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Volumn 8, Issue 1, 2012, Pages 47-57

Intrinsically disordered regions as affinity tuners in protein-DNA interactions

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA BINDING PROTEIN;

EID: 82655179905     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/c1mb05273j     Document Type: Review
Times cited : (162)

References (133)
  • 1
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • DOI 10.1006/jmbi.1999.3110
    • P. E. Wright H. J. Dyson Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm J. Mol. Biol. 1999 293 321 331 (Pubitemid 29516173)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 3
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • DOI 10.1016/S0968-0004(02)02169-2, PII S0968000402021692
    • P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 2002 27 527 533 (Pubitemid 35279598)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 4
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • H. J. Dyson P. E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 2005 6 197 208 (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 5
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • DOI 10.1046/j.0014-2956.2001.02649.x
    • V. N. Uversky What does it mean to be natively unfolded? Eur. J. Biochem. 2002 269 2 12 (Pubitemid 34107333)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.1 , pp. 2-12
    • Uversky, V.N.1
  • 7
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • T. Mittag L. E. Kay J. D. Forman-Kay Protein dynamics and conformational disorder in molecular recognition J. Mol. Recognit. 2010 23 105 116
    • (2010) J. Mol. Recognit. , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 9
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • DOI 10.1126/science.1163581
    • J. Gsponer M. E. Futschik S. A. Teichmann M. M. Babu Tight regulation of unstructured proteins: from transcript synthesis to protein degradation Science 2008 322 1365 1368 (Pubitemid 352775246)
    • (2008) Science , vol.322 , Issue.5906 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 14
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
    • DOI 10.1016/j.jmb.2004.02.002, PII S0022283604001482
    • J. J. Ward J. S. Sodhi L. J. McGuffin B. F. Buxton D. T. Jones Prediction and functional analysis of native disorder in proteins from the three kingdoms of life J. Mol. Biol. 2004 337 635 645 (Pubitemid 38326883)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 15
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • V. N. Uversky J. R. Gillespie A. L. Fink Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins: Struct., Funct., Genet. 2000 41 415 427
    • (2000) Proteins: Struct., Funct., Genet. , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 17
    • 44949262123 scopus 로고    scopus 로고
    • Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins
    • DOI 10.1021/ja710446s
    • H. T. Tran A. Mao R. V. Pappu Role of backbone - solvent interactions in determining conformational equilibria of intrinsically disordered proteins J. Am. Chem. Soc. 2008 130 7380 7392 (Pubitemid 351813231)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.23 , pp. 7380-7392
    • Tran, H.T.1    Mao, A.2    Pappu, R.V.3
  • 19
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • D. Eliezer Biophysical characterization of intrinsically disordered proteins Curr. Opin. Struct. Biol. 2009 19 23 30
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 20
    • 77951645923 scopus 로고    scopus 로고
    • Sequence Determinants of Compaction in Intrinsically Disordered Proteins
    • J. A. Marsh J. D. Forman-Kay Sequence Determinants of Compaction in Intrinsically Disordered Proteins Biophys. J. 2010 98 2383 2390
    • (2010) Biophys. J. , vol.98 , pp. 2383-2390
    • Marsh, J.A.1    Forman-Kay, J.D.2
  • 21
    • 77952335311 scopus 로고    scopus 로고
    • Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
    • A. H. Mao S. L. Crick A. Vitalis C. L. Chicoine R. V. Pappu Net charge per residue modulates conformational ensembles of intrinsically disordered proteins Proc. Natl. Acad. Sci. U. S. A. 2010 107 8183 8188
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4    Pappu, R.V.5
  • 24
    • 79955923819 scopus 로고    scopus 로고
    • Energy landscape analyses of disordered histones tails reveal special organization of their conformational dynamics
    • D. Potoyan G. Papoian Energy landscape analyses of disordered histones tails reveal special organization of their conformational dynamics J. Am. Chem. Soc. 2011 133 7405 7415
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7405-7415
    • Potoyan, D.1    Papoian, G.2
  • 25
    • 77249102545 scopus 로고    scopus 로고
    • Comparing models of evolution for ordered and disordered proteins
    • C. J. Brown A. K. Johnson G. W. Daughdrill Comparing models of evolution for ordered and disordered proteins Mol. Biol. Evol. 2010 27 609 621
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 609-621
