.
    • (2010) Cell , vol.141 , pp. 739-745
    • Beltrao, P.1    Cagney, G.2    Krogan, N.J.3
  • 14
    • 33845864966 scopus 로고    scopus 로고
    • Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein
    • Bershtein S., Segal M., Bekerman R., Tokuriki N., Tawfik D.S. Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein. Nature 2006, 444:929-932.
    • (2006) Nature , vol.444 , pp. 929-932
    • Bershtein, S.1    Segal, M.2    Bekerman, R.3    Tokuriki, N.4    Tawfik, D.S.5
  • 15
    • 79953823548 scopus 로고    scopus 로고
    • A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis
    • Bhabha G., Lee J., Ekiert D.C., Gam J., Wilson I.A., Dyson H.J., Benkovic S.J., Wright P.E. A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis. Science 2011, 332:234-238.
    • (2011) Science , vol.332 , pp. 234-238
    • Bhabha, G.1    Lee, J.2    Ekiert, D.C.3    Gam, J.4    Wilson, I.A.5    Dyson, H.J.6    Benkovic, S.J.7    Wright, P.E.8
  • 16
    • 80053145220 scopus 로고    scopus 로고
    • Integration of protein motions with molecular networks reveals different mechanisms for permanent and transient interactions
    • Bhardwaj N., Abyzov A., Clarke D., Shou C., Gerstein M.B. Integration of protein motions with molecular networks reveals different mechanisms for permanent and transient interactions. Protein Sci. 2011, 20:1745-1754.
    • (2011) Protein Sci. , vol.20 , pp. 1745-1754
    • Bhardwaj, N.1    Abyzov, A.2    Clarke, D.3    Shou, C.4    Gerstein, M.B.5
  • 17
    • 79960245388 scopus 로고    scopus 로고
    • Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor
    • Bisson N., James D.A., Ivosev G., Tate S.A., Bonner R., Taylor L., Pawson T. Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor. Nat. Biotechnol. 2011, 29:653-658.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 653-658
    • Bisson, N.1    James, D.A.2    Ivosev, G.3    Tate, S.A.4    Bonner, R.5    Taylor, L.6    Pawson, T.7
  • 19
    • 84872607723 scopus 로고    scopus 로고
    • Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system
    • Published online December 16, 2012
    • Bondy-Denomy J., Pawluk A., Maxwell K.L., Davidson A.R. Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system. Nature 2012, Published online December 16, 2012. 10.1038/nature11723.
    • (2012) Nature
    • Bondy-Denomy, J.1    Pawluk, A.2    Maxwell, K.L.3    Davidson, A.R.4
  • 24
    • 0021504608 scopus 로고
    • The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
    • Carter P.J., Winter G., Wilkinson A.J., Fersht A.R. The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell 1984, 38:835-840.
    • (1984) Cell , vol.38 , pp. 835-840
    • Carter, P.J.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 27
    • 77956046092 scopus 로고    scopus 로고
    • Quantitative genetic interaction mapping using the E-MAP approach
    • Collins S.R., Roguev A., Krogan N.J. Quantitative genetic interaction mapping using the E-MAP approach. Methods Enzymol. 2010, 470:205-231.
    • (2010) Methods Enzymol. , vol.470 , pp. 205-231
    • Collins, S.R.1    Roguev, A.2    Krogan, N.J.3
  • 30
    • 80055012207 scopus 로고    scopus 로고
    • Expanding the proteome: disordered and alternatively folded proteins
    • Dyson H.J. Expanding the proteome: disordered and alternatively folded proteins. Q. Rev. Biophys. 2011, 44:467-518.
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 467-518
    • Dyson, H.J.1
  • 31
    • 58749102026 scopus 로고    scopus 로고
    • Protein kinase R reveals an evolutionary model for defeating viral mimicry
    • Elde N.C., Child S.J., Geballe A.P., Malik H.S. Protein kinase R reveals an evolutionary model for defeating viral mimicry. Nature 2009, 457:485-489.
    • (2009) Nature , vol.457 , pp. 485-489
    • Elde, N.C.1    Child, S.J.2    Geballe, A.P.3    Malik, H.S.4
  • 32
    • 77957283851 scopus 로고    scopus 로고
    • The next frontier of systems biology: higher-order and interspecies interactions
    • Fischbach M.A., Krogan N.J. The next frontier of systems biology: higher-order and interspecies interactions. Genome Biol. 2010, 11:208.
