메뉴 건너뛰기




Volumn 104, Issue 1, 2013, Pages 63-74

Kinetics of ligand-receptor interaction reveals an induced-fit mode of binding in a cyclic nucleotide-activated protein

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL PROTEIN; CELL SURFACE RECEPTOR; CYCLIC NUCLEOTIDE GATED CHANNEL; LIGAND; MUTANT PROTEIN;

EID: 84872123461     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.11.3816     Document Type: Article
Times cited : (32)

References (69)
  • 1
    • 78650882598 scopus 로고    scopus 로고
    • Cooperative and uncooperative cyclic-nucleotide-gated ion channels
    • A. Cukkemane, R. Seifert, and U.B. Kaupp Cooperative and uncooperative cyclic-nucleotide-gated ion channels Trends Biochem. Sci. 36 2011 55 64
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 55-64
    • Cukkemane, A.1    Seifert, R.2    Kaupp, U.B.3
  • 2
    • 0036301043 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels
    • U.B. Kaupp, and R. Seifert Cyclic nucleotide-gated ion channels Physiol. Rev. 82 2002 769 824 (Pubitemid 34743338)
    • (2002) Physiological Reviews , vol.82 , Issue.3 , pp. 769-824
    • Kaupp, U.B.1    Seifert, R.2
  • 3
    • 0014985944 scopus 로고
    • An adenosine 3′:5′-cyclic monophosphate-binding protein that acts on the transcription process
    • L. Eron, and R. Arditti J.R. Beckwith An adenosine 3′:5′- cyclic monophosphate-binding protein that acts on the transcription process Proc. Natl. Acad. Sci. USA 68 1971 215 218
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 215-218
    • Eron, L.1    Arditti, R.2    Beckwith, J.R.3
  • 4
    • 0019463941 scopus 로고
    • Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
    • DOI 10.1038/290744a0
    • D.B. McKay, and T.A. Steitz Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA Nature 290 1981 744 749 (Pubitemid 11068041)
    • (1981) Nature , vol.290 , Issue.5809 , pp. 744-749
    • McKay, D.B.1    Steitz, T.A.2
  • 5
    • 69249241732 scopus 로고    scopus 로고
    • Structural overview on the allosteric activation of cyclic AMP receptor protein
    • H.S. Won, and Y.S. Lee B.J. Lee Structural overview on the allosteric activation of cyclic AMP receptor protein Biochim. Biophys. Acta 1794 2009 1299 1308
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1299-1308
    • Won, H.S.1    Lee, Y.S.2    Lee, B.J.3
  • 6
    • 0014779269 scopus 로고
    • Mechanism of activation of catabolite-sensitive genes: A positive control system
    • G. Zubay, D. Schwartz, and J. Beckwith Mechanism of activation of catabolite-sensitive genes: a positive control system Proc. Natl. Acad. Sci. USA 66 1970 104 110
    • (1970) Proc. Natl. Acad. Sci. USA , vol.66 , pp. 104-110
    • Zubay, G.1    Schwartz, D.2    Beckwith, J.3
  • 7
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • S.S. Taylor, and A.P. Kornev Protein kinases: evolution of dynamic regulatory proteins Trends Biochem. Sci. 36 2011 65 77
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 8
    • 0032848914 scopus 로고    scopus 로고
    • Cyclic nucleotide-dependent protein kinases: Intracellular receptors for cAMP and cGMP action
    • DOI 10.1080/10408369991239213
    • S.H. Francis, and J.D. Corbin Cyclic nucleotide-dependent protein kinases: intracellular receptors for cAMP and cGMP action Crit. Rev. Clin. Lab. Sci. 36 1999 275 328 (Pubitemid 29431414)
    • (1999) Critical Reviews in Clinical Laboratory Sciences , vol.36 , Issue.4 , pp. 275-328
    • Francis, S.H.1    Corbin, J.D.2
  • 9
    • 0014962127 scopus 로고
    • Cyclic nucleotide-dependent protein kinases. VI. Isolation and partial purification of a protein kinase activated by guanosine 3′,5′- monophosphate
    • J.F. Kuo, and P. Greengard Cyclic nucleotide-dependent protein kinases. VI. Isolation and partial purification of a protein kinase activated by guanosine 3′,5′-monophosphate J. Biol. Chem. 245 1970 2493 2498
    • (1970) J. Biol. Chem. , vol.245 , pp. 2493-2498
    • Kuo, J.F.1    Greengard, P.2
  • 10
    • 0014409394 scopus 로고
    • An adenosine 3′,5′-monophosphate-dependant protein kinase from rabbit skeletal muscle
    • D.A. Walsh, J.P. Perkins, and E.G. Krebs An adenosine 3′,5′-monophosphate-dependant protein kinase from rabbit skeletal muscle J. Biol. Chem. 243 1968 3763 3765
    • (1968) J. Biol. Chem. , vol.243 , pp. 3763-3765
    • Walsh, D.A.1    Perkins, J.P.2    Krebs, E.G.3