    • Brown, C.J.1    Johnson, A.K.2    Daughdrill, G.W.3
  • 27
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • DOI 10.1016/j.febslet.2005.03.072, PII S0014579305004242
    • P. Tompa The interplay between structure and function in intrinsically unstructured proteins FEBS Lett. 2005 579 3346 3354 (Pubitemid 40804685)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3346-3354
    • Tompa, P.1
  • 28
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • DOI 10.1016/S0959-440X(02)00289-0
    • H. J. Dyson P. E. Wright Coupling of folding and binding for unstructured proteins Curr. Opin. Struct. Biol. 2002 12 54 60 (Pubitemid 34142721)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.1 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 29
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • P. Tompa M. Fuxreiter Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions Trends Biochem. Sci. 2008 33 2 8
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 30
    • 0027311259 scopus 로고
    • Close encounters: Why unstructured, polymeric domains can increase rates of specific macromolecular association
    • DOI 10.1016/0968-0004(93)90111-Y
    • B. W. Pontius Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association Trends Biochem. Sci. 1993 18 181 186 (Pubitemid 23142574)
    • (1993) Trends in Biochemical Sciences , vol.18 , Issue.5 , pp. 181-186
    • Pontius, B.W.1
  • 33
    • 70350321301 scopus 로고    scopus 로고
    • Disordered tails of homeodomains facilitate DNA recognition by providing a trade-off between folding and specific binding
    • A. Tóth-Petróczy M. Fuxreiter Y. Levy Disordered tails of homeodomains facilitate DNA recognition by providing a trade-off between folding and specific binding J. Am. Chem. Soc. 2009 131 15084 15085
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15084-15085
    • Tóth-Petróczy, A.1    Fuxreiter, M.2    Levy, Y.3
  • 34
    • 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
    • K. Gunasekaran C. J. Tsai R. Nussinov Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers J. Mol. Biol. 2004 341 1327 1341 (Pubitemid 39092318)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1327-1341
    • Gunasekaran, K.1    Tsai, C.-J.2    Nussinov, R.3
  • 35
    • 34547943482 scopus 로고    scopus 로고
    • Molecular Principles of the Interactions of Disordered Proteins
    • DOI 10.1016/j.jmb.2007.07.004, PII S0022283607009205
    • B. Meszaros P. Tompa I. Simon Z. Dosztanyi Molecular principles of the interactions of disordered proteins J. Mol. Biol. 2007 372 549 561 (Pubitemid 47267965)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.2 , pp. 549-561
    • Meszaros, B.1    Tompa, P.2    Simon, I.3    Dosztanyi, Z.4
  • 36
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • DOI 10.1016/j.jmb.2004.03.017, PII S0022283604003079
    • M. Fuxreiter I. Simon P. Friedrich P. Tompa Preformed structural elements feature in partner recognition by intrinsically unstructured proteins J. Mol. Biol. 2004 338 1015 1026 (Pubitemid 38542830)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.5 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 37
    • 14844361449 scopus 로고    scopus 로고
    • Primary contact sites in intrinsically unstructured proteins: The case of calpastatin and microtubule-associated protein 2
    • DOI 10.1021/bi047817f
    • V. Csizmok M. Bokor P. Banki E. Klement K. F. Medzihradszky P. Friedrich K. Tompa P. Tompa Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2 Biochemistry 2005 44 3955 3964 (Pubitemid 40358047)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 3955-3964
    • Csizmok, V.1    Bokor, M.2    Banki, P.3    Klement, E.4    Medzihradszky, K.F.5    Friedrich, P.6    Tompa, K.7    Tompa, P.8
  • 38
    • 20444414545 scopus 로고    scopus 로고
    • Linear motifs: Evolutionary interaction switches
    • DOI 10.1016/j.febslet.2005.04.005, PII S0014579305004618
    • V. Neduva R. B. Russell Linear motifs: evolutionary interaction switches FEBS Lett. 2005 579 3342 3345 (Pubitemid 40804684)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3342-3345
    • Neduva, V.1    Russell, R.B.2
  • 39
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • DOI 10.1093/bioinformatics/btm035
    • M. Fuxreiter P. Tompa I. Simon Local structural disorder imparts plasticity on linear motifs Bioinformatics 2007 23 950 956 (Pubitemid 47050581)
    • (2007) Bioinformatics , vol.23 , Issue.8 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 40
    • 80053441923 scopus 로고    scopus 로고
    • Dynamic protein-DNA recognition: Beyond what can be seen
    • M. Fuxreiter I. Simon S. Bondos Dynamic protein-DNA recognition: beyond what can be seen Trends Biochem. Sci. 2011 36 415 423
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 415-423
    • Fuxreiter, M.1    Simon, I.2    Bondos, S.3
  • 41
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • R. S. Spolar M. T. Record, Jr Coupling of local folding to site-specific binding of proteins to DNA Science 1994 263 777 784 (Pubitemid 24093205)