    • (2010) Genome Biol. , vol.11 , pp. 208
    • Fischbach, M.A.1    Krogan, N.J.2
  • 33
    • 79960617916 scopus 로고    scopus 로고
    • Structural principles within the human-virus protein-protein interaction network
    • Franzosa E.A., Xia Y. Structural principles within the human-virus protein-protein interaction network. Proc. Natl. Acad. Sci. USA 2011, 108:10538-10543.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10538-10543
    • Franzosa, E.A.1    Xia, Y.2
  • 34
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • Fraser J.S., Clarkson M.W., Degnan S.C., Erion R., Kern D., Alber T. Hidden alternative structures of proline isomerase essential for catalysis. Nature 2009, 462:669-673.
    • (2009) Nature , vol.462 , pp. 669-673
    • Fraser, J.S.1    Clarkson, M.W.2    Degnan, S.C.3    Erion, R.4    Kern, D.5    Alber, T.6
  • 35
    • 78149392991 scopus 로고    scopus 로고
    • Subtle alterations in PCNA-partner interactions severely impair DNA replication and repair
    • Fridman Y., Palgi N., Dovrat D., Ben-Aroya S., Hieter P., Aharoni A. Subtle alterations in PCNA-partner interactions severely impair DNA replication and repair. PLoS Biol. 2010, 8:e1000507.
    • (2010) PLoS Biol. , vol.8
    • Fridman, Y.1    Palgi, N.2    Dovrat, D.3    Ben-Aroya, S.4    Hieter, P.5    Aharoni, A.6
  • 37
    • 33846471075 scopus 로고    scopus 로고
    • Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance
    • Geller R., Vignuzzi M., Andino R., Frydman J. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 2007, 21:195-205.
    • (2007) Genes Dev. , vol.21 , pp. 195-205
    • Geller, R.1    Vignuzzi, M.2    Andino, R.3    Frydman, J.4
  • 38
    • 0021097083 scopus 로고
    • The combinatorial distance geometry method for the calculation of molecular conformation. I. A new approach to an old problem
    • Havel T.F., Kuntz I.D., Crippen G.M. The combinatorial distance geometry method for the calculation of molecular conformation. I. A new approach to an old problem. J. Theor. Biol. 1983, 104:359-381.
    • (1983) J. Theor. Biol. , vol.104 , pp. 359-381
    • Havel, T.F.1    Kuntz, I.D.2    Crippen, G.M.3
  • 40
    • 84861534981 scopus 로고    scopus 로고
    • Contingency and statistical laws in replicate microbial closed ecosystems
    • Hekstra D.R., Leibler S. Contingency and statistical laws in replicate microbial closed ecosystems. Cell 2012, 149:1164-1173.
    • (2012) Cell , vol.149 , pp. 1164-1173
    • Hekstra, D.R.1    Leibler, S.2
  • 43
    • 79953289737 scopus 로고    scopus 로고
    • Mapping of signaling networks through synthetic genetic interaction analysis by RNAi
    • Horn T., Sandmann T., Fischer B., Axelsson E., Huber W., Boutros M. Mapping of signaling networks through synthetic genetic interaction analysis by RNAi. Nat. Methods 2011, 8:341-346.
    • (2011) Nat. Methods , vol.8 , pp. 341-346
    • Horn, T.1    Sandmann, T.2    Fischer, B.3    Axelsson, E.4    Huber, W.5    Boutros, M.6
  • 44
    • 0023645205 scopus 로고
    • Non-additivity in protein-protein interactions
    • Horovitz A. Non-additivity in protein-protein interactions. J. Mol. Biol. 1987, 196:733-735.
    • (1987) J. Mol. Biol. , vol.196 , pp. 733-735
    • Horovitz, A.1
  • 45
    • 0030322783 scopus 로고    scopus 로고
    • Double-mutant cycles: a powerful tool for analyzing protein structure and function
    • Horovitz A. Double-mutant cycles: a powerful tool for analyzing protein structure and function. Fold. Des. 1996, 1:R121-R126.
