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Volumn 282, Issue 7, 2015, Pages 1182-1189

Functional roles of transiently and intrinsically disordered regions within proteins

Author keywords

foldon; induced foldon; intrinsically disordered protein; intrinsically disordered region; molecular recognition; nonfoldon; post translational modification; protein protein interaction; semi foldon; unfoldon

Indexed keywords

FOLDON; INTRINSICALLY DISORDERED REGION; NONFOLDON; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN UNFOLDING; REVIEW; SEMI FOLDON; UNFOLDON; CHEMISTRY; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE;

EID: 84926068561     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13202     Document Type: Review
Times cited : (166)

References (83)
  • 1
    • 84892166712 scopus 로고
    • Einfluss der configuration auf die wirkung der enzyme
    • Fischer E, (1894) Einfluss der configuration auf die wirkung der enzyme. Ber Dtsch Chem Ges 27, 2985-2993.
    • (1894) Ber Dtsch Chem Ges , vol.27 , pp. 2985-2993
    • Fischer, E.1
  • 2
    • 0028321021 scopus 로고
    • How Emil Fischer was led to the lock and key concept for enzyme specificity
    • Lemieux UR, &, Spohr U, (1994) How Emil Fischer was led to the lock and key concept for enzyme specificity. Adv Carbohydr Chem Biochem 50, 1-20.
    • (1994) Adv Carbohydr Chem Biochem , vol.50 , pp. 1-20
    • Lemieux, U.R.1    Spohr, U.2
  • 3
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker BA, Portman JJ, &, Wolynes PG, (2000) Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc Natl Acad Sci USA 97, 8868-8873.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 4
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland DE, (1958) Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci USA 44, 98-104.
    • (1958) Proc Natl Acad Sci USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 6
    • 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
  • 7
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, &, Fink AL, (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41, 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 8
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P, (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27, 527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 9
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein non-folding
    • Uversky VN, &, Dunker AK, (2010) Understanding protein non-folding. Biochim Biophys Acta 1804, 1231-1264.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, A.K.2
  • 10
    • 84870057622 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: A 10-year recap
    • Tompa P, (2012) Intrinsically disordered proteins: a 10-year recap. Trends Biochem Sci 37, 509-516.
    • (2012) Trends Biochem Sci , vol.37 , pp. 509-516
    • Tompa, P.1
  • 11
    • 84876281768 scopus 로고    scopus 로고
    • Unusual biophysics of intrinsically disordered proteins
    • Uversky VN, (2013) Unusual biophysics of intrinsically disordered proteins. Biochim Biophys Acta 1834, 932-951.
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 932-951
    • Uversky, V.N.1
  • 12
    • 84878940937 scopus 로고    scopus 로고
    • A decade and a half of protein intrinsic disorder: Biology still waits for physics
    • Uversky VN, (2013) A decade and a half of protein intrinsic disorder: biology still waits for physics. Protein Sci 22, 693-724.
    • (2013) Protein Sci , vol.22 , pp. 693-724
    • Uversky, V.N.1
  • 14
    • 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
  • 15
    • 84902160274 scopus 로고    scopus 로고
    • Intrinsically disordered proteins and intrinsically disordered protein regions
    • Oldfield CJ, &, Dunker AK, (2014) Intrinsically disordered proteins and intrinsically disordered protein regions. Annu Rev Biochem 83, 553-584.
    • (2014) Annu Rev Biochem , vol.83 , pp. 553-584
    • Oldfield, C.J.1    Dunker, A.K.2
  • 17
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, &, Jones DT, (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337, 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 19
    • 84859701551 scopus 로고    scopus 로고
    • Orderly order in protein intrinsic disorder distribution: Disorder in 3500 proteomes from viruses and the three domains of life
    • Xue B, Dunker AK, &, Uversky VN, (2012) Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn 30, 137-149.
    • (2012) J Biomol Struct Dyn , vol.30 , pp. 137-149
    • Xue, B.1    Dunker, A.K.2    Uversky, V.N.3
  • 20
    • 84925227741 scopus 로고    scopus 로고
    • Exceptionally abundant exceptions: Comprehensive characterization of intrinsic disorder in all domains of life
    • Peng Z, Yan J, Fan X, Mizianty MJ, Xue B, Wang K, Hu G, Uversky VN, &, Kurgan L, (2015) Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life. Cell Mol Life Sci 72, 137-151.
