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Volumn 283, Issue 4, 2016, Pages 576-594

Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions

Author keywords

deletion variants; excluded volume; intrinsically disordered proteins; partner binding; split GFP

Indexed keywords

HEAT SHOCK PROTEIN 70; INTRINSICALLY DISORDERED PROTEIN; NUCLEOPROTEIN; PHOSPHOPROTEIN; PROTEIN BINDING;

EID: 84958945587     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13631     Document Type: Article
Times cited : (40)

References (82)
  • 2
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright PE, &, Dyson HJ, (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 293, 321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 5
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky VN, Oldfield CJ, &, Dunker AK, (2005) Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18, 343-384.
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 6
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, &, Wright PE, (2002) Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 12, 54-60.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 7
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, &, Wright PE, (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6, 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 8
    • 84903957091 scopus 로고    scopus 로고
    • Introducing protein intrinsic disorder
    • Habchi J, Tompa P, Longhi S, &, Uversky VN, (2014) Introducing protein intrinsic disorder. Chem Rev 114, 6561-6588.
    • (2014) Chem Rev , vol.114 , pp. 6561-6588
    • Habchi, J.1    Tompa, P.2    Longhi, S.3    Uversky, V.N.4
  • 10
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    • Tompa P, &, Fuxreiter M, (2008) Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 33, 2-8.
    • (2008) Trends Biochem Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 11
    • 58149215982 scopus 로고    scopus 로고
    • Fuzzy interactome: the limitations of models in molecular biology
    • Fuxreiter M, &, Tompa P, (2009) Fuzzy interactome: the limitations of models in molecular biology. Trends Biochem Sci 34, 3.
    • (2009) Trends Biochem Sci , vol.34 , pp. 3
    • Fuxreiter, M.1    Tompa, P.2
  • 12
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: linking regulation to protein dynamics
    • Fuxreiter M, (2012) Fuzziness: linking regulation to protein dynamics. Mol BioSyst 8, 168-177.
    • (2012) Mol BioSyst , vol.8 , pp. 168-177
    • Fuxreiter, M.1
  • 14
    • 80053441923 scopus 로고    scopus 로고
    • Dynamic protein-DNA recognition: beyond what can be seen
    • Fuxreiter M, Simon I, &, Bondos S, (2011) Dynamic protein-DNA recognition: beyond what can be seen. Trends Biochem Sci 36, 415-423.
    • (2011) Trends Biochem Sci , vol.36 , pp. 415-423
    • Fuxreiter, M.1    Simon, I.2    Bondos, S.3
  • 15
    • 84856694618 scopus 로고    scopus 로고
    • Coupled folding-binding in a hydrophobic/polar protein model: impact of synergistic folding and disordered flanks
    • Bhattacherjee A, &, Wallin S, (2012) Coupled folding-binding in a hydrophobic/polar protein model: impact of synergistic folding and disordered flanks. Biophys J 102, 569-578.
    • (2012) Biophys J , vol.102 , pp. 569-578
    • Bhattacherjee, A.1    Wallin, S.2
  • 16
    • 0035929161 scopus 로고    scopus 로고
    • AFM force measurements on microtubule-associated proteins: the projection domain exerts a long-range repulsive force
    • Mukhopadhyay R, &, Hoh JH, (2001) AFM force measurements on microtubule-associated proteins: the projection domain exerts a long-range repulsive force. FEBS Lett 505, 374-378.
    • (2001) FEBS Lett , vol.505 , pp. 374-378
    • Mukhopadhyay, R.1    Hoh, J.H.2
  • 18
    • 34447536953 scopus 로고    scopus 로고
    • Intrinsic disorder and autonomous domain function in the multifunctional nuclear protein, MeCP2
    • Adams VH, McBryant SJ, Wade PA, Woodcock CL, &, Hansen JC, (2007) Intrinsic disorder and autonomous domain function in the multifunctional nuclear protein, MeCP2. J Biol Chem 282, 15057-15064.