    • (1996) Fold. Des. , vol.1
    • Horovitz, A.1
  • 46
    • 0025126043 scopus 로고
    • Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins
    • Horovitz A., Fersht A.R. Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. J. Mol. Biol. 1990, 214:613-617.
    • (1990) J. Mol. Biol. , vol.214 , pp. 613-617
    • Horovitz, A.1    Fersht, A.R.2
  • 51
    • 33845875196 scopus 로고    scopus 로고
    • Relating three-dimensional structures to protein networks provides evolutionary insights
    • Kim P.M., Lu L.J., Xia Y., Gerstein M.B. Relating three-dimensional structures to protein networks provides evolutionary insights. Science 2006, 314:1938-1941.
    • (2006) Science , vol.314 , pp. 1938-1941
    • Kim, P.M.1    Lu, L.J.2    Xia, Y.3    Gerstein, M.B.4
  • 52
    • 84874283933 scopus 로고    scopus 로고
    • CBFβ stabilizes HIV Vif to counteract APOBEC3 at the expense of RUNX1 target gene expression
    • Published online January 17, 2013
    • Kim D.Y., Kwon E., Hartley P.D., Crosby D.C., Mann S., Krogan N.J., Gross J.D. CBFβ stabilizes HIV Vif to counteract APOBEC3 at the expense of RUNX1 target gene expression. Mol. Cell 2013, 49. Published online January 17, 2013. 10.1016/j.molcel.2012.12.012.
    • (2013) Mol. Cell , vol.49
    • Kim, D.Y.1    Kwon, E.2    Hartley, P.D.3    Crosby, D.C.4    Mann, S.5    Krogan, N.J.6    Gross, J.D.7
  • 55
    • 79951481957 scopus 로고    scopus 로고
    • Initial impact of the sequencing of the human genome
    • Lander E.S. Initial impact of the sequencing of the human genome. Nature 2011, 470:187-197.
    • (2011) Nature , vol.470 , pp. 187-197
    • Lander, E.S.1
  • 56
    • 84860851412 scopus 로고    scopus 로고
    • Sequential application of anticancer drugs enhances cell death by rewiring apoptotic signaling networks
    • Lee M.J., Ye A.S., Gardino A.K., Heijink A.M., Sorger P.K., MacBeath G., Yaffe M.B. Sequential application of anticancer drugs enhances cell death by rewiring apoptotic signaling networks. Cell 2012, 149:780-794.
    • (2012) Cell , vol.149 , pp. 780-794
    • Lee, M.J.1    Ye, A.S.2    Gardino, A.K.3    Heijink, A.M.4    Sorger, P.K.5    MacBeath, G.6    Yaffe, M.B.7
  • 57
    • 79960642108 scopus 로고    scopus 로고
    • Molecular mechanisms of epistasis within and between genes
    • Lehner B. Molecular mechanisms of epistasis within and between genes. Trends Genet. 2011, 27:323-331.
    • (2011) Trends Genet. , vol.27 , pp. 323-331
    • Lehner, B.1
  • 60
    • 84872824241 scopus 로고    scopus 로고
    • Design principles of regulatory networks: Searching for the molecular algorithms of the cell
    • this issue
    • Lim W.A., Lee C.M., Tang C. Design principles of regulatory networks: Searching for the molecular algorithms of the cell. Mol. Cell 2013, 49:202-212. this issue.
    • (2013) Mol. Cell , vol.49 , pp. 202-212
    • Lim, W.A.1    Lee, C.M.2    Tang, C.3
  • 62
    • 27144538817 scopus 로고    scopus 로고
    • The biochemical architecture of an ancient adaptive landscape
    • Lunzer M., Miller S.P., Felsheim R., Dean A.M. The biochemical architecture of an ancient adaptive landscape. Science 2005, 310:499-501.
    • (2005) Science , vol.310 , pp. 499-501
    • Lunzer, M.1    Miller, S.P.2    Felsheim, R.3    Dean, A.M.4
  • 63
    • 78449233935 scopus 로고    scopus 로고
    • Pervasive cryptic epistasis in molecular evolution
    • Lunzer M., Golding G.B., Dean A.M. Pervasive cryptic epistasis in molecular evolution. PLoS Genet. 2010, 6:e1001162.