    • (2015) Cell Mol Life Sci , vol.72 , pp. 137-151
    • Peng, Z.1    Yan, J.2    Fan, X.3    Mizianty, M.J.4    Xue, B.5    Wang, K.6    Hu, G.7    Uversky, V.N.8    Kurgan, L.9
  • 22
    • 4644359012 scopus 로고    scopus 로고
    • How cytochrome c folds, and why: Submolecular foldon units and their stepwise sequential stabilization
    • Maity H, Maity M, &, Englander SW, (2004) How cytochrome c folds, and why: submolecular foldon units and their stepwise sequential stabilization. J Mol Biol 343, 223-233.
    • (2004) J Mol Biol , vol.343 , pp. 223-233
    • Maity, H.1    Maity, M.2    Englander, S.W.3
  • 25
    • 42449151176 scopus 로고    scopus 로고
    • Protein folding and misfolding: Mechanism and principles
    • Englander SW, Mayne L, &, Krishna MM, (2007) Protein folding and misfolding: mechanism and principles. Q Rev Biophys 40, 287-326.
    • (2007) Q Rev Biophys , vol.40 , pp. 287-326
    • Englander, S.W.1    Mayne, L.2    Krishna, M.M.3
  • 26
    • 44449113414 scopus 로고    scopus 로고
    • Protein folding: Independent unrelated pathways or predetermined pathway with optional errors
    • Bedard S, Krishna MM, Mayne L, &, Englander SW, (2008) Protein folding: independent unrelated pathways or predetermined pathway with optional errors. Proc Natl Acad Sci USA 105, 7182-7187.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7182-7187
    • Bedard, S.1    Krishna, M.M.2    Mayne, L.3    Englander, S.W.4
  • 27
    • 33847306593 scopus 로고    scopus 로고
    • A unified mechanism for protein folding: Predetermined pathways with optional errors
    • Krishna MM, &, Englander SW, (2007) A unified mechanism for protein folding: predetermined pathways with optional errors. Protein Sci 16, 449-464.
    • (2007) Protein Sci , vol.16 , pp. 449-464
    • Krishna, M.M.1    Englander, S.W.2
  • 28
    • 84909606742 scopus 로고    scopus 로고
    • The nature of protein folding pathways
    • Englander SW, &, Mayne L, (2014) The nature of protein folding pathways. Proc Natl Acad Sci USA 111, 15873-15880.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 15873-15880
    • Englander, S.W.1    Mayne, L.2
  • 29
    • 33846916730 scopus 로고    scopus 로고
    • Malleability of protein folding pathways: A simple reason for complex behaviour
    • Lindberg MO, &, Oliveberg M, (2007) Malleability of protein folding pathways: a simple reason for complex behaviour. Curr Opin Struct Biol 17, 21-29.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 21-29
    • Lindberg, M.O.1    Oliveberg, M.2
  • 30
    • 33645277619 scopus 로고    scopus 로고
    • Functional role of a protein foldon-an Omega-loop foldon controls the alkaline transition in ferricytochrome c
    • Maity H, Rumbley JN, &, Englander SW, (2006) Functional role of a protein foldon-an Omega-loop foldon controls the alkaline transition in ferricytochrome c. Proteins 63, 349-355.
    • (2006) Proteins , vol.63 , pp. 349-355
    • Maity, H.1    Rumbley, J.N.2    Englander, S.W.3
  • 31
    • 84902446848 scopus 로고    scopus 로고
    • Conditionally and transiently disordered proteins: Awakening cryptic disorder to regulate protein function
    • Jakob U, Kriwacki R, &, Uversky VN, (2014) Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function. Chem Rev 114, 6779-6805.
    • (2014) Chem Rev , vol.114 , pp. 6779-6805
    • Jakob, U.1    Kriwacki, R.2    Uversky, V.N.3
  • 32
    • 84878899241 scopus 로고    scopus 로고
    • The most important thing is the tail: Multitudinous functionalities of intrinsically disordered protein termini
    • Uversky VN, (2013) The most important thing is the tail: multitudinous functionalities of intrinsically disordered protein termini. FEBS Lett 587, 1891-1901.