    • (2007) J Biol Chem , vol.282 , pp. 15057-15064
    • Adams, V.H.1    McBryant, S.J.2    Wade, P.A.3    Woodcock, C.L.4    Hansen, J.C.5
  • 19
    • 45749124759 scopus 로고    scopus 로고
    • The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding
    • Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, &, Benecke A, (2008) The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. Biochemistry 47, 6519-6530.
    • (2008) Biochemistry , vol.47 , pp. 6519-6530
    • Smet-Nocca, C.1    Wieruszeski, J.M.2    Chaar, V.3    Leroy, A.4    Benecke, A.5
  • 20
    • 77749322192 scopus 로고    scopus 로고
    • The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a 'fuzzy' complex upon DNA binding
    • Aguado-Llera D, Goormaghtigh E, de Geest N, Quan XJ, Prieto A, Hassan BA, Gomez J, &, Neira JL, (2010) The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a 'fuzzy' complex upon DNA binding. Biochemistry 49, 1577-1589.
    • (2010) Biochemistry , vol.49 , pp. 1577-1589
    • Aguado-Llera, D.1    Goormaghtigh, E.2    De Geest, N.3    Quan, X.J.4    Prieto, A.5    Hassan, B.A.6    Gomez, J.7    Neira, J.L.8
  • 21
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • Longhi S, Receveur-Brechot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, &, Canard B, (2003) The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. J Biol Chem 278, 18638-18648.
    • (2003) J Biol Chem , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3    Johansson, K.4    Darbon, H.5    Bhella, D.6    Yeo, R.7    Finet, S.8    Canard, B.9
  • 22
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • Bourhis J, Johansson K, Receveur-Bréchot V, Oldfield CJ, Dunker AK, Canard B, &, Longhi S, (2004) The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. Virus Res 99, 157-167.
    • (2004) Virus Res , vol.99 , pp. 157-167
    • Bourhis, J.1    Johansson, K.2    Receveur-Bréchot, V.3    Oldfield, C.J.4    Dunker, A.K.5    Canard, B.6    Longhi, S.7
  • 23
    • 23644449725 scopus 로고    scopus 로고
    • The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded
    • Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, &, Longhi S, (2005) The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. Protein Sci 14, 1975-1992.
    • (2005) Protein Sci , vol.14 , pp. 1975-1992
    • Bourhis, J.M.1    Receveur-Bréchot, V.2    Oglesbee, M.3    Zhang, X.4    Buccellato, M.5    Darbon, H.6    Canard, B.7    Finet, S.8    Longhi, S.9
  • 24
    • 84866614430 scopus 로고    scopus 로고
    • Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site
    • Blocquel D, Habchi J, Costanzo S, Doizy A, Oglesbee M, &, Longhi S, (2012) Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site. Protein Sci 21, 1577-1585.
    • (2012) Protein Sci , vol.21 , pp. 1577-1585
    • Blocquel, D.1    Habchi, J.2    Costanzo, S.3    Doizy, A.4    Oglesbee, M.5    Longhi, S.6
  • 26
    • 82655175457 scopus 로고    scopus 로고
    • Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies
    • Blocquel D, Habchi J, Gruet A, Blangy S, &, Longhi S, (2012) Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies. Mol BioSyst 8, 392-410.
    • (2012) Mol BioSyst , vol.8 , pp. 392-410
    • Blocquel, D.1    Habchi, J.2    Gruet, A.3    Blangy, S.4    Longhi, S.5
  • 29
    • 84920758588 scopus 로고    scopus 로고
    • Dynamics of the intrinsically disordered C-terminal domain of the Nipah virus nucleoprotein and interaction with the X domain of the phosphoprotein as unveiled by NMR spectroscopy
    • Baronti L, Erales J, Habchi J, Felli IC, Pierattelli R, &, Longhi S, (2015) Dynamics of the intrinsically disordered C-terminal domain of the Nipah virus nucleoprotein and interaction with the X domain of the phosphoprotein as unveiled by NMR spectroscopy. ChemBioChem 16, 268-276.
    • (2015) ChemBioChem , vol.16 , pp. 268-276
    • Baronti, L.1    Erales, J.2    Habchi, J.3    Felli, I.C.4    Pierattelli, R.5    Longhi, S.6
  • 30
    • 0242582329 scopus 로고    scopus 로고
    • Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
    • Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, &, Longhi S, (2003) Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J Biol Chem 278, 44567-44573.
