메뉴 건너뛰기




Volumn 76, Issue 3, 2009, Pages 731-746

Order propensity of an intrinsically disordered protein, the cyclin-dependent kinase inhibitor Sic1

Author keywords

Cell cycle; Circular dichroism; Disorder prediction; Limited proteolysis; Mass spectrometry; Molten globule; Protein folding; Protein phosphorylation; Protein protein interactions; Saccharomyces cerevisiae

Indexed keywords

CASEIN KINASE II; CYCLIN DEPENDENT KINASE INHIBITOR; PROTEIN SIC 1; UNCLASSIFIED DRUG;

EID: 68049128317     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22385     Document Type: Article
Times cited : (57)

References (103)
  • 1
    • 47649102449 scopus 로고    scopus 로고
    • Regulation of cell division by intrinsically unstructured proteins: Intrinsic flexibility, modularity, and signaling conduits
    • Galea CA, Wang Y, Sivakolundu SG, Kriwacki RW. Regulation of cell division by intrinsically unstructured proteins: intrinsic flexibility, modularity, and signaling conduits. Biochemistry 2008;47:7598-7609.
    • (2008) Biochemistry , vol.47 , pp. 7598-7609
    • Galea, C.A.1    Wang, Y.2    Sivakolundu, S.G.3    Kriwacki, R.W.4
  • 2
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink AL. Natively unfolded proteins. Curr Opin Struct Biol 2005;15:35-41.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 3
    • 0034669882 scopus 로고    scopus 로고
    • Why are "Natively Unfolded" Proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL. Why are "Natively Unfolded" Proteins unstructured under physiologic conditions? Proteins 2000; 41:415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 4
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky VN. Natively unfolded proteins: A point where biology waits for physics. Protein Sci 2002;11:739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 6
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity-linking function and disorder
    • Dunker AK, Obradovic Z. The protein trinity-linking function and disorder. Nat Biotechnol 2001;19:805-806.
    • (2001) Nat Biotechnol , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 8
    • 41049091705 scopus 로고    scopus 로고
    • Intrinsic disorder in pathogenic and non-pathogenic microbes: Discovering and analyzing the unfoldomes of early-branching eukaryotes
    • Mohan A, Sullivan WJ, Jr., Radivojac P, Dunker AK, Uversky VN. Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes. Mol Biosyst 2008;4:328-340.
    • (2008) Mol Biosyst , vol.4 , pp. 328-340
    • Mohan, A.1    Sullivan Jr., W.J.2    Radivojac, P.3    Dunker, A.K.4    Uversky, V.N.5
  • 12
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • Dunker AK, Brown CJ, Obradovic Z. Identification and functions of usefully disordered proteins. Adv Protein Chem 2002;62:25-49.
    • (2002) Adv Protein Chem , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 13
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker AK, Cortese MS, Romero P, Iakoucheva LM, Uversky VN. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 2005;272:5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 14
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J Mol Biol 1999;293:321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 15
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005;6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 17
    • 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. Showing Your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 2005;18:343-384.
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 19
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfield CJ, Meng J, Yang JY, Yang MQ, Uversky VN, Dunker AK. Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics 2008;9(Suppl 1):S1.
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL. 1
    • Oldfield, C.J.1    Meng, J.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5    Dunker, A.K.6
  • 20
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky VN, Oldfield CJ, Dunker AK. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 2008;37:215-246.
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 22
    • 33645778262 scopus 로고    scopus 로고
    • Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions
    • Chen JW, Romero P, Uversky VN, Dunker AK. Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions. J Proteome Res 2006;5:879-887.
    • (2006) J Proteome Res , vol.5 , pp. 879-887
    • Chen, J.W.1    Romero, P.2    Uversky, V.N.3    Dunker, A.K.4
  • 23
    • 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. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc Natl Acad Sci U S A 1996;93:11504-11509.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 24
    • 0028114987 scopus 로고
    • The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae
    • Schwob E, Bohm T, Mendenhall MD, Nasmyth K. The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae. Cell 1994;79:233-244.
    • (1994) Cell , vol.79 , pp. 233-244
    • Schwob, E.1    Bohm, T.2    Mendenhall, M.D.3    Nasmyth, K.4
  • 25
    • 0035966288 scopus 로고    scopus 로고
    • Multisite phosphorylation and the countdown to S phase
    • Deshaies RJ, Ferrell JE, Jr. Multisite phosphorylation and the countdown to S phase. Cell 2001;107:819-822.