    • (1994) Science , vol.263 , Issue.5148 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 42
    • 0030916275 scopus 로고    scopus 로고
    • Interactions of the vnd/NK-2 homeodomain with DNA by nuclear magnetic resonance spectroscopy: Basis of binding specificity
    • DOI 10.1021/bi9620060
    • J. M. Gruschus D. H. Tsao L. H. Wang M. Nirenberg J. A. Ferretti Interactions of the vnd/NK-2 homeodomain with DNA by nuclear magnetic resonance spectroscopy: basis of binding specificity Biochemistry 1997 36 5372 5380 (Pubitemid 27200033)
    • (1997) Biochemistry , vol.36 , Issue.18 , pp. 5372-5380
    • Gruschus, J.M.1    Tsao, D.H.H.2    Wang, L.-H.3    Nirenberg, M.4    Ferretti, J.A.5
  • 43
    • 0027787519 scopus 로고
    • Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex
    • DOI 10.1006/jmbi.1993.1661
    • M. Billeter Y. Q. Qian G. Otting M. Muller W. Gehring K. Wuthrich Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex J. Mol. Biol. 1993 234 1084 1093 (Pubitemid 24027238)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.4 , pp. 1084-1093
    • Billeter, M.1    Qian, Y.Q.2    Otting, G.3    Muller, M.4    Gehring, W.5    Wuthrich, K.6
  • 44
    • 35548931586 scopus 로고    scopus 로고
    • Functional Specificity of a Hox Protein Mediated by the Recognition of Minor Groove Structure
    • DOI 10.1016/j.cell.2007.09.024, PII S0092867407012123
    • R. Joshi J. M. Passner R. Rohs R. Jain A. Sosinsky M. A. Crickmore V. Jacob A. K. Aggarwal B. Honig R. S. Mann Functional specificity of a Hox protein mediated by the recognition of minor groove structure Cell 2007 131 530 543 (Pubitemid 350007697)
    • (2007) Cell , vol.131 , Issue.3 , pp. 530-543
    • Joshi, R.1    Passner, J.M.2    Rohs, R.3    Jain, R.4    Sosinsky, A.5    Crickmore, M.A.6    Jacob, V.7    Aggarwal, A.K.8    Honig, B.9    Mann, R.S.10
  • 45
    • 33749014926 scopus 로고    scopus 로고
    • The extended arms of DNA-binding domains: a tale of tails
    • DOI 10.1016/j.tibs.2006.08.006, PII S0968000406002283
    • C. Crane-Robinson A. I. Dragan P. L. Privalov The extended arms of DNA-binding domains: a tale of tails Trends Biochem. Sci. 2006 31 547 552 (Pubitemid 44444875)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.10 , pp. 547-552
    • Crane-Robinson, C.1    Dragan, A.I.2    Privalov, P.L.3
  • 46
    • 0027288479 scopus 로고
    • Ectopic expression and function of the Antp and Scr homeotic genes: The N terminus of the homeodomain is critical to functional specificity
    • W. L. Zeng D. J. Andrew L. D. Mathies M. A. Horner M. P. Scott Ectopic Expression and Function of the Antp and Scr Homeotic Genes - the N-Terminus of the Homeodomain Is Critical to Functional Specificity Development 1993 118 339 352 (Pubitemid 23214023)
    • (1993) Development , vol.118 , Issue.2 , pp. 339-352
    • Zeng, W.1    Andrew, D.J.2    Mathies, L.D.3    Horner, M.A.4    Scott, M.P.5
  • 49
    • 0004238344 scopus 로고    scopus 로고
    • Oxford Univ. Press, Oxford
    • B. Lewin, Genes VII, Oxford Univ. Press, Oxford, 2000
    • (2000) Genes VII
    • Lewin, B.1
  • 50
    • 0036789619 scopus 로고    scopus 로고
    • Physics of protein-DNA interaction
    • R. F. Bruinsma Physics of protein-DNA interaction Phys. A (Amsterdam, Neth.) 2002 313 211 237
    • (2002) Phys. A (Amsterdam, Neth.) , vol.313 , pp. 211-237
    • Bruinsma, R.F.1
  • 51
    • 65549171477 scopus 로고    scopus 로고
    • An end to 40 years of mistakes in DNA-protein association kinetics?
    • S. E. Halford An end to 40 years of mistakes in DNA-protein association kinetics? Biochem. Soc. Trans. 2009 37 343 348
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 343-348
    • Halford, S.E.1
  • 52
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • DOI 10.1093/nar/gkh624
    • S. E. Halford J. F. Marko How do site-specific DNA-binding proteins find their targets? Nucleic Acids Res. 2004 32 3040 3052 (Pubitemid 39022995)
    • (2004) Nucleic Acids Research , vol.32 , Issue.10 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 54
    • 0024531901 scopus 로고
    • Facilitated Target Location in Biological-Systems
    • P. H. Von Hippel O. G. Berg Facilitated Target Location in Biological-Systems J. Biol. Chem. 1989 264 675 678
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 55
    • 0019887628 scopus 로고
    • Diffusion-Driven Mechanisms of Protein Translocation on Nucleic-Acids. 1. Models and Theory
    • O. G. Berg R. B. Winter P. H. Vonhippel Diffusion-Driven Mechanisms of Protein Translocation on Nucleic-Acids. 1. Models and Theory Biochemistry 1981 20 6929 6948
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Vonhippel, P.H.3
  • 56
    • 19744381543 scopus 로고    scopus 로고
    • Enhancement of association rates by nonspecific binding to DNA and cell membranes
    • H. X. Zhou A. Szabo Enhancement of association rates by nonspecific binding to DNA and cell membranes Phys. Rev. Lett. 2004 93 178101-1 18101-4