    • (2003) J Biol Chem , vol.278 , pp. 44567-44573
    • Johansson, K.1    Bourhis, J.M.2    Campanacci, V.3    Cambillau, C.4    Canard, B.5    Longhi, S.6
  • 32
    • 58149279796 scopus 로고    scopus 로고
    • Mapping α-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy
    • Belle V, Rouger S, Costanzo S, Liquiere E, Strancar J, Guigliarelli B, Fournel A, &, Longhi S, (2008) Mapping α-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy. Proteins 73, 973-988.
    • (2008) Proteins , vol.73 , pp. 973-988
    • Belle, V.1    Rouger, S.2    Costanzo, S.3    Liquiere, E.4    Strancar, J.5    Guigliarelli, B.6    Fournel, A.7    Longhi, S.8
  • 33
    • 63149095444 scopus 로고    scopus 로고
    • Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR
    • Bernard C, Gely S, Bourhis JM, Morelli X, Longhi S, &, Darbon H, (2009) Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR. FEBS Lett 583, 1084-1089.
    • (2009) FEBS Lett , vol.583 , pp. 1084-1089
    • Bernard, C.1    Gely, S.2    Bourhis, J.M.3    Morelli, X.4    Longhi, S.5    Darbon, H.6
  • 34
    • 77956578649 scopus 로고    scopus 로고
    • Probing structural transitions in the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by vibrational spectroscopy of cyanylated cysteines
    • Bischak CG, Longhi S, Snead DM, Costanzo S, Terrer E, &, Londergan CH, (2010) Probing structural transitions in the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by vibrational spectroscopy of cyanylated cysteines. Biophys J 99, 1676-1683.
    • (2010) Biophys J , vol.99 , pp. 1676-1683
    • Bischak, C.G.1    Longhi, S.2    Snead, D.M.3    Costanzo, S.4    Terrer, E.5    Londergan, C.H.6
  • 35
    • 77955378293 scopus 로고    scopus 로고
    • Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein
    • Gely S, Lowry DF, Bernard C, Ringkjobing-Jensen M, Blackledge M, Costanzo S, Darbon H, Daughdrill GW, &, Longhi S, (2010) Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein. J Mol Recognit 23, 435-447.
    • (2010) J Mol Recognit , vol.23 , pp. 435-447
    • Gely, S.1    Lowry, D.F.2    Bernard, C.3    Ringkjobing-Jensen, M.4    Blackledge, M.5    Costanzo, S.6    Darbon, H.7    Daughdrill, G.W.8    Longhi, S.9
  • 39
    • 84885065793 scopus 로고    scopus 로고
    • Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein
    • Wang Y, Chu X, Longhi S, Roche P, Han W, Wang E, &, Wang J, (2013) Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein. Proc Natl Acad Sci USA 110, E3743-E3752.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E3743-E3752
    • Wang, Y.1    Chu, X.2    Longhi, S.3    Roche, P.4    Han, W.5    Wang, E.6    Wang, J.7
  • 40
  • 41
    • 84859499620 scopus 로고    scopus 로고
    • TAIL-XD complex: an illustrative example of fuzziness
    • TAIL-XD complex: an illustrative example of fuzziness. Adv Exp Med Biol 725, 126-141.
    • (2012) Adv Exp Med Biol , vol.725 , pp. 126-141
    • Longhi, S.1
  • 42
    • 24144454858 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with GFP-fragment reassembly
    • Wilson CG, Magliery TJ, &, Regan L, (2004) Detecting protein-protein interactions with GFP-fragment reassembly. Nat Methods 1, 255-262.
    • (2004) Nat Methods , vol.1 , pp. 255-262
    • Wilson, C.G.1    Magliery, T.J.2    Regan, L.3
  • 43
    • 84883289774 scopus 로고    scopus 로고
    • Dissecting partner recognition by an intrinsically disordered protein using descriptive random mutagenesis
    • Gruet A, Dosnon M, Vassena A, Lombard V, Gerlier D, Bignon C, &, Longhi S, (2013) Dissecting partner recognition by an intrinsically disordered protein using descriptive random mutagenesis. J Mol Biol 425, 3495-3509.