    • (2001) Cell , vol.107 , pp. 819-822
    • Deshaies, R.J.1    Ferrell Jr., J.E.2
  • 26
    • 0030612012 scopus 로고    scopus 로고
    • Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase
    • Verma R, Annan RS, Huddleston MJ, Carr SA, Reynard G, Deshaies RJ. Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase. Science 1997;278:455-460.
    • (1997) Science , vol.278 , pp. 455-460
    • Verma, R.1    Annan, R.S.2    Huddleston, M.J.3    Carr, S.A.4    Reynard, G.5    Deshaies, R.J.6
  • 29
    • 34247627985 scopus 로고    scopus 로고
    • Cell size at S phase initiation: An emergent property of the G1/S network
    • Barberis M, Klipp E, Vanoni M, Alberghina L. Cell size at S phase initiation: an emergent property of the G1/S network. PLoS Comput Biol 2007;3:e64.
    • (2007) PLoS Comput Biol , vol.3
    • Barberis, M.1    Klipp, E.2    Vanoni, M.3    Alberghina, L.4
  • 30
    • 29244475066 scopus 로고    scopus 로고
    • Subcellular localization of the cyclin dependent kinase inhibitor Sic1 is modulated by the carbon source in budding yeast
    • Rossi RL, Zinzalla V, Mastriani A, Vanoni M, Alberghina L. Subcellular localization of the cyclin dependent kinase inhibitor Sic1 is modulated by the carbon source in budding yeast. Cell Cycle 2005;4:1798-1807.
    • (2005) Cell Cycle , vol.4 , pp. 1798-1807
    • Rossi, R.L.1    Zinzalla, V.2    Mastriani, A.3    Vanoni, M.4    Alberghina, L.5
  • 31
    • 33846964530 scopus 로고    scopus 로고
    • Rapamycin-mediated G1 arrest involves regulation of the Cdk inhibitor Sic1 in Saccharomyces cerevisiae
    • Zinzalla V, Graziola M, Mastriani A, Vanoni M, Alberghina L. Rapamycin-mediated G1 arrest involves regulation of the Cdk inhibitor Sic1 in Saccharomyces cerevisiae. Mol Microbiol 2007;63:1482-1494.
    • (2007) Mol Microbiol , vol.63 , pp. 1482-1494
    • Zinzalla, V.1    Graziola, M.2    Mastriani, A.3    Vanoni, M.4    Alberghina, L.5
  • 32
    • 5444253797 scopus 로고    scopus 로고
    • Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of Sic1
    • Escote X, Zapater M, Clotet J, Posas F. Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of Sic1. Nat Cell Biol 2004;6:997-1002.
    • (2004) Nat Cell Biol , vol.6 , pp. 997-1002
    • Escote, X.1    Zapater, M.2    Clotet, J.3    Posas, F.4
  • 33
    • 0032878307 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitory domain of the yeast Sic1 protein is contained within the C-terminal 70 amino acids
    • Hodge A, Mendenhall M. The cyclin-dependent kinase inhibitory domain of the yeast Sic1 protein is contained within the C-terminal 70 amino acids. Mol Gen Genet 1999;262:55-64.
    • (1999) Mol Gen Genet , vol.262 , pp. 55-64
    • Hodge, A.1    Mendenhall, M.2
  • 34
    • 18844415826 scopus 로고    scopus 로고
    • The yeast cyclin-dependent kinase inhibitor Sic1 and mammalian p27Kip1 are functional homologues with a structurally conserved inhibitory domain
    • Barberis M, De Gioia L, Ruzzene M, Sarno S, Coccetti P, Fantucci P, Vanoni M, Alberghina L. The yeast cyclin-dependent kinase inhibitor Sic1 and mammalian p27Kip1 are functional homologues with a structurally conserved inhibitory domain. Biochem J 2005;387:639-647.