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 1781011-181014
    • Zhou, H.X.1    Szabo, A.2
  • 57
    • 0036656143 scopus 로고    scopus 로고
    • How to get from A to B: Strategies for analysing protein motion on DNA
    • S. E. Halford M. D. Szczelkun How to get from A to B: strategies for analysing protein motion on DNA Eur. Biophys. J. 2002 31 257 267
    • (2002) Eur. Biophys. J. , vol.31 , pp. 257-267
    • Halford, S.E.1    Szczelkun, M.D.2
  • 60
    • 34249932435 scopus 로고    scopus 로고
    • Probing transcription factor dynamics at the single-molecule level in a living cell
    • DOI 10.1126/science.1141967
    • J. Elf G. W. Li X. S. Xie Probing transcription factor dynamics at the single-molecule level in a living cell Science 2007 316 1191 1194 (Pubitemid 46877481)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1191-1194
    • Elf, J.1    Li, G.-W.2    Xie, X.S.3
  • 63
    • 58149345492 scopus 로고    scopus 로고
    • Protein Sliding along DNA: Dynamics and Structural Characterization
    • O. Givaty Y. Levy Protein Sliding along DNA: Dynamics and Structural Characterization J. Mol. Biol. 2009 385 1087 1097
    • (2009) J. Mol. Biol. , vol.385 , pp. 1087-1097
    • Givaty, O.1    Levy, Y.2
  • 64
    • 77949320402 scopus 로고    scopus 로고
    • Searching DNA via a "monkey bar" mechanism: The significance of disordered tails
    • D. Vuzman A. Azia Y. Levy Searching DNA via a "monkey bar" mechanism: the significance of disordered tails J. Mol. Biol. 2010 396 674 684
    • (2010) J. Mol. Biol. , vol.396 , pp. 674-684
    • Vuzman, D.1    Azia, A.2    Levy, Y.3
  • 66
    • 10044223573 scopus 로고    scopus 로고
    • Kinetics of protein-DNA interaction: Facilitated target location in sequence-dependent potential
    • DOI 10.1529/biophysj.104.050765
    • M. Slutsky L. A. Mirny Kinetics of protein-DNA interaction: facilitated target location in sequence-dependent potential Biophys. J. 2004 87 4021 4035 (Pubitemid 39602906)
    • (2004) Biophysical Journal , vol.87 , Issue.6 , pp. 4021-4035
    • Slutsky, M.1    Mirny, L.A.2
  • 67
    • 46349108554 scopus 로고    scopus 로고
    • Spatial effects on the speed and reliability of protein-DNA search
    • DOI 10.1093/nar/gkn173
    • Z. Wunderlich L. A. Mirny Spatial effects on the speed and reliability of protein-DNA search Nucleic Acids Res. 2008 36 3570 3578 (Pubitemid 351917521)
    • (2008) Nucleic Acids Research , vol.36 , Issue.11 , pp. 3570-3578
    • Wunderlich, Z.1    Mirny, L.A.2
  • 69
    • 0030025170 scopus 로고    scopus 로고
    • Oct-1 POU domain-DNA interactions: Cooperative binding of isolated subdomains and effects of covalent linkage
    • J. D. Klemm C. O. Pabo Oct-1 POU domain DNA interactions: cooperative binding of isolated subdomains and effects of covalent linkage Genes Dev. 1996 10 27 36 (Pubitemid 26025296)
    • (1996) Genes and Development , vol.10 , Issue.1 , pp. 27-36
    • Klemm, J.D.1    Pabo, C.O.2
  • 70
    • 78650453629 scopus 로고    scopus 로고
    • DNA search efficiency is modulated by charge composition and distribution in the intrinsically disordered tail
    • D. Vuzman Y. Levy DNA search efficiency is modulated by charge composition and distribution in the intrinsically disordered tail Proc. Natl. Acad. Sci. U. S. A. 2010 107 21004 21009
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 21004-21009
    • Vuzman, D.1    Levy, Y.2
  • 71
    • 77958168396 scopus 로고    scopus 로고
    • Facilitated DNA search by multidomain transcription factors: Cross talk via a flexible linker
    • D. Vuzman M. Polonsky Y. Levy Facilitated DNA search by multidomain transcription factors: cross talk via a flexible linker Biophys. J. 2010 99 1202 1211
    • (2010) Biophys. J. , vol.99 , pp. 1202-1211
    • Vuzman, D.1    Polonsky, M.2    Levy, Y.3
  • 73
    • 33646356250 scopus 로고    scopus 로고
    • Detecting transient intermediates in macromolecular binding by paramagnetic NMR
    • J. Iwahara G. M. Clore Detecting transient intermediates in macromolecular binding by paramagnetic NMR Nature 2006 440 1227 1230
    • (2006) Nature , vol.440 , pp. 1227-1230
    • Iwahara, J.1    Clore, G.M.2
  • 74
    • 31544448614 scopus 로고    scopus 로고
    • Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy
    • DOI 10.1021/ja056786o
    • J. Iwahara G. M. Clore Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy J. Am. Chem. Soc. 2006 128 404 405 (Pubitemid 43157521)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.2 , pp. 404-405
    • Iwahara, J.1    Clore, G.M.2
  • 75
    • 36048978623 scopus 로고    scopus 로고
    • How a protein searches for its specific site on DNA: The role of intersegment transfer
    • T. Hu B. I. Shklovskii How a protein searches for its specific site on DNA: the role of intersegment transfer Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. 2007 76 051909
    • (2007) Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. , vol.76 , pp. 051909
    • Hu, T.1    Shklovskii, B.I.2