    • (2013) J Mol Biol , vol.425 , pp. 3495-3509
    • Gruet, A.1    Dosnon, M.2    Vassena, A.3    Lombard, V.4    Gerlier, D.5    Bignon, C.6    Longhi, S.7
  • 45
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism
    • Magliery TJ, Wilson CG, Pan W, Mishler D, Ghosh I, Hamilton AD, &, Regan L, (2005) Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. J Am Chem Soc 127, 146-157.
    • (2005) J Am Chem Soc , vol.127 , pp. 146-157
    • Magliery, T.J.1    Wilson, C.G.2    Pan, W.3    Mishler, D.4    Ghosh, I.5    Hamilton, A.D.6    Regan, L.7
  • 46
    • 0034711421 scopus 로고    scopus 로고
    • The effect of the acidic tail on the DNA-binding properties of the HMG1,2 class of proteins: insights from tail switching and tail removal
    • Lee KB, &, Thomas JO, (2000) The effect of the acidic tail on the DNA-binding properties of the HMG1,2 class of proteins: insights from tail switching and tail removal. J Mol Biol 304, 135-149.
    • (2000) J Mol Biol , vol.304 , pp. 135-149
    • Lee, K.B.1    Thomas, J.O.2
  • 47
    • 84885648103 scopus 로고    scopus 로고
    • The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity
    • Krumm SA, Takeda M, &, Plemper RK, (2013) The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity. J Biol Chem 288, 29943-29953.
    • (2013) J Biol Chem , vol.288 , pp. 29943-29953
    • Krumm, S.A.1    Takeda, M.2    Plemper, R.K.3
  • 48
    • 82655179925 scopus 로고    scopus 로고
    • Structural disorder within paramyxovirus nucleoproteins and phosphoproteins
    • Habchi J, &, Longhi S, (2012) Structural disorder within paramyxovirus nucleoproteins and phosphoproteins. Mol BioSyst 8, 69-81.
    • (2012) Mol BioSyst , vol.8 , pp. 69-81
    • Habchi, J.1    Longhi, S.2
  • 49
    • 84939561035 scopus 로고    scopus 로고
    • Structural disorder within paramyxoviral nucleoproteins and phosphoproteins in their free and bound forms: from predictions to experimental assessment
    • Habchi J, &, Longhi S, (2015) Structural disorder within paramyxoviral nucleoproteins and phosphoproteins in their free and bound forms: from predictions to experimental assessment. Int J Mol Sci 16, 15688-15726.
    • (2015) Int J Mol Sci , vol.16 , pp. 15688-15726
    • Habchi, J.1    Longhi, S.2
  • 50
    • 84942293554 scopus 로고    scopus 로고
    • Structural disorder within paramyxoviral nucleoproteins
    • Longhi S, (2015) Structural disorder within paramyxoviral nucleoproteins. FEBS Lett 589, 2649-2659.
    • (2015) FEBS Lett , vol.589 , pp. 2649-2659
    • Longhi, S.1
  • 54
    • 36249025734 scopus 로고    scopus 로고
    • Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach
    • Watson M, Stott K, &, Thomas JO, (2007) Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach. J Mol Biol 374, 1286-1297.
    • (2007) J Mol Biol , vol.374 , pp. 1286-1297
    • Watson, M.1    Stott, K.2    Thomas, J.O.3
  • 55
    • 77955399035 scopus 로고    scopus 로고
    • Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment
    • Habchi J, Mamelli L, Darbon H, &, Longhi S, (2010) Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. PLoS One 5, e11684.
    • (2010) PLoS One , vol.5
    • Habchi, J.1    Mamelli, L.2    Darbon, H.3    Longhi, S.4
  • 56
    • 84879206318 scopus 로고    scopus 로고
    • Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site directed spin labeling EPR spectroscopy
    • Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, &, Longhi S, (2013) Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site directed spin labeling EPR spectroscopy. J Biomol Struct Dyn 31, 453-471.