  • 11
    • 33947480382 scopus 로고
    • Studies on UDPG-α-glucan transglucosylase. III. Interconversion of two forms of muscle UDPG-α-glucan transglucosylase by a phosphorylation-dephosphorylation reaction sequence
    • D.L. Friedman, and J. Larner Studies on UDPG-α-glucan transglucosylase. III. Interconversion of two forms of muscle UDPG-α-glucan transglucosylase by a phosphorylation-dephosphorylation reaction sequence Biochemistry 2 1963 669 675
    • (1963) Biochemistry , vol.2 , pp. 669-675
    • Friedman, D.L.1    Larner, J.2
  • 12
    • 77949538387 scopus 로고    scopus 로고
    • Epac: Defining a new mechanism for cAMP action
    • M. Gloerich, and J.L. Bos Epac: defining a new mechanism for cAMP action Annu. Rev. Pharmacol. Toxicol. 50 2010 355 375
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 355-375
    • Gloerich, M.1    Bos, J.L.2
  • 13
    • 33751241720 scopus 로고    scopus 로고
    • Epac proteins: Multi-purpose cAMP targets
    • DOI 10.1016/j.tibs.2006.10.002, PII S0968000406002921
    • J.L. Bos Epac proteins: multi-purpose cAMP targets Trends Biochem. Sci. 31 2006 680 686 (Pubitemid 44791945)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.12 , pp. 680-686
    • Bos, J.L.1
  • 15
    • 0032508032 scopus 로고    scopus 로고
    • Molecular identification of a hyperpolarization-activated channel in sea urchin sperm
    • DOI 10.1038/31248
    • R. Gauss, R. Seifert, and U.B. Kaupp Molecular identification of a hyperpolarization-activated channel in sea urchin sperm Nature 393 1998 583 587 (Pubitemid 28319248)
    • (1998) Nature , vol.393 , Issue.6685 , pp. 583-587
    • Gauss, R.1    Seifert, R.2    Kaupp, U.B.3
  • 17
    • 8844263765 scopus 로고    scopus 로고
    • Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel
    • DOI 10.1016/j.cell.2004.10.030, PII S0092867404010359
    • G.M. Clayton, and W.R. Silverman J.H. Morais-Cabral Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel Cell 119 2004 615 627 (Pubitemid 39535750)
    • (2004) Cell , vol.119 , Issue.5 , pp. 615-627
    • Clayton, G.M.1    Silverman, W.R.2    Heginbotham, L.3    Morais-Cabral, J.H.4
  • 18
    • 33845800991 scopus 로고    scopus 로고
    • Capturing cyclic nucleotides in action: Snapshots from crystallographic studies
    • DOI 10.1038/nrm2082, PII NRM2082
    • H. Rehmann, A. Wittinghofer, and J.L. Bos Capturing cyclic nucleotides in action: snapshots from crystallographic studies Nat. Rev. Mol. Cell Biol. 8 2007 63 73 (Pubitemid 46012015)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.1 , pp. 63-73
    • Rehmann, H.1    Wittinghofer, A.2    Bos, J.L.3
  • 19
    • 79955011398 scopus 로고    scopus 로고
    • Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel
    • S. Schünke, and M. Stoldt D. Willbold Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel Proc. Natl. Acad. Sci. USA 108 2011 6121 6126
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 6121-6126
    • Schünke, S.1    Stoldt, M.2    Willbold, D.3
  • 20
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • H. Frauenfelder, S.G. Sligar, and P.G. Wolynes The energy landscapes and motions of proteins Science 254 1991 1598 1603 (Pubitemid 21917496)
    • (1991) Science , vol.254 , Issue.5038 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 21
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • D.E. Koshland Application of a theory of enzyme specificity to protein synthesis Proc. Natl. Acad. Sci. USA 44 1958 98 104
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 22
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • C.J. Tsai, and S. Kumar R. Nussinov Folding funnels, binding funnels, and protein function Protein Sci. 8 1999 1181 1190 (Pubitemid 29264948)
    • (1999) Protein Science , vol.8 , Issue.6 , pp. 1181-1190
    • Tsai, C.-J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 23
    • 77957231785 scopus 로고    scopus 로고
    • Induced fit, conformational selection and independent dynamic segments: An extended view of binding events
    • P. Csermely, R. Palotai, and R. Nussinov Induced fit, conformational selection and independent dynamic segments: an extended view of binding events Trends Biochem. Sci. 35 2010 539 546
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 24
    • 65249090946 scopus 로고    scopus 로고
    • Selected-fit versus induced-fit protein binding: Kinetic differences and mutational analysis