  • 76
    • 60849133933 scopus 로고    scopus 로고
    • The effects of intersegmental transfers on target location by proteins
    • M. Sheinman Y. Kafri The effects of intersegmental transfers on target location by proteins Phys. Biol. 2009 6 016003-1 016003-17
    • (2009) Phys. Biol. , vol.6 , pp. 0160031-01600317
    • Sheinman, M.1    Kafri, Y.2
  • 78
    • 52949100201 scopus 로고    scopus 로고
    • Global jumping and domain-specific intersegment transfer between DNA cognate sites of the multidomain transcription factor Oct-1
    • M. Doucleff G. M. Clore Global jumping and domain-specific intersegment transfer between DNA cognate sites of the multidomain transcription factor Oct-1 Proc. Natl. Acad. Sci. U. S. A. 2008 105 13871 13876
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13871-13876
    • Doucleff, M.1    Clore, G.M.2
  • 79
    • 42949161558 scopus 로고    scopus 로고
    • Binding-induced folding of a natively unstructured transcription factor
    • A. G. Turjanski J. S. Gutkind R. B. Best G. Hummer Binding-induced folding of a natively unstructured transcription factor PLoS Comput. Biol. 2008 4 e1000060
    • (2008) PLoS Comput. Biol. , vol.4 , pp. 1000060
    • Turjanski, A.G.1    Gutkind, J.S.2    Best, R.B.3    Hummer, G.4
  • 80
    • 67949106402 scopus 로고    scopus 로고
    • Intrinsically Disordered p53 Extreme C-Terminus Binds to S100B(beta beta) through "fly-Casting"
    • J. H. Chen Intrinsically Disordered p53 Extreme C-Terminus Binds to S100B(beta beta) through "Fly-Casting" J. Am. Chem. Soc. 2009 131 2088 2089
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2088-2089
    • Chen, J.H.1
  • 81
    • 79952489792 scopus 로고    scopus 로고
    • Topology-based modeling of intrinsically disordered proteins: Balancing intrinsic structural propensities and intermolecular interactions
    • D. Ganguly J. Chen Topology-based modeling of intrinsically disordered proteins: balancing intrinsic structural propensities and intermolecular interactions Proteins: Struct., Funct., Bioinf. 2011 79 1251 1266
    • (2011) Proteins: Struct., Funct., Bioinf. , vol.79 , pp. 1251-1266
    • Ganguly, D.1    Chen, J.2
  • 82
    • 78650988465 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in a physics-based world
    • T. Click D. Ganguly J. Chen Intrinsically disordered proteins in a physics-based world Int. J. Mol. Sci. 2010 11 5292 5309
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 5292-5309
    • Click, T.1    Ganguly, D.2    Chen, J.3
  • 83
    • 70349442548 scopus 로고    scopus 로고
    • The first 30 years of p53: Growing ever more complex
    • A. J. Levine M. Oren The first 30 years of p53: growing ever more complex Nat. Rev. Cancer 2009 9 749 758
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 749-758
    • Levine, A.J.1    Oren, M.2
  • 84
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the Light: The Growing Complexity of p53
    • K. H. Vousden C. Prives Blinded by the Light: The Growing Complexity of p53 Cell 2009 137 413 431
    • (2009) Cell , vol.137 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 85
    • 0034862475 scopus 로고    scopus 로고
    • The C-terminus of p53: The more you learn the less you know
    • DOI 10.1038/nsb0901-730
    • J. Ahn C. Prives The C-terminus of p53: the more you learn the less you know Nat. Struct. Biol. 2001 8 730 732 (Pubitemid 32803581)
    • (2001) Nature Structural Biology , vol.8 , Issue.9 , pp. 730-732
    • Ahn, J.1    Prives, C.2
  • 87
    • 8644241631 scopus 로고    scopus 로고
    • P53 linear diffusion along DNA requires its C terminus
    • DOI 10.1016/j.molcel.2004.09.032, PII S1097276504005842
    • K. McKinney M. Mattia V. Gottifredi C. Prives p53 linear diffusion along DNA requires its C terminus Mol. Cell 2004 16 413 424 (Pubitemid 39504795)
    • (2004) Molecular Cell , vol.16 , Issue.3 , pp. 413-424
    • McKinney, K.1    Mattia, M.2    Gottifredi, V.3    Prives, C.4
  • 88
    • 79953695332 scopus 로고    scopus 로고
    • Sliding of p53 along DNA Can Be Modulated by Its Oligomeric State and by Cross-Talks between Its Constituent Domains
    • N. Khazanov Y. Levy Sliding of p53 along DNA Can Be Modulated by Its Oligomeric State and by Cross-Talks between Its Constituent Domains J. Mol. Biol. 2011 408 335 355
    • (2011) J. Mol. Biol. , vol.408 , pp. 335-355
    • Khazanov, N.1    Levy, Y.2
  • 91
    • 49149090309 scopus 로고    scopus 로고
    • P53-induced DNA bending: The interplay between p53-ONA and p53-p53 interactions
    • Y. P. Pan R. Nussinov P53-induced DNA bending: the interplay between p53-ONA and p53-p53 interactions J. Phys. Chem. B 2008 112 6716 6724
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6716-6724
    • Pan, Y.P.1    Nussinov, R.2
  • 92
    • 82655188435 scopus 로고    scopus 로고
    • Structural basis for specific p53 binding-induced DNA bending
    • Y. P. Pan R. Nussinov Structural basis for specific p53 binding-induced DNA bending Biophys. J. 2007 233a
    • (2007) Biophys. J.