    • (2013) J Biomol Struct Dyn , vol.31 , pp. 453-471
    • Martinho, M.1    Habchi, J.2    El Habre, Z.3    Nesme, L.4    Guigliarelli, B.5    Belle, V.6    Longhi, S.7
  • 57
    • 73149092964 scopus 로고    scopus 로고
    • High local concentration: a fundamental strategy of life
    • Oehler S, &, Muller-Hill B, (2010) High local concentration: a fundamental strategy of life. J Mol Biol 395, 242-253.
    • (2010) J Mol Biol , vol.395 , pp. 242-253
    • Oehler, S.1    Muller-Hill, B.2
  • 58
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy I, &, Michnick SW, (2006) A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat Methods 3, 977-979.
    • (2006) Nat Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 59
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky VN, (2002) What does it mean to be natively unfolded? Eur J Biochem 269, 2-12.
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 60
    • 58549094957 scopus 로고    scopus 로고
    • Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder
    • Lu X, Hamkalo B, Parseghian MH, &, Hansen JC, (2009) Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry 48, 164-172.
    • (2009) Biochemistry , vol.48 , pp. 164-172
    • Lu, X.1    Hamkalo, B.2    Parseghian, M.H.3    Hansen, J.C.4
  • 62
    • 80052021703 scopus 로고    scopus 로고
    • Kinetic recognition of the retinoblastoma tumor suppressor by a specific protein target
    • Chemes LB, Sanchez IE, &, de Prat-Gay G, (2011) Kinetic recognition of the retinoblastoma tumor suppressor by a specific protein target. J Mol Biol 412, 267-284.
    • (2011) J Mol Biol , vol.412 , pp. 267-284
    • Chemes, L.B.1    Sanchez, I.E.2    De Prat-Gay, G.3
  • 63
    • 84865689638 scopus 로고    scopus 로고
    • Electrostatically accelerated coupled binding and folding of intrinsically disordered proteins
    • Ganguly D, Otieno S, Waddell B, Iconaru L, Kriwacki RW, &, Chen J, (2012) Electrostatically accelerated coupled binding and folding of intrinsically disordered proteins. J Mol Biol 422, 674-684.
    • (2012) J Mol Biol , vol.422 , pp. 674-684
    • Ganguly, D.1    Otieno, S.2    Waddell, B.3    Iconaru, L.4    Kriwacki, R.W.5    Chen, J.6
  • 64
    • 84886648634 scopus 로고    scopus 로고
    • Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX
    • Shammas SL, Travis AJ, &, Clarke J, (2013) Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX. J Phys Chem B 117, 13346-13356.
    • (2013) J Phys Chem B , vol.117 , pp. 13346-13356
    • Shammas, S.L.1    Travis, A.J.2    Clarke, J.3
  • 65
    • 84873828976 scopus 로고    scopus 로고
    • Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'
    • Rogers JM, Steward A, &, Clarke J, (2013) Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'. J Am Chem Soc 135, 1415-1422.
    • (2013) J Am Chem Soc , vol.135 , pp. 1415-1422
    • Rogers, J.M.1    Steward, A.2    Clarke, J.3
  • 67
    • 33645935390 scopus 로고    scopus 로고
    • The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions
    • Jonker HR, Wechselberger RW, Boelens R, Kaptein R, &, Folkers GE, (2006) The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. Biochemistry 45, 5067-5081.
    • (2006) Biochemistry , vol.45 , pp. 5067-5081
    • Jonker, H.R.1    Wechselberger, R.W.2    Boelens, R.3    Kaptein, R.4    Folkers, G.E.5
  • 68
    • 69949134806 scopus 로고    scopus 로고
    • Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements
    • Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, &, Morikawa K, (2009) Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. J Biol Chem 284, 24610-24621.