    • (2013) FEBS Lett , vol.587 , pp. 1891-1901
    • Uversky, V.N.1
  • 34
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki RW, Hengst L, Tennant L, Reed SI, &, Wright PE, (1996) Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc Natl Acad Sci USA 93, 11504-11509.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 35
    • 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
  • 39
    • 36749037699 scopus 로고    scopus 로고
    • Mining alpha-helix-forming molecular recognition features with cross species sequence alignments
    • Cheng Y, Oldfield CJ, Meng J, Romero P, Uversky VN, &, Dunker AK, (2007) Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry 46, 13468-13477.
    • (2007) Biochemistry , vol.46 , pp. 13468-13477
    • Cheng, Y.1    Oldfield, C.J.2    Meng, J.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 42
    • 79951905332 scopus 로고    scopus 로고
    • Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes
    • Uversky VN, (2011) Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes. Chem Soc Rev 40, 1623-1634.
    • (2011) Chem Soc Rev , vol.40 , pp. 1623-1634
    • Uversky, V.N.1
  • 43
    • 84924061187 scopus 로고    scopus 로고
    • An intrinsically disordered linker plays a critical role in bacterial cell division
    • Buske PJ, Mittal A, Pappu RV, &, Levin PA, (2014) An intrinsically disordered linker plays a critical role in bacterial cell division. Semin Cell Dev Biol, doi: 10.1016/j.semcdb.2014.09.017.
    • (2014) Semin Cell Dev Biol
    • Buske, P.J.1    Mittal, A.2    Pappu, R.V.3    Levin, P.A.4
  • 44
    • 84908220940 scopus 로고    scopus 로고
    • Multiscale conformational heterogeneity in staphylococcal protein a: Possible determinant of functional plasticity
    • Deis LN, Pemble CWT, Qi Y, Hagarman A, Richardson DC, Richardson JS, &, Oas TG, (2014) Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity. Structure 22, 1467-1477.
    • (2014) Structure , vol.22 , pp. 1467-1477
    • Deis, L.N.1    Pemble, C.W.T.2    Qi, Y.3    Hagarman, A.4    Richardson, D.C.5    Richardson, J.S.6    Oas, T.G.7
  • 45
    • 84922211452 scopus 로고    scopus 로고
    • Design and characterization of structured protein linkers with differing flexibilities
    • Klein JS, Jiang S, Galimidi RP, Keeffe JR, &, Bjorkman PJ, (2014) Design and characterization of structured protein linkers with differing flexibilities. Protein Eng Des Sel 27, 325-330.
    • (2014) Protein Eng des Sel , vol.27 , pp. 325-330
    • Klein, J.S.1    Jiang, S.2    Galimidi, R.P.3    Keeffe, J.R.4    Bjorkman, P.J.5
  • 47
    • 84874033858 scopus 로고    scopus 로고
    • Linkers in the structural biology of protein-protein interactions
    • Reddy Chichili VP, Kumar V, &, Sivaraman J, (2013) Linkers in the structural biology of protein-protein interactions. Protein Sci 22, 153-167.
    • (2013) Protein Sci , vol.22 , pp. 153-167
    • Reddy Chichili, V.P.1    Kumar, V.2    Sivaraman, J.3
  • 49
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: Linkers are not merely flexible
    • Ma B, Tsai CJ, Haliloglu T, &, Nussinov R, (2011) Dynamic allostery: linkers are not merely flexible. Structure 19, 907-917.
    • (2011) Structure , vol.19 , pp. 907-917
    • Ma, B.1    Tsai, C.J.2    Haliloglu, T.3    Nussinov, R.4
  • 50
    • 84881018686 scopus 로고    scopus 로고
    • Fusion protein linkers: Property, design and functionality
    • Chen X, Zaro JL, &, Shen WC, (2013) Fusion protein linkers: property, design and functionality. Adv Drug Deliv Rev 65, 1357-1369.
    • (2013) Adv Drug Deliv Rev , vol.65 , pp. 1357-1369
    • Chen, X.1    Zaro, J.L.2    Shen, W.C.3
  • 52
    • 80052657051 scopus 로고    scopus 로고
    • One small step for Mot1; One giant leap for other Swi2/Snf2 enzymes?