    • (2010) PLoS Genet. , vol.6
    • Lunzer, M.1    Golding, G.B.2    Dean, A.M.3
  • 65
    • 0033026065 scopus 로고    scopus 로고
    • Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals
    • Marston N.J., Richards W.J., Hughes D., Bertwistle D., Marshall C.J., Ashworth A. Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals. Mol. Cell. Biol. 1999, 19:4633-4642.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4633-4642
    • Marston, N.J.1    Richards, W.J.2    Hughes, D.3    Bertwistle, D.4    Marshall, C.J.5    Ashworth, A.6
  • 67
    • 84871042527 scopus 로고    scopus 로고
    • Aggravating genetic interactions allow a solution to redundancy in a bacterial pathogen
    • O'Connor T.J., Boyd D., Dorer M.S., Isberg R.R. Aggravating genetic interactions allow a solution to redundancy in a bacterial pathogen. Science 2012, 338:1440-1444.
    • (2012) Science , vol.338 , pp. 1440-1444
    • O'Connor, T.J.1    Boyd, D.2    Dorer, M.S.3    Isberg, R.R.4
  • 68
    • 34548040966 scopus 로고    scopus 로고
    • Crystal structure of an ancient protein: evolution by conformational epistasis
    • Ortlund E.A., Bridgham J.T., Redinbo M.R., Thornton J.W. Crystal structure of an ancient protein: evolution by conformational epistasis. Science 2007, 317:1544-1548.
    • (2007) Science , vol.317 , pp. 1544-1548
    • Ortlund, E.A.1    Bridgham, J.T.2    Redinbo, M.R.3    Thornton, J.W.4
  • 70
    • 0024457568 scopus 로고
    • Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase
    • Perry K.M., Onuffer J.J., Gittelman M.S., Barmat L., Matthews C.R. Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase. Biochemistry 1989, 28:7961-7968.
    • (1989) Biochemistry , vol.28 , pp. 7961-7968
    • Perry, K.M.1    Onuffer, J.J.2    Gittelman, M.S.3    Barmat, L.4    Matthews, C.R.5
  • 71
    • 54149088214 scopus 로고    scopus 로고
    • Epistasis-the essential role of gene interactions in the structure and evolution of genetic systems
    • Phillips P.C. Epistasis-the essential role of gene interactions in the structure and evolution of genetic systems. Nat. Rev. Genet. 2008, 9:855-867.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 855-867
    • Phillips, P.C.1
  • 73
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • Rappsilber J. The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes. J. Struct. Biol. 2011, 173:530-540.
    • (2011) J. Struct. Biol. , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 74
    • 84455167671 scopus 로고    scopus 로고
    • Hot spots for allosteric regulation on protein surfaces
    • Reynolds K.A., McLaughlin R.N., Ranganathan R. Hot spots for allosteric regulation on protein surfaces. Cell 2011, 147:1564-1575.
    • (2011) Cell , vol.147 , pp. 1564-1575
    • Reynolds, K.A.1    McLaughlin, R.N.2    Ranganathan, R.3
  • 78
    • 38049148291 scopus 로고    scopus 로고
    • Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel
    • Sadovsky E., Yifrach O. Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel. Proc. Natl. Acad. Sci. USA 2007, 104:19813-19818.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19813-19818
    • Sadovsky, E.1    Yifrach, O.2
  • 80
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • Schreiber G., Fersht A.R. Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J. Mol. Biol. 1995, 248:478-486.
    • (1995) J. Mol. Biol. , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 81
  • 84
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa M.E., Bennett E.J., Gygi S.P., Harper J.W. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009, 138:389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 87
    • 33749125656 scopus 로고    scopus 로고
    • Combinatorial RNA interference in Caenorhabditis elegans reveals that redundancy between gene duplicates can be maintained for more than 80 million years of evolution
    • R69
    • Tischler J., Lehner B., Chen N., Fraser A.G. Combinatorial RNA interference in Caenorhabditis elegans reveals that redundancy between gene duplicates can be maintained for more than 80 million years of evolution. Genome Biol. 2006, 7. R69.
    • (2006) Genome Biol. , vol.7
    • Tischler, J.1    Lehner, B.2    Chen, N.3    Fraser, A.G.4
  • 88
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki N., Tawfik D.S. Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 2009, 459:668-673.