    • Pan, Y.P.1    Nussinov, R.2
  • 94
    • 82655181393 scopus 로고    scopus 로고
    • Modulating Protein-DNA Interactions by Post-Translational Modifications at Disordered Regions, submitted
    • D. Vuzman, Y. Hoffman, Y. Levy, Modulating Protein-DNA Interactions by Post-Translational Modifications at Disordered Regions, submitted
    • Vuzman, D.1    Hoffman, Y.2    Levy, Y.3
  • 96
    • 0037436383 scopus 로고    scopus 로고
    • Allosteric regulation of the transcription factor NFAT1 by multiple phosphorylation sites: A mathematical analysis
    • DOI 10.1016/S0022-2836(03)00085-8
    • C. Salazar T. Hofer Allosteric regulation of the transcription factor NFAT1 by multiple phosphorylation sites: a mathematical analysis J. Mol. Biol. 2003 327 31 45 (Pubitemid 36293301)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.1 , pp. 31-45
    • Salazar, C.1    Hofer, T.2
  • 97
    • 0037462424 scopus 로고    scopus 로고
    • Cdc4 ubiquitin ligase
    • DOI 10.1016/S0092-8674(03)00034-5
    • S. Orlicky X. J. Tang A. Willems M. Tyers F. Sicheri Structural basis for phospho-dependent substrate selection and orientation by the SCF(Cdc4) ubiquitin ligase Cell 2003 112 243 256 (Pubitemid 36144113)
    • (2003) Cell , vol.112 , Issue.2 , pp. 243-256
    • Orlicky, S.1    Tang, X.2    Willems, A.3    Tyers, M.4    Sicheri, F.5
  • 98
    • 21744436606 scopus 로고    scopus 로고
    • Biochemistry: Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region
    • DOI 10.1126/science.1111915
    • M. A. Pufall G. M. Lee M. L. Nelson H. S. Kang A. Velyvis L. E. Kay L. P. McIntosh B. J. Graves Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region Science 2005 309 142 145 (Pubitemid 40934995)
    • (2005) Science , vol.309 , Issue.5731 , pp. 142-145
    • Pufall, M.A.1    Lee, G.M.2    Nelson, M.L.3    Kang, H.-S.4    Velyvis, A.5    Kay, L.E.6    McIntosh, L.P.7    Graves, B.J.8
  • 99
    • 69949134806 scopus 로고    scopus 로고
    • Phosphorylated Intrinsically Disordered Region of FACT Masks Its Nucleosomal DNA Binding Elements
    • K. Morikawa Y. Tsunaka J. Toga H. Yamaguchi S. Tate S. Hirose Phosphorylated Intrinsically Disordered Region of FACT Masks Its Nucleosomal DNA Binding Elements J. Biol. Chem. 2009 284 24610 24621
    • (2009) J. Biol. Chem. , vol.284 , pp. 24610-24621
    • Morikawa, K.1    Tsunaka, Y.2    Toga, J.3    Yamaguchi, H.4    Tate, S.5    Hirose, S.6
  • 100
    • 33745116557 scopus 로고    scopus 로고
    • Gradual phosphorylation regulates PC4 coactivator function
    • DOI 10.1111/j.1742-4658.2006.05165.x
    • H. R. A. Jonker R. W. Wechselberger M. Pinkse R. Kaptein G. E. Folkers Gradual phosphorylation regulates PC4 coactivator function FEBS J. 2006 273 1430 1444 (Pubitemid 44055059)
    • (2006) FEBS Journal , vol.273 , Issue.7 , pp. 1430-1444
    • Jonker, H.R.A.1    Wechselberger, R.W.2    Pinkse, M.3    Kaptein, R.4    Folkers, G.E.5
  • 101
    • 4944255743 scopus 로고    scopus 로고
    • Post-translational modification of p53 in tumorigenesis
    • DOI 10.1038/nrc1455
    • A. M. Bode Z. G. Dong Post-translational modification of p53 in tumorigenesis Nat. Rev. Cancer 2004 4 793 805 (Pubitemid 39331151)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.10 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 102
    • 0033027346 scopus 로고    scopus 로고
    • Covalent and noncovalent modifiers of the p53 protein
    • DOI 10.1007/s000180050271
    • L. Jayaraman C. Prives Covalent and noncovalent modifiers of the p53 protein Cell. Mol. Life Sci. 1999 55 76 87 (Pubitemid 29077856)
    • (1999) Cellular and Molecular Life Sciences , vol.55 , Issue.1 , pp. 76-87
    • Jayaraman, L.1    Prives, C.2
  • 103
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • DOI 10.1046/j.1432-1327.2001.02225.x
    • E. Appella C. W. Anderson Post-translational modifications and activation of p53 by genotoxic stresses Eur. J. Biochem. 2001 268 2764 2772 (Pubitemid 32862957)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.10 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 104
