메뉴 건너뛰기




Volumn 21, Issue 8, 2012, Pages 1222-1230

Designing redox potential-controlled protein switches based on mutually exclusive proteins

Author keywords

Mutually exclusive protein; Protein folding and unfolding; Protein switch; Stopped flow spectrofluorometry

Indexed keywords

IMMUNOGLOBULIN G;

EID: 84863807314     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2109     Document Type: Article
Times cited : (16)

References (34)
  • 1
    • 79957473559 scopus 로고    scopus 로고
    • ARF family G proteins and their regulators: Roles in membrane transport, development and disease
    • Donaldson JG, Jackson CL (2011) ARF family G proteins and their regulators: roles in membrane transport, development and disease. Nat Rev Mol Cell Biol 12:362-375.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 362-375
    • Donaldson, J.G.1    Jackson, C.L.2
  • 2
    • 79960706295 scopus 로고    scopus 로고
    • The 'invisible hand': Regulation of RHO GTPases by RHOGDIs
    • Garcia-Mata R, Boulter E, Burridge K (2011) The 'invisible hand': regulation of RHO GTPases by RHOGDIs. Nat Rev Mol Cell Biol 12:493-504.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 493-504
    • Garcia-Mata, R.1    Boulter, E.2    Burridge, K.3
  • 3
    • 79958768182 scopus 로고    scopus 로고
    • MOB control: Reviewing a conserved family of kinase regulators
    • Hergovich A (2011) MOB control: reviewing a conserved family of kinase regulators. Cell Signal 23:1433-1440.
    • (2011) Cell Signal , vol.23 , pp. 1433-1440
    • Hergovich, A.1
  • 4
    • 79551647444 scopus 로고    scopus 로고
    • Switching TGFbeta from a tumor suppressor to a tumor promoter
    • Inman GJ (2011) Switching TGFbeta from a tumor suppressor to a tumor promoter. Curr Opin Genet Dev 21:93-99.
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 93-99
    • Inman, G.J.1
  • 5
    • 79955632686 scopus 로고    scopus 로고
    • Complex regulation and function of activation-induced cytidine deaminase
    • Stavnezer J (2011) Complex regulation and function of activation-induced cytidine deaminase. Trends Immunol 32:194-201.
    • (2011) Trends Immunol , vol.32 , pp. 194-201
    • Stavnezer, J.1
  • 7
    • 33746635140 scopus 로고    scopus 로고
    • Design of protein conformational switches
    • DOI 10.1016/j.sbi.2006.05.014, PII S0959440X06000984
    • Ambroggio XI, Kuhlman B (2006) Design of protein conformational switches. Curr Opin Struct Biol 16:525-530. (Pubitemid 44149060)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.4 , pp. 525-530
    • Ambroggio, X.I.1    Kuhlman, B.2
  • 9
    • 69249087672 scopus 로고    scopus 로고
    • Designing switchable enzymes
    • Ostermeier M (2009) Designing switchable enzymes. Curr Opin Struct Biol 19:442-448.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 442-448
    • Ostermeier, M.1
  • 10
    • 70349770900 scopus 로고    scopus 로고
    • Generation of new protein functions by nonhomologous combinations and rearrangements of domains and modules
    • Koide S (2009) Generation of new protein functions by nonhomologous combinations and rearrangements of domains and modules. Curr Opin Biotech 20:398-404.
    • (2009) Curr Opin Biotech , vol.20 , pp. 398-404
    • Koide, S.1
  • 11
    • 77955984136 scopus 로고    scopus 로고
    • Structure-switching biosensors: Inspired by Nature
    • Vallee-Belisle A, Plaxco KW (2010) Structure-switching biosensors: inspired by Nature. Curr Opin Struct Biol 20:518-526.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 518-526
    • Vallee-Belisle, A.1    Plaxco, K.W.2
  • 12
    • 78650796409 scopus 로고    scopus 로고
    • Converting a protein into a switch for biosensing and functional regulation