    • (2009) J Biol Chem , vol.284 , pp. 24610-24621
    • Tsunaka, Y.1    Toga, J.2    Yamaguchi, H.3    Tate, S.4    Hirose, S.5    Morikawa, K.6
  • 69
    • 84930216174 scopus 로고    scopus 로고
    • Insights into the Hendra virus NTAIL-XD complex: evidence for a parallel organization of the helical MoRE at the XD surface stabilized by a combination of hydrophobic and polar interactions
    • Erales J, Beltrandi M, Roche J, Maté M, &, Longhi S, (2015) Insights into the Hendra virus NTAIL-XD complex: evidence for a parallel organization of the helical MoRE at the XD surface stabilized by a combination of hydrophobic and polar interactions. Biochimica and Biopysical Acta 1854, 1038-1053.
    • (2015) Biochimica and Biopysical Acta , vol.1854 , pp. 1038-1053
    • Erales, J.1    Beltrandi, M.2    Roche, J.3    Maté, M.4    Longhi, S.5
  • 70
    • 77952335311 scopus 로고    scopus 로고
    • Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
    • Mao AH, Crick SL, Vitalis A, Chicoine CL, &, Pappu RV, (2010) Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc Natl Acad Sci USA 107, 8183-8188.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4    Pappu, R.V.5
  • 72
    • 84882364963 scopus 로고    scopus 로고
    • Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues
    • Das RK, &, Pappu RV, (2013) Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. Proc Natl Acad Sci USA 110, 13392-13397.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 13392-13397
    • Das, R.K.1    Pappu, R.V.2
  • 73
    • 84961288478 scopus 로고    scopus 로고
    • Relating sequence encoded information to form and function of intrinsically disordered proteins
    • Das RK, Ruff KM, &, Pappu RV, (2015) Relating sequence encoded information to form and function of intrinsically disordered proteins. Curr Opin Struct Biol 32, 102-112.
    • (2015) Curr Opin Struct Biol , vol.32 , pp. 102-112
    • Das, R.K.1    Ruff, K.M.2    Pappu, R.V.3
  • 74
    • 45849104776 scopus 로고    scopus 로고
    • Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1
    • Day CL, Smits C, Fan FC, Lee EF, Fairlie WD, &, Hinds MG, (2008) Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. J Mol Biol 380, 958-971.
    • (2008) J Mol Biol , vol.380 , pp. 958-971
    • Day, C.L.1    Smits, C.2    Fan, F.C.3    Lee, E.F.4    Fairlie, W.D.5    Hinds, M.G.6
  • 76
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F, (1988) Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 16, 10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 77
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi Z, Csizmok V, Tompa P, &, Simon I, (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21, 3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 79
    • 84862989011 scopus 로고    scopus 로고
    • Fractional factorial approach combining 4 Escherichia coli strains, 3 culture media, 3 expression temperatures and 5 N-terminal fusion tags for screening the soluble expression of recombinant proteins
    • Noguere C, Larsson AM, Guyot JC, &, Bignon C, (2012) Fractional factorial approach combining 4 Escherichia coli strains, 3 culture media, 3 expression temperatures and 5 N-terminal fusion tags for screening the soluble expression of recombinant proteins. Protein Expr Purif 84, 204-213.
    • (2012) Protein Expr Purif , vol.84 , pp. 204-213
    • Noguere, C.1    Larsson, A.M.2    Guyot, J.C.3    Bignon, C.4
  • 80
    • 30944459888 scopus 로고    scopus 로고
    • Improved solubility of TEV protease by directed evolution
    • van den Berg S, Lofdahl PA, Hard T, &, Berglund H, (2006) Improved solubility of TEV protease by directed evolution. J Biotechnol 121, 291-298.
    • (2006) J Biotechnol , vol.121 , pp. 291-298
    • Van Den Berg, S.1    Lofdahl, P.A.2    Hard, T.3    Berglund, H.4
  • 81
    • 84861736272 scopus 로고    scopus 로고
    • Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables
    • Ozenne V, Bauer F, Salmon L, Huang JR, Jensen MR, Segard S, Bernado P, Charavay C, &, Blackledge M, (2012) flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables. Bioinformatics 28, 1463-1470.
    • (2012) Bioinformatics , vol.28 , pp. 1463-1470
    • Ozenne, V.1    Bauer, F.2    Salmon, L.3    Huang, J.R.4    Jensen, M.R.5    Segard, S.6    Bernado, P.7    Charavay, C.8    Blackledge, M.9


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