    • 0037737758 scopus 로고    scopus 로고
    • Regulation of p53 responses by post-translational modifications
    • X. Yang Regulation of p53 responses by post-translational modifications Cell Death Differ. 2003 10 400 403
    • (2003) Cell Death Differ. , vol.10 , pp. 400-403
    • Yang, X.1
  • 106
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • DOI 10.1016/S0092-8674(00)80521-8
    • W. Gu R. G. Roeder Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain Cell 1997 90 595 606 (Pubitemid 27357952)
    • (1997) Cell , vol.90 , Issue.4 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 107
    • 0026448672 scopus 로고
    • Regulation of the Specific DNA-Binding Function of P53
    • T. R. Hupp D. W. Meek C. A. Midgley D. P. Lane Regulation of the Specific DNA-Binding Function of P53 Cell 1992 71 875 886
    • (1992) Cell , vol.71 , pp. 875-886
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 111
  • 112
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • DOI 10.1016/S0092-8674(00)81958-3
    • R. D. Kornberg Y. L. Lorch Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome Cell 1999 98 285 294 (Pubitemid 29380564)
    • (1999) Cell , vol.98 , Issue.3 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 113
    • 0001932547 scopus 로고
    • ed. A. Rich
    • K. E. van Holde, Chromatin, ed., A. Rich, 1988, pp. 111-148
    • (1988) Chromatin , pp. 111-148
    • Van Holde, K.E.1
  • 114
    • 0037385490 scopus 로고    scopus 로고
    • Structures and interactions of the core histone tail domains
    • DOI 10.1002/bip.10303
    • C. Y. Zheng J. J. Hayes Structures and interactions of the core histone tail domains Biopolymers 2003 68 539 546 (Pubitemid 36432066)
    • (2003) Biopolymers , vol.68 , Issue.4 , pp. 539-546
    • Zheng, C.1    Hayes, J.J.2
  • 115
    • 0020185003 scopus 로고
    • Effect of Acetylation on the Binding of N-Terminal Peptides of Histone-H4 to DNA
    • P. D. Cary C. Cranerobinson E. M. Bradbury G. H. Dixon Effect of Acetylation on the Binding of N-Terminal Peptides of Histone-H4 to DNA Eur. J. Biochem. 1982 127 137 143
    • (1982) Eur. J. Biochem. , vol.127 , pp. 137-143
    • Cary, P.D.1    Cranerobinson, C.2    Bradbury, E.M.3    Dixon, G.H.4
  • 116
    • 0023039170 scopus 로고
    • Lysine-containing DNA-binding regions on the surface of the histone octamer in the nucleosome core particle
    • DOI 10.1111/j.1432-1033.1986.tb09957.x
    • S. F. Lambert J. O. Thomas Lysine-Containing DNA-Binding Regions on the Surface of the Histone Octamer in the Nucleosome Core Particle Eur. J. Biochem. 1986 160 191 201 (Pubitemid 17177463)
    • (1986) European Journal of Biochemistry , vol.160 , Issue.1 , pp. 191-201
    • Lambert, S.F.1    Thomas, J.O.2
  • 117
    • 0025056959 scopus 로고
    • Core histone-DNA interactions in sea urchin sperm chromatin. The N-terminal tail of H2B interacts with linker DNA
    • DOI 10.1111/j.1432-1033.1990.tb15288.x
    • C. Hill J. Thomas Core histone-DNA interactions in Sea-Urchin sperm chromatin- the N-terminal tail of H2b interacts with linker DNA Eur. J. Biochem. 1990 187 145 153 (Pubitemid 20040371)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.1 , pp. 145-153
    • Hill, C.S.1    Thomas, J.O.2
  • 118
    • 0036211013 scopus 로고    scopus 로고
    • Histone acetylation: A switch between repressive and permissive chromatin. Second in review on chromatin dynamics
    • DOI 10.1093/embo-reports/kvf053
    • A. Eberharter P. B. Becker Histone acetylation: a switch between repressive and permissive chromatin - second in review series on chromatin dynamics EMBO Rep. 2002 3 224 229 (Pubitemid 34269514)
    • (2002) EMBO Reports , vol.3 , Issue.3 , pp. 224-229
    • Eberharter, A.1    Becker, P.B.2
  • 119
    • 0035814925 scopus 로고    scopus 로고
    • Chromatin remodeling enzymes: Who's on first?