    • Stratton MM, Loh SN (2011) Converting a protein into a switch for biosensing and functional regulation. Protein Sci 20:19-29.
    • (2011) Protein Sci , vol.20 , pp. 19-29
    • Stratton, M.M.1    Loh, S.N.2
  • 13
    • 79951671135 scopus 로고    scopus 로고
    • Design and application of genetically encoded biosensors
    • Palmer AE, Qin Y, Park JG, McCombs JE (2011) Design and application of genetically encoded biosensors. Trends Biotech 29:144-152.
    • (2011) Trends Biotech , vol.29 , pp. 144-152
    • Palmer, A.E.1    Qin, Y.2    Park, J.G.3    McCombs, J.E.4
  • 14
    • 62349086577 scopus 로고    scopus 로고
    • Beyond molecular beacons: Optical sensors based on the binding-induced folding of proteins and polypeptides
    • Oh KJ, Cash KJ, Plaxco KW (2009) Beyond molecular beacons: optical sensors based on the binding-induced folding of proteins and polypeptides. Chemistry 15:2244-2251.
    • (2009) Chemistry , vol.15 , pp. 2244-2251
    • Oh, K.J.1    Cash, K.J.2    Plaxco, K.W.3
  • 16
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • DOI 10.1126/science.1085945
    • Dueber JE, Yeh BJ, Chak K, Lim WA (2003) Reprogramming control of an allosteric signaling switch through modular recombination. Science 301:1904-1908. (Pubitemid 37221395)
    • (2003) Science , vol.301 , Issue.5641 , pp. 1904-1908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 18
    • 34247465989 scopus 로고    scopus 로고
    • Engineering modular protein interaction switches by sequence overlap
    • DOI 10.1021/ja0672728
    • Sallee NA, Yeh BJ, Lim WA (2007) Engineering modular protein interaction switches by sequence overlap. J Am Chem Soc 129:4606-4611. (Pubitemid 46648759)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.15 , pp. 4606-4611
    • Sallee, N.A.1    Yeh, B.J.2    Lim, W.A.3
  • 19
    • 49449118042 scopus 로고    scopus 로고
    • Light-activated DNA binding in a designed allosteric protein
    • Strickland D, Moffat K, Sosnick TR (2008) Light-activated DNA binding in a designed allosteric protein. Proc Natl Acad Sci USA 105:10709-10714.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10709-10714
    • Strickland, D.1    Moffat, K.2    Sosnick, T.R.3
  • 22
    • 34447273196 scopus 로고    scopus 로고
    • Thermodynamic Analysis of an Antagonistic Folding-Unfolding Equilibrium Between Two Protein Domains
    • DOI 10.1016/j.jmb.2007.05.077, PII S0022283607007358
    • Cutler TA, Loh SN (2007) Thermodynamic analysis of an antagonistic folding-unfolding equilibrium between two protein domains. J Mol Biol 371:308-316. (Pubitemid 47048284)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.2 , pp. 308-316
    • Cutler, T.A.1    Loh, S.N.2
  • 23
    • 33644831449 scopus 로고    scopus 로고
    • Modular enzyme design: Regulation by mutually exclusive protein folding
    • DOI 10.1016/j.jmb.2006.01.073, PII S0022283606001148
    • Ha JH, Butler JS, Mitrea DM, Loh SN (2006) Modular enzyme design: regulation by mutually exclusive protein folding. J Mol Biol 357:1058-1062. (Pubitemid 43357972)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.4 , pp. 1058-1062
    • Ha, J.-H.1    Butler, J.S.2    Mitrea, D.M.3    Loh, S.N.4
  • 24
    • 59649096956 scopus 로고    scopus 로고
    • Effect of interdomain linker length on an antagonistic folding-unfolding equilibrium between two protein domains
    • Cutler TA, Mills BM, Lubin DJ, Chong LT, Loh SN (2009) Effect of interdomain linker length on an antagonistic folding-unfolding equilibrium between two protein domains. J Mol Biol 386:854-868.
    • (2009) J Mol Biol , vol.386 , pp. 854-868
    • Cutler, T.A.1    Mills, B.M.2    Lubin, D.J.3    Chong, L.T.4    Loh, S.N.5
  • 25
    • 70349386569 scopus 로고    scopus 로고