    • Viswanathan R, &, Auble DT, (2011) One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes? Biochim Biophys Acta 1809, 488-496.
    • (2011) Biochim Biophys Acta , vol.1809 , pp. 488-496
    • Viswanathan, R.1    Auble, D.T.2
  • 53
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham RN, (2000) Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem 69, 961-1004.
    • (2000) Annu Rev Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 54
    • 0028506122 scopus 로고
    • The Merck Frosst Award Lecture 1994. Calmodulin: A versatile calcium mediator protein
    • Vogel HJ, (1994) The Merck Frosst Award Lecture 1994. Calmodulin: a versatile calcium mediator protein. Biochem Cell Biol 72, 357-376.
    • (1994) Biochem Cell Biol , vol.72 , pp. 357-376
    • Vogel, H.J.1
  • 55
    • 0032469789 scopus 로고    scopus 로고
    • Molecular mechanisms of calmodulin's functional versatility, Biochemistry and Cell Biology =
    • Zhang M, &, Yuan T, (1998) Molecular mechanisms of calmodulin's functional versatility, Biochemistry and Cell Biology = Biochem Cell Biol 76, 313-323.
    • (1998) Biochem Cell Biol , vol.76 , pp. 313-323
    • Zhang, M.1    Yuan, T.2
  • 56
    • 84906854634 scopus 로고    scopus 로고
    • The structural and functional signatures of proteins that undergo multiple events of post-translational modification
    • Pejaver V, Hsu WL, Xin F, Dunker AK, Uversky VN, &, Radivojac P, (2014) The structural and functional signatures of proteins that undergo multiple events of post-translational modification. Protein Sci 23, 1077-1093.
    • (2014) Protein Sci , vol.23 , pp. 1077-1093
    • Pejaver, V.1    Hsu, W.L.2    Xin, F.3    Dunker, A.K.4    Uversky, V.N.5    Radivojac, P.6
  • 57
    • 34247571020 scopus 로고    scopus 로고
    • Posttranslational modifications and subcellular localization signals: Indicators of sequence regions without inherent 3D structure?
    • Eisenhaber B, &, Eisenhaber F, (2007) Posttranslational modifications and subcellular localization signals: indicators of sequence regions without inherent 3D structure? Curr Protein Pept Sci 8, 197-203.
    • (2007) Curr Protein Pept Sci , vol.8 , pp. 197-203
    • Eisenhaber, B.1    Eisenhaber, F.2
  • 58
    • 0029070171 scopus 로고
    • Omega loops: Nonregular secondary structures significant in protein function and stability
    • Fetrow JS, (1995) Omega loops: nonregular secondary structures significant in protein function and stability. FASEB J 9, 708-717.
    • (1995) FASEB J , vol.9 , pp. 708-717
    • Fetrow, J.S.1
  • 59
    • 11844280851 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in glycosyltransferases
    • Qasba PK, Ramakrishnan B, &, Boeggeman E, (2005) Substrate-induced conformational changes in glycosyltransferases. Trends Biochem Sci 30, 53-62.
    • (2005) Trends Biochem Sci , vol.30 , pp. 53-62
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 60
    • 42949090427 scopus 로고    scopus 로고
    • Structure and function of beta -1,4-galactosyltransferase
    • Qasba PK, Ramakrishnan B, &, Boeggeman E, (2008) Structure and function of beta -1,4-galactosyltransferase. Curr Drug Targets 9, 292-309.
    • (2008) Curr Drug Targets , vol.9 , pp. 292-309
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 61
    • 36048990877 scopus 로고    scopus 로고
    • Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin alpha: Evidence for metalation as an entropic switch
    • Yi S, Boys BL, Brickenden A, Konermann L, &, Choy WY, (2007) Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin alpha: evidence for metalation as an entropic switch. Biochemistry 46, 13120-13130.