    • DOI 10.1016/S0960-9822(01)00090-2
    • C. Fry C. Peterson Chromatin remodeling enzymes: who's on first? Curr. Biol. 2001 11 R185 R197 (Pubitemid 32200731)
    • (2001) Current Biology , vol.11 , Issue.5
    • Fry, C.J.1    Peterson, C.L.2
  • 121
    • 0033080794 scopus 로고    scopus 로고
    • Chromatin disruption and modification
    • DOI 10.1093/nar/27.3.711
    • A. P. Wolffe J. J. Hayes Chromatin disruption and modification Nucleic Acids Res. 1999 27 711 720 (Pubitemid 29209356)
    • (1999) Nucleic Acids Research , vol.27 , Issue.3 , pp. 711-720
    • Wolffe, A.P.1    Hayes, J.J.2
  • 122
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • DOI 10.1038/47412
    • B. D. Strahl C. D. Allis The language of covalent histone modifications Nature 2000 403 41 45 (Pubitemid 30038513)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 123
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • T. Jenuwein C. D. Allis Translating the histone code Science 2001 293 1074 1080 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 125
    • 0035816218 scopus 로고    scopus 로고
    • Domain combinations in archaeal, eubacterial and eukaryotic proteomes
    • DOI 10.1006/jmbi.2001.4776
    • G. Apic J. Gough S. A. Teichmann Domain combinations in archaeal, eubacterial and eukaryotic proteomes J. Mol. Biol. 2001 310 311 325 (Pubitemid 32664871)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.2 , pp. 311-325
    • Apic, G.1    Gough, J.2    Teichmann, S.A.3
  • 126
    • 0035909804 scopus 로고    scopus 로고
    • The affinity-enhancing roles of flexible linkers in two-domain DNA-Binding proteins
    • H. X. Zhou The affinity-enhancing roles of flexible linkers in two-domain DNA-Binding proteins Biochemistry 2001 40 15069 15073
    • (2001) Biochemistry , vol.40 , pp. 15069-15073
    • Zhou, H.X.1
  • 127
    • 0034657645 scopus 로고    scopus 로고
    • Thermodynamics of DNA binding of MM17, a 'single chain dimer' of transcription factor MASH-1
    • M. Sieber R. K. Allemann Thermodynamics of DNA binding of MM17, a 'single chain dimer' of transcription factor MASH-1 Nucleic Acids Res. 2000 28 2122 2127 (Pubitemid 30255534)
    • (2000) Nucleic Acids Research , vol.28 , Issue.10 , pp. 2122-2127
    • Sieber, M.1    Allemann, R.K.2
  • 128
    • 0034804243 scopus 로고    scopus 로고
    • Single-chain versus dimeric protein folding: Thermodynamic and kinetic consequences of covalent linkage
    • H. X. Zhou Single-chain versus dimeric protein folding: thermodynamic and kinetic consequences of covalent linkage J. Am. Chem. Soc. 2001 123 6730 6731
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6730-6731
    • Zhou, H.X.1
  • 129
    • 34047224955 scopus 로고    scopus 로고
    • Structure-function-rescue: The diverse nature of common p53 cancer mutants
    • DOI 10.1038/sj.onc.1210291, PII 1210291
    • A. C. Joerger A. R. Fersht Structure-function-rescue: the diverse nature of common p53 cancer mutants Oncogene 2007 26 2226 2242 (Pubitemid 46536643)
    • (2007) Oncogene , vol.26 , Issue.15 , pp. 2226-2242
    • Joerger, A.C.1    Fersht, A.R.2
  • 130
    • 0030937754 scopus 로고    scopus 로고
    • Linker length and composition influence the flexibility of Oct-1 DNA binding
    • DOI 10.1093/emboj/16.8.2043
    • H. C. vanLeeuwen M. J. Strating M. Rensen W. deLaat P. C. vanderVliet Linker length and composition influence the flexibility of Oct-1 DNA binding EMBO J. 1997 16 2043 2053 (Pubitemid 27170965)
    • (1997) EMBO Journal , vol.16 , Issue.8 , pp. 2043-2053
    • Van Leeuwen, H.C.1    Strating, M.J.2    Rensen, M.3    De Laat, W.4    Van Der Vliet, P.C.5
  • 131
    • 17544381252 scopus 로고    scopus 로고
    • NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain
    • DOI 10.1093/nar/gki336
    • P. D. Vise B. Baral A. J. Latos G. W. Daughdrill NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain Nucleic Acids Res. 2005 33 2061 2077 (Pubitemid 41439875)
    • (2005) Nucleic Acids Research , vol.33 , Issue.7 , pp. 2061-2077
    • Vise, P.D.1    Baral, B.2    Latos, A.J.3    Daughdrill, G.W.4
  • 132
    • 77956572160 scopus 로고    scopus 로고
    • NMR Studies of Translocation of the Zif268 Protein between Its Target DNA Sites
    • Y. Takayama D. Sahu J. Iwahara NMR Studies of Translocation of the Zif268 Protein between Its Target DNA Sites Biochemistry 2010 49 7998 8005
    • (2010) Biochemistry , vol.49 , pp. 7998-8005
    • Takayama, Y.1    Sahu, D.2    Iwahara, J.3
  • 133
    • 79959360942 scopus 로고    scopus 로고
    • Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR
    • Y. Takayama G. M. Clore Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR Proc. Natl. Acad. Sci. U. S. A. 2011 108 E169 E176
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108
    • Takayama, Y.1    Clore, G.M.2


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