    • (2005) Biochem J , vol.387 , pp. 639-647
    • Barberis, M.1    De Gioia, L.2    Ruzzene, M.3    Sarno, S.4    Coccetti, P.5    Fantucci, P.6    Vanoni, M.7    Alberghina, L.8
  • 35
    • 33644534140 scopus 로고    scopus 로고
    • Thermodynamic characterization of interactions between p27(Kip1) and activated and non-activated Cdk2: Intrinsically unstructured proteins as thermodynamic tethers
    • Bowman P, Galea CA, Lacy E, Kriwacki RW. Thermodynamic characterization of interactions between p27(Kip1) and activated and non-activated Cdk2: intrinsically unstructured proteins as thermodynamic tethers. Biochim Biophys Acta 2006;1764:182-189.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 182-189
    • Bowman, P.1    Galea, C.A.2    Lacy, E.3    Kriwacki, R.W.4
  • 36
    • 27144528728 scopus 로고    scopus 로고
    • Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation
    • Sivakolundu SG, Bashford D, Kriwacki RW. Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. J Mol Biol 2005;353:1118-1128.
    • (2005) J Mol Biol , vol.353 , pp. 1118-1128
    • Sivakolundu, S.G.1    Bashford, D.2    Kriwacki, R.W.3
  • 37
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 1996;382:325-331.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5
  • 39
    • 34250662658 scopus 로고    scopus 로고
    • In CK2 inactivated cells the cyclin dependent kinase inhibitor Sic1 is involved in cell-cycle arrest before the onset of S phase
    • Tripodi F, Zinzalla V, Vanoni M, Alberghina L, Coccetti P. In CK2 inactivated cells the cyclin dependent kinase inhibitor Sic1 is involved in cell-cycle arrest before the onset of S phase. Biochem Biophys Res Commun 2007;359:921-927.
    • (2007) Biochem Biophys Res Commun , vol.359 , pp. 921-927
    • Tripodi, F.1    Zinzalla, V.2    Vanoni, M.3    Alberghina, L.4    Coccetti, P.5
  • 40
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson HJ, Wright PE. Unfolded proteins and protein folding studied by NMR. Chem Rev 2004;104:3607-3622.
    • (2004) Chem Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 45
    • 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. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005;21:3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 46
    • 20744437001 scopus 로고    scopus 로고
    • RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang ZR, Thomson R, McNeil P, Esnouf RM. RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 2005;21:3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 47
    • 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. Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry 2007;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
  • 49
    • 30344485673 scopus 로고    scopus 로고
    • Exploiting heterogeneous sequence properties improves prediction of protein disorder
    • Obradovic Z, Peng K, Vucetic S, Radivojac P, Dunker AK. Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins 2005;61(Suppl 7):176-182.
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 176-182
    • Obradovic, Z.1    Peng, K.2    Vucetic, S.3    Radivojac, P.4    Dunker, A.K.5
  • 50
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 2005;347:827-839.
    • (2005) J Mol Biol , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 52
    • 34447539760 scopus 로고    scopus 로고
    • Composition Profiler: A tool for discovery and visualization of amino acid composition differences
    • Vacic V, Uversky VN, Dunker AK, Lonardi S. Composition Profiler: A tool for discovery and visualization of amino acid composition differences. BMC Bioinformatics 2007;8:211.
    • (2007) BMC Bioinformatics , vol.8 , pp. 211
    • Vacic, V.1    Uversky, V.N.2    Dunker, A.K.3    Lonardi, S.4
  • 54
    • 0002440928 scopus 로고
    • Molecular cloning
    • Cold Spring Harbor, NY, Cold Spring Harbor Laboratory Press
    • Sambrook J, Fritsch EF, Maniatis T. Molecular cloning. A laboratory manual. Cold Spring Harbor, NY.: Cold Spring Harbor Laboratory Press.; 1989.
    • (1989) A laboratory manual
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 55
    • 18044363663 scopus 로고    scopus 로고
    • Whole plasmid mutagenic PCR for directed protein evolution
    • Matsumura I, Rowe LA. Whole plasmid mutagenic PCR for directed protein evolution. Biomol Engineering 2005;22:73-79.
    • (2005) Biomol Engineering , vol.22 , pp. 73-79
    • Matsumura, I.1    Rowe, L.A.2
  • 56
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 57
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitzky A, Golay MJE. Smoothing and differentiation of data by simplified least squares procedures. Anal Chem 1964;36:1627-1639.
    • (1964) Anal Chem , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2
  • 58
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, Woody RW. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 2000;287:252-260.
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 59
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ouali M, King RD. Cascaded multiple classifiers for secondary structure prediction. Protein Sci 2000;9:1162-1176.
    • (2000) Protein Sci , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 61
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem Sci 2002;27:527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 62
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky VN. What does it mean to be natively unfolded? Eur J Biochem 2002;269:2-12.