    • Direct observation of tug-of-war during the folding of a mutually exclusive protein
    • Peng Q, Li H (2009) Direct observation of tug-of-war during the folding of a mutually exclusive protein. J Am Chem Soc 131:13347-13354.
    • (2009) J Am Chem Soc , vol.131 , pp. 13347-13354
    • Peng, Q.1    Li, H.2
  • 26
    • 0022384947 scopus 로고
    • Protein G: A powerful tool for binding and detection of monoclonal and polyclonal antibodies
    • Akerstrom B, Brodin T, Reis K, Bjorck L (1985) Protein G: a powerful tool for binding and detection of monoclonal and polyclonal antibodies. J Immunol 135: 2589-2592. (Pubitemid 16215854)
    • (1985) Journal of Immunology , vol.135 , Issue.4 , pp. 2589-2592
    • Akerstrom, B.1    Brodin, T.2    Reis, K.3    Bjorck, L.4
  • 27
    • 44149110851 scopus 로고    scopus 로고
    • Configurational entropy modulates the mechanical stability of protein GB1
    • Li H, Wang HC, Cao Y, Sharma D, Wang M (2008) Configurational entropy modulates the mechanical stability of protein GB1. J Mol Biol 379:871-880.
    • (2008) J Mol Biol , vol.379 , pp. 871-880
    • Li, H.1    Wang, H.C.2    Cao, Y.3    Sharma, D.4    Wang, M.5
  • 28
    • 0029644247 scopus 로고
    • Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG
    • Sauer-Eriksson AE, Kleywegt GJ, Uhlen M, Jones TA (1995) Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 3:265-278.
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1    Kleywegt, G.J.2    Uhlen, M.3    Jones, T.A.4
  • 29
    • 42649120688 scopus 로고    scopus 로고
    • Protein-protein interaction regulates proteins' mechanical stability
    • Cao Y, Yoo T, Zhuang S, Li H (2008) Protein-protein interaction regulates proteins' mechanical stability. J Mol Biol 378:1132-1141.
    • (2008) J Mol Biol , vol.378 , pp. 1132-1141
    • Cao, Y.1    Yoo, T.2    Zhuang, S.3    Li, H.4
  • 31
    • 79952805688 scopus 로고    scopus 로고
    • The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function
    • Morrone A, McCully ME, Bryan PN, Brunori M, Daggett V, Gianni S, Travaglini-Allocatelli C (2011) The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function. J Biol Chem 286:3863-3872.
    • (2011) J Biol Chem , vol.286 , pp. 3863-3872
    • Morrone, A.1    McCully, M.E.2    Bryan, P.N.3    Brunori, M.4    Daggett, V.5    Gianni, S.6    Travaglini-Allocatelli, C.7
  • 32
    • 0032867418 scopus 로고    scopus 로고
    • Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing
    • DOI 10.1038/13311
    • Park SH, Shastry MC, Roder H (1999) Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing. Nat Struct Biol 6:943-947. (Pubitemid 29463308)
    • (1999) Nature Structural Biology , vol.6 , Issue.10 , pp. 943-947
    • Park, S.-H.1    Shastry, M.C.R.2    Roder, H.3
  • 33
    • 0034687150 scopus 로고    scopus 로고
    • Nanosecond dynamics of the single tryptophan reveals multi-state equilibrium unfolding of protein GB1
    • Tcherkasskaya O, Knutson JR, Bowley SA, Frank MK, Gronenborn AM (2000) Nanosecond dynamics of the single tryptophan reveals multi-state equilibrium unfolding of protein GB1. Biochemistry 39:11216-11226.
    • (2000) Biochemistry , vol.39 , pp. 11216-11226
    • Tcherkasskaya, O.1    Knutson, J.R.2    Bowley, S.A.3    Frank, M.K.4    Gronenborn, A.M.5
  • 34
    • 65249094239 scopus 로고    scopus 로고
    • Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase
    • Butler JS, Mitrea DM, Mitrousis G, Cingolani G, Loh SN (2009) Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. Biochemistry 48:3497-3507.
    • (2009) Biochemistry , vol.48 , pp. 3497-3507
    • Butler, J.S.1    Mitrea, D.M.2    Mitrousis, G.3    Cingolani, G.4    Loh, S.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.