    • (2007) Biochemistry , vol.46 , pp. 13120-13130
    • Yi, S.1    Boys, B.L.2    Brickenden, A.3    Konermann, L.4    Choy, W.Y.5
  • 64
    • 84860324033 scopus 로고    scopus 로고
    • Disorder-to-order transition of an intrinsically disordered region of sortase revealed by multiscale enhanced sampling
    • Moritsugu K, Terada T, &, Kidera A, (2012) Disorder-to-order transition of an intrinsically disordered region of sortase revealed by multiscale enhanced sampling. J Am Chem Soc 134, 7094-7101.
    • (2012) J Am Chem Soc , vol.134 , pp. 7094-7101
    • Moritsugu, K.1    Terada, T.2    Kidera, A.3
  • 65
    • 84911885077 scopus 로고    scopus 로고
    • The conformational response to Zn(II) and Ni(II) binding of Sporosarcina pasteurii UreG, an intrinsically disordered GTPase
    • D'Urzo A, Santambrogio C, Grandori R, Ciurli S, &, Zambelli B, (2014) The conformational response to Zn(II) and Ni(II) binding of Sporosarcina pasteurii UreG, an intrinsically disordered GTPase. J Biol Inorg Chem 19, 1341-1354.
    • (2014) J Biol Inorg Chem , vol.19 , pp. 1341-1354
    • D'Urzo, A.1    Santambrogio, C.2    Grandori, R.3    Ciurli, S.4    Zambelli, B.5
  • 66
    • 59449107337 scopus 로고    scopus 로고
    • RTX calcium binding motifs are intrinsically disordered in the absence of calcium: Implication for protein secretion
    • Chenal A, Guijarro JI, Raynal B, Delepierre M, &, Ladant D, (2009) RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. J Biol Chem 284, 1781-1789.
    • (2009) J Biol Chem , vol.284 , pp. 1781-1789
    • Chenal, A.1    Guijarro, J.I.2    Raynal, B.3    Delepierre, M.4    Ladant, D.5
  • 67
    • 67650242421 scopus 로고    scopus 로고
    • Zinc ion-induced domain organization in metallo-beta-lactamases: A flexible "zinc arm" for rapid metal ion transfer?
    • Selevsek N, Rival S, Tholey A, Heinzle E, Heinz U, Hemmingsen L, &, Adolph HW, (2009) Zinc ion-induced domain organization in metallo-beta-lactamases: a flexible "zinc arm" for rapid metal ion transfer? J Biol Chem 284, 16419-16431.
    • (2009) J Biol Chem , vol.284 , pp. 16419-16431
    • Selevsek, N.1    Rival, S.2    Tholey, A.3    Heinzle, E.4    Heinz, U.5    Hemmingsen, L.6    Adolph, H.W.7
  • 68
    • 84862123641 scopus 로고    scopus 로고
    • Engineering of an environmentally responsive beta roll peptide for use as a calcium-dependent cross-linking domain for peptide hydrogel formation
    • Dooley K, Kim YH, Lu HD, Tu R, &, Banta S, (2012) Engineering of an environmentally responsive beta roll peptide for use as a calcium-dependent cross-linking domain for peptide hydrogel formation. Biomacromolecules 13, 1758-1764.
    • (2012) Biomacromolecules , vol.13 , pp. 1758-1764
    • Dooley, K.1    Kim, Y.H.2    Lu, H.D.3    Tu, R.4    Banta, S.5
  • 69
    • 84890955045 scopus 로고    scopus 로고
    • NS3 protease from hepatitis C virus: Biophysical studies on an intrinsically disordered protein domain
    • Vega S, Neira JL, Marcuello C, Lostao A, Abian O, &, Velazquez-Campoy A, (2013) NS3 protease from hepatitis C virus: biophysical studies on an intrinsically disordered protein domain. Int J Mol Sci 14, 13282-13306.
    • (2013) Int J Mol Sci , vol.14 , pp. 13282-13306
    • Vega, S.1    Neira, J.L.2    Marcuello, C.3    Lostao, A.4    Abian, O.5    Velazquez-Campoy, A.6
  • 71
    • 64349106349 scopus 로고    scopus 로고
    • AP7, a partially disordered pseudo C-RING protein, is capable of forming stabilized aragonite in vitro
    • Amos FF, &, Evans JS, (2009) AP7, a partially disordered pseudo C-RING protein, is capable of forming stabilized aragonite in vitro. Biochemistry 48, 1332-1339.