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 63
    • 23944446530 scopus 로고    scopus 로고
    • Recent developments in electrospray ionisation mass spectrometry: Noncovalently bound protein complexes
    • Ashcroft AE. Recent developments in electrospray ionisation mass spectrometry: noncovalently bound protein complexes. Nat Prod Rep 2005;22:452-464.
    • (2005) Nat Prod Rep , vol.22 , pp. 452-464
    • Ashcroft, A.E.1
  • 65
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon M, Robinson CV. The role of mass spectrometry in structure elucidation of dynamic protein complexes. Ann Rev Biochem 2007;76:167-193.
    • (2007) Ann Rev Biochem , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 66
    • 0141483579 scopus 로고    scopus 로고
    • Electrospray-ionization mass spectrometry for protein conformational studies
    • Grandori R. Electrospray-ionization mass spectrometry for protein conformational studies. Curr Org Chem 2003;7:1589-1603.
    • (2003) Curr Org Chem , vol.7 , pp. 1589-1603
    • Grandori, R.1
  • 67
    • 3042648557 scopus 로고    scopus 로고
    • Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry
    • Borysik AJ, Radford SE, Ashcroft AE. Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J Biol Chem 2004;279:27069-27077.
    • (2004) J Biol Chem , vol.279 , pp. 27069-27077
    • Borysik, A.J.1    Radford, S.E.2    Ashcroft, A.E.3
  • 68
    • 34347332295 scopus 로고    scopus 로고
    • A minimalist model for exploring conformational effects on the electrospray charge state distribution of proteins
    • Konermann L. A minimalist model for exploring conformational effects on the electrospray charge state distribution of proteins. J Phys Chem B 2007;111:6534-6543.
    • (2007) J Phys Chem B , vol.111 , pp. 6534-6543
    • Konermann, L.1
  • 69
    • 36348991325 scopus 로고    scopus 로고
    • Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometrymass spectrometry
    • Smith DP, Giles K, Bateman RH, Radford SE, Ashcroft AE. Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometrymass spectrometry. J Am Soc Mass Spectrom 2007;18:2180-2190.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 2180-2190
    • Smith, D.P.1    Giles, K.2    Bateman, R.H.3    Radford, S.E.4    Ashcroft, A.E.5
  • 70
    • 50849098485 scopus 로고    scopus 로고
    • Do ionic charges in ESI MS provide useful information on macromolecular structure?
    • Kaltashov IA, Abzalimov RR. Do ionic charges in ESI MS provide useful information on macromolecular structure? J Am Soc Mass Spectrom 2008;19:1239-1246.
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1239-1246
    • Kaltashov, I.A.1    Abzalimov, R.R.2
  • 71
    • 0036182699 scopus 로고    scopus 로고
    • Uncoupled analysis of secondary and tertiary protein structure by circular dichroism and electrospray ionization mass spectrometry
    • Grandori R, Matecko I, Müller N. Uncoupled analysis of secondary and tertiary protein structure by circular dichroism and electrospray ionization mass spectrometry. J Mass Spectrom 2001;37:191-196.
    • (2001) J Mass Spectrom , vol.37 , pp. 191-196
    • Grandori, R.1    Matecko, I.2    Müller, N.3
  • 73
    • 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. Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin alpha: evidence for metalation as an entropic switch. Biochemistry 2007;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
  • 74
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • Heck AJ, Van Den Heuvel RH. Investigation of intact protein complexes by mass spectrometry. Mass Spectrom Rev 2004;23:368-389.
    • (2004) Mass Spectrom Rev , vol.23 , pp. 368-389
    • Heck, A.J.1    Van Den Heuvel, R.H.2
  • 75
    • 0032444658 scopus 로고    scopus 로고
    • cosolvents come of age. Recent studies with peptides and proteins
    • Buck M. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q Rev Biophys 1998;31:297-355.
    • (1998) Q Rev Biophys , vol.31 , pp. 297-355
    • Trifluoroethanol, B.M.1
  • 76
    • 33751289801 scopus 로고    scopus 로고
    • Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling electron paramagnetic resonance spectroscopy
    • Morin B, Bourhis JM, Belle V, Woudstra M, Carriere F, Guigliarelli B, Fournel A, Longhi S. Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling electron paramagnetic resonance spectroscopy. J Phys Chem B 2006;110:20596-20608.