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 91
    • 0035065485 scopus 로고    scopus 로고
    • SNPs, protein structure, and disease
    • Wang Z., Moult J. SNPs, protein structure, and disease. Hum. Mutat. 2001, 17:263-270.
    • (2001) Hum. Mutat. , vol.17 , pp. 263-270
    • Wang, Z.1    Moult, J.2
  • 92
    • 84863010950 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of protein networks provides insight into human genetic disease
    • Wang X., Wei X., Thijssen B., Das J., Lipkin S.M., Yu H. Three-dimensional reconstruction of protein networks provides insight into human genetic disease. Nat. Biotechnol. 2012, 30:159-164.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 159-164
    • Wang, X.1    Wei, X.2    Thijssen, B.3    Das, J.4    Lipkin, S.M.5    Yu, H.6
  • 93
    • 84867835793 scopus 로고    scopus 로고
    • A remote mutation affects the hydride transfer by disrupting concerted protein motions in thymidylate synthase
    • Wang Z., Abeysinghe T., Finer-Moore J.S., Stroud R.M., Kohen A. A remote mutation affects the hydride transfer by disrupting concerted protein motions in thymidylate synthase. J. Am. Chem. Soc. 2012, 134:17722-17730.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 17722-17730
    • Wang, Z.1    Abeysinghe, T.2    Finer-Moore, J.S.3    Stroud, R.M.4    Kohen, A.5
  • 94
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells J.A. Additivity of mutational effects in proteins. Biochemistry 1990, 29:8509-8517.
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 96
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • Wittinghofer A., Vetter I.R. Structure-function relationships of the G domain, a canonical switch motif. Annu. Rev. Biochem. 2011, 80:943-971.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 97
    • 78650947473 scopus 로고    scopus 로고
    • Interplay of transcription factors in T-cell differentiation and function: the role of Runx
    • Wong W.F., Kohu K., Chiba T., Sato T., Satake M. Interplay of transcription factors in T-cell differentiation and function: the role of Runx. Immunology 2011, 132:157-164.
    • (2011) Immunology , vol.132 , pp. 157-164
    • Wong, W.F.1    Kohu, K.2    Chiba, T.3    Sato, T.4    Satake, M.5
  • 100
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X., Yu Y., Liu B., Luo K., Kong W., Mao P., Yu X.F. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 2003, 302:1056-1060.
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.F.7
  • 102
    • 84856014513 scopus 로고    scopus 로고
    • T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction
    • Zhang W., Du J., Evans S.L., Yu Y., Yu X.F. T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction. Nature 2012, 481:376-379.
    • (2012) Nature , vol.481 , pp. 376-379
    • Zhang, W.1    Du, J.2    Evans, S.L.3    Yu, Y.4    Yu, X.F.5
  • 103
    • 64849098267 scopus 로고    scopus 로고
    • Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha
    • Zhao S., Lin Y., Xu W., Jiang W., Zha Z., Wang P., Yu W., Li Z., Gong L., Peng Y., et al. Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha. Science 2009, 324:261-265.
    • (2009) Science , vol.324 , pp. 261-265
    • Zhao, S.1    Lin, Y.2    Xu, W.3    Jiang, W.4    Zha, Z.5    Wang, P.6    Yu, W.7    Li, Z.8    Gong, L.9    Peng, Y.10
  • 104
    • 0034638921 scopus 로고    scopus 로고
    • Lessons learned from BRCA1 and BRCA2
    • Zheng L., Li S., Boyer T.G., Lee W.H. Lessons learned from BRCA1 and BRCA2. Oncogene 2000, 19:6159-6175.
    • (2000) Oncogene , vol.19 , pp. 6159-6175
    • Zheng, L.1    Li, S.2    Boyer, T.G.3    Lee, W.H.4
  • 106
    • 84856405512 scopus 로고    scopus 로고
    • The mystery of missing heritability: Genetic interactions create phantom heritability
    • Zuk O., Hechter E., Sunyaev S.R., Lander E.S. The mystery of missing heritability: Genetic interactions create phantom heritability. Proc. Natl. Acad. Sci. USA 2012, 109:1193-1198.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 1193-1198
    • Zuk, O.1    Hechter, E.2    Sunyaev, S.R.3    Lander, E.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.