    • (2009) Biochemistry , vol.48 , pp. 1332-1339
    • Amos, F.F.1    Evans, J.S.2
  • 72
    • 84882594567 scopus 로고    scopus 로고
    • A pearl protein self-assembles to form protein complexes that amplify mineralization
    • Perovic I, Mandal T, &, Evans JS, (2013) A pearl protein self-assembles to form protein complexes that amplify mineralization. Biochemistry 52, 5696-5703.
    • (2013) Biochemistry , vol.52 , pp. 5696-5703
    • Perovic, I.1    Mandal, T.2    Evans, J.S.3
  • 73
    • 33745617904 scopus 로고    scopus 로고
    • Intrinsically disordered C-terminal segments of voltage-activated potassium channels: A possible fishing rod-like mechanism for channel binding to scaffold proteins
    • Magidovich E, Fleishman SJ, &, Yifrach O, (2006) Intrinsically disordered C-terminal segments of voltage-activated potassium channels: a possible fishing rod-like mechanism for channel binding to scaffold proteins. Bioinformatics 22, 1546-1550.
    • (2006) Bioinformatics , vol.22 , pp. 1546-1550
    • Magidovich, E.1    Fleishman, S.J.2    Yifrach, O.3
  • 74
    • 84879836180 scopus 로고    scopus 로고
    • The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein
    • Vassall KA, Bessonov K, De Avila M, Polverini E, &, Harauz G, (2013) The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein. PLoS One 8, e68175.
    • (2013) PLoS One , vol.8 , pp. e68175
    • Vassall, K.A.1    Bessonov, K.2    De Avila, M.3    Polverini, E.4    Harauz, G.5
  • 76
    • 50049097448 scopus 로고    scopus 로고
    • Intrinsic disorder in scaffold proteins: Getting more from less
    • Cortese MS, Uversky VN, &, Dunker AK, (2008) Intrinsic disorder in scaffold proteins: getting more from less. Prog Biophys Mol Biol 98, 85-106.
    • (2008) Prog Biophys Mol Biol , vol.98 , pp. 85-106
    • Cortese, M.S.1    Uversky, V.N.2    Dunker, A.K.3
  • 77
    • 67650665028 scopus 로고    scopus 로고
    • High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1
    • Balazs A, Csizmok V, Buday L, Rakacs M, Kiss R, Bokor M, Udupa R, Tompa K, &, Tompa P, (2009) High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1. FEBS J 276, 3744-3756.
    • (2009) FEBS J , vol.276 , pp. 3744-3756
    • Balazs, A.1    Csizmok, V.2    Buday, L.3    Rakacs, M.4    Kiss, R.5    Bokor, M.6    Udupa, R.7    Tompa, K.8    Tompa, P.9
  • 78
    • 79952114716 scopus 로고    scopus 로고
    • Functional classification of scaffold proteins and related molecules
    • Buday L, &, Tompa P, (2010) Functional classification of scaffold proteins and related molecules. FEBS J 277, 4348-4355.
    • (2010) FEBS J , vol.277 , pp. 4348-4355
    • Buday, L.1    Tompa, P.2
  • 81
    • 84893286454 scopus 로고    scopus 로고
    • Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association
    • Hisaoka M, Nagata K, &, Okuwaki M, (2014) Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association. Nucleic Acids Res 42, 1180-1195.
    • (2014) Nucleic Acids Res , vol.42 , pp. 1180-1195
    • Hisaoka, M.1    Nagata, K.2    Okuwaki, M.3
  • 82
    • 34547462095 scopus 로고    scopus 로고
    • Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity
    • Borg M, Mittag T, Pawson T, Tyers M, Forman-Kay JD, &, Chan HS, (2007) Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proc Natl Acad Sci USA 104, 9650-9655.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 9650-9655
    • Borg, M.1    Mittag, T.2    Pawson, T.3    Tyers, M.4    Forman-Kay, J.D.5    Chan, H.S.6
  • 83
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • Mittag T, Kay LE, &, Forman-Kay JD, (2010) Protein dynamics and conformational disorder in molecular recognition. J Mol Recognit 23, 105-116.
    • (2010) J Mol Recognit , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.