    • (2006) J Phys Chem B , vol.110 , pp. 20596-20608
    • Morin, B.1    Bourhis, J.M.2    Belle, V.3    Woudstra, M.4    Carriere, F.5    Guigliarelli, B.6    Fournel, A.7    Longhi, S.8
  • 78
    • 0033733510 scopus 로고    scopus 로고
    • A systematic, general proteolytic method for defining structural and functional domains of proteins
    • Carey J. A systematic, general proteolytic method for defining structural and functional domains of proteins. Methods in Enzymol 2000;328:499-514.
    • (2000) Methods in Enzymol , vol.328 , pp. 499-514
    • Carey, J.1
  • 79
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana A, Fassina G, Vita C, Dalzoppo D, Zamai M, Zambonin M. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry 1986;25:1847-1851.
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 80
    • 0031812617 scopus 로고    scopus 로고
    • Assessment of conformational parameters as predictors of limited proteolytic sites in native protein structures
    • Hubbard SJ, Beynon RJ, Thornton JM. Assessment of conformational parameters as predictors of limited proteolytic sites in native protein structures. Protein Eng 1998;11:349-359.
    • (1998) Protein Eng , vol.11 , pp. 349-359
    • Hubbard, S.J.1    Beynon, R.J.2    Thornton, J.M.3
  • 81
    • 0028336661 scopus 로고
    • Modeling studies of the change in conformation required for cleavage of limited proteolytic sites
    • Hubbard SJ, Eisenmenger F, Thornton JM. Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci 1994;3:757-768.
    • (1994) Protein Sci , vol.3 , pp. 757-768
    • Hubbard, S.J.1    Eisenmenger, F.2    Thornton, J.M.3
  • 82
    • 0025912338 scopus 로고
    • Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors
    • Hubbard SJ, Campbell SF, Thornton JM. Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors. J Mol Biol 1991;220:507-530.
    • (1991) J Mol Biol , vol.220 , pp. 507-530
    • Hubbard, S.J.1    Campbell, S.F.2    Thornton, J.M.3
  • 83
    • 0023140225 scopus 로고
    • Correlation among sites of limited proteolysis, enzyme accessibility and segmental mobility
    • Novotny J, Bruccoleri RE. Correlation among sites of limited proteolysis, enzyme accessibility and segmental mobility. FEBS Lett 1987;211:185-189.
    • (1987) FEBS Lett , vol.211 , pp. 185-189
    • Novotny, J.1    Bruccoleri, R.E.2
  • 86
    • 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. 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 2003;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
  • 87
    • 9644252804 scopus 로고    scopus 로고
    • Characterization of segments from the central region of BRCA1: An intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions?
    • Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? J Mol Biol 2005;345:275-287.
    • (2005) J Mol Biol , vol.345 , pp. 275-287
    • Mark, W.Y.1    Liao, J.C.2    Lu, Y.3    Ayed, A.4    Laister, R.5    Szymczyna, B.6    Chakrabartty, A.7    Arrowsmith, C.H.8
  • 88
    • 33749028479 scopus 로고    scopus 로고
    • Conformational properties of the SDS-bound state of alphasynuclein probed by limited proteolysis: Unexpected rigidity of the acidic C-terminal tail
    • de Laureto PP, Tosatto L, Frare E, Marin O, Uversky VN, Fontana A. Conformational properties of the SDS-bound state of alphasynuclein probed by limited proteolysis: unexpected rigidity of the acidic C-terminal tail. Biochemistry 2006;45:11523-11531.
    • (2006) Biochemistry , vol.45 , pp. 11523-11531
    • de Laureto, P.P.1    Tosatto, L.2    Frare, E.3    Marin, O.4    Uversky, V.N.5    Fontana, A.6
  • 90
    • 0032574795 scopus 로고    scopus 로고
    • Transcriptional activator-coactivator recognition: Nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding
    • Hua QX, Jia WH, Bullock BP, Habener JF, Weiss MA. Transcriptional activator-coactivator recognition: nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding. Biochemistry 1998;37:5858-5866.
    • (1998) Biochemistry , vol.37 , pp. 5858-5866
    • Hua, Q.X.1    Jia, W.H.2    Bullock, B.P.3    Habener, J.F.4    Weiss, M.A.5
  • 91
    • 0034677220 scopus 로고    scopus 로고
    • Model for stathmin/OP18 binding to tubulin
    • Wallon G, Rappsilber J, Mann M, Serrano L. Model for stathmin/OP18 binding to tubulin. EMBO J 2000;19:213-222.
    • (2000) EMBO J , vol.19 , pp. 213-222
    • Wallon, G.1    Rappsilber, J.2    Mann, M.3    Serrano, L.4
  • 92
    • 0034598940 scopus 로고    scopus 로고
    • Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system
    • Zitzewitz JA, Ibarra-Molero B, Fishel DR, Terry KL, Matthews CR. Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system. J Mol Biol 2000;296:1105-1116.
    • (2000) J Mol Biol , vol.296 , pp. 1105-1116
    • Zitzewitz, J.A.1    Ibarra-Molero, B.2    Fishel, D.R.3    Terry, K.L.4    Matthews, C.R.5
  • 93
    • 33746032693 scopus 로고    scopus 로고
    • Solution NMR studies of an intrinsically unstructured protein within a dilute, 75 kDa eukaryotic protein assembly; probing the practical limits for efficiently assigning polypeptide backbone resonances
    • Wang Y, Filippov I, Richter C, Luo R, Kriwacki RW. Solution NMR studies of an intrinsically unstructured protein within a dilute, 75 kDa eukaryotic protein assembly; probing the practical limits for efficiently assigning polypeptide backbone resonances. Chembiochem 2005;6:2242-2246.
    • (2005) Chembiochem , vol.6 , pp. 2242-2246
    • Wang, Y.1    Filippov, I.2    Richter, C.3    Luo, R.4    Kriwacki, R.W.5
  • 95
    • 39049162291 scopus 로고    scopus 로고
    • Role of intrinsic flexibility in signal transduction mediated by the cell cycle regulator, p27 Kip1
    • Galea CA, Nourse A, Wang Y, Sivakolundu SG, Heller WT, Kriwacki RW. Role of intrinsic flexibility in signal transduction mediated by the cell cycle regulator, p27 Kip1. J Mol Biol 2008;376:827-838.
    • (2008) J Mol Biol , vol.376 , pp. 827-838
    • Galea, C.A.1    Nourse, A.2    Wang, Y.3    Sivakolundu, S.G.4    Heller, W.T.5    Kriwacki, R.W.6
  • 97
    • 16644393375 scopus 로고    scopus 로고
    • Cell cycle regulatory protein p27KIP1 is a substrate and interacts with the protein kinase CK2
    • Tapia JC, Bolanos-Garcia VM, Sayed M, Allende CC, Allende JE. Cell cycle regulatory protein p27KIP1 is a substrate and interacts with the protein kinase CK2. J Cell Biochem 2004;91:865-879.
    • (2004) J Cell Biochem , vol.91 , pp. 865-879
    • Tapia, J.C.1    Bolanos-Garcia, V.M.2    Sayed, M.3    Allende, C.C.4    Allende, J.E.5
  • 98
    • 34248333450 scopus 로고    scopus 로고
    • Conformational changes upon calcium binding and phosphorylation in a synthetic fragment of calmodulin
    • Settimo L, Donnini S, Juffer AH, Woody RW, Marin O. Conformational changes upon calcium binding and phosphorylation in a synthetic fragment of calmodulin. Biopolymers 2007;88:373-385.
    • (2007) Biopolymers , vol.88 , pp. 373-385
    • Settimo, L.1    Donnini, S.2    Juffer, A.H.3    Woody, R.W.4    Marin, O.5
  • 99
    • 0141838136 scopus 로고    scopus 로고
    • Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site
    • Klein P, Pawson T, Tyers M. Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site. Curr Biol 2003;13:1669-1678.
    • (2003) Curr Biol , vol.13 , pp. 1669-1678
    • Klein, P.1    Pawson, T.2    Tyers, M.3
  • 101
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interaction
    • Tompa P, Fuxreiter M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interaction. Trends Biochem Sci 2008;33:2-8.
    • (2008) Trends Biochem Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 102
    • 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. Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proc Natl Acad Sci U S A 2007;104:9650-9655.
    • (2007) Proc Natl Acad Sci U S A , 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
  • 103
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to thermostability
    • Vihinen M. Relationship of protein flexibility to thermostability. Protein Eng 1987;1:477-480.
    • (1987) Protein Eng , vol.1 , pp. 477-480
    • Vihinen, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.