    • T.R. Weikl, and C. von Deuster Selected-fit versus induced-fit protein binding: kinetic differences and mutational analysis Proteins 75 2009 104 110
    • (2009) Proteins , vol.75 , pp. 104-110
    • Weikl, T.R.1    Von Deuster, C.2
  • 25
    • 84872142634 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 26
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • DOI 10.1038/nature06522, PII NATURE06522
    • K. Henzler-Wildman, and D. Kern Dynamic personalities of proteins Nature 450 2007 964 972 (Pubitemid 350273626)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 29
    • 79551678422 scopus 로고    scopus 로고
    • Mechanisms of protein-ligand association and its modulation by protein mutations
    • M. Held, and P. Metzner F. Noé Mechanisms of protein-ligand association and its modulation by protein mutations Biophys. J. 100 2011 701 710
    • (2011) Biophys. J. , vol.100 , pp. 701-710
    • Held, M.1    Metzner, P.2    Noé, F.3
  • 30
    • 0017845014 scopus 로고
    • Test reactions for a stopped-flow apparatus. Reduction of 2,6 dichlorophenolindophenol and potassium ferricyanide by L-ascorbic acid
    • B. Tonomura, and H. Nakatani K. Hiromi Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichlorophenolindophenol and potassium ferricyanide by L-ascorbic acid Anal. Biochem. 84 1978 370 383 (Pubitemid 8279555)
    • (1978) Analytical Biochemistry , vol.84 , Issue.2 , pp. 370-383
    • Tonomura, B.1    Nakatani, H.2    Ohnishi, M.3
  • 31
    • 84857364039 scopus 로고    scopus 로고
    • Calculating kinetics and pathways of protein-ligand association
    • M. Held, and F. Noé Calculating kinetics and pathways of protein-ligand association Eur. J. Cell Biol. 91 2012 357 364
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 357-364
    • Held, M.1    Noé, F.2
  • 32
    • 70450255797 scopus 로고    scopus 로고
    • Constructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations
    • F. Noé, and C. Schütte T.R. Weikl Constructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations Proc. Natl. Acad. Sci. USA 106 2009 19011 19016
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19011-19016
    • Noé, F.1    Schütte, C.2    Weikl, T.R.3
  • 34
    • 3242886771 scopus 로고    scopus 로고
    • PDB 2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • T.J. Dolinsky, and J.E. Nielsen N.A. Baker PDB 2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations Nucleic Acids Res. 32 Web Server issue 2004 W665 W667
    • (2004) Nucleic Acids Res. , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    Baker, N.A.3
  • 36
    • 0025388039 scopus 로고
    • Prediction of diffusion coefficients of proteins
    • M.T. Tyn, and T.W. Gusek Prediction of diffusion coefficients of proteins Biotechnol. Bioeng. 35 1990 327 338 (Pubitemid 20137339)
    • (1990) Biotechnology and Bioengineering , vol.35 , Issue.4 , pp. 327-338
    • Tyn, M.T.1    Gusek, T.W.2
  • 37
    • 0017620144 scopus 로고
    • Solubility and diffusion coefficient of adenosine 3:5 monophosphate
    • M. Dworkin, and K.H. Keller Solubility and diffusion coefficient of adenosine 3′:5′-monophosphate J. Biol. Chem. 252 1977 864 865 (Pubitemid 8041875)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.3 , pp. 864-865
    • Dworkin, M.1    Keller, K.H.2
  • 39
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • DOI 10.1006/abio.1996.0238
    • P. Kuzmic Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase Anal. Biochem. 237 1996 260 273 (Pubitemid 26177089)
    • (1996) Analytical Biochemistry , vol.237 , Issue.2 , pp. 260-273
    • Kuzmic, P.1
  • 40
    • 0027386759 scopus 로고
    • Acetylcholinesterase: Electrostatic steering increases the rate of ligand binding
    • DOI 10.1021/bi00053a003
    • R.C. Tan, and T.N. Truong J.L. Sussman Acetylcholinesterase: electrostatic steering increases the rate of ligand binding Biochemistry 32 1993 401 403 (Pubitemid 23034875)
    • (1993) Biochemistry , vol.32 , Issue.2 , pp. 401-403
    • Tan, R.C.1    Truong, T.N.2    McCammon, J.A.3    Sussman, J.L.4
  • 42
    • 0010576408 scopus 로고    scopus 로고
    • Glossary of terms in quantities and units in clinical chemistry
    • H.P. Lehmann, X. Fuentes-Arderiu, and F. Bertello Glossary of terms in quantities and units in clinical chemistry Pure Appl. Chem. 68 1996 957 1000
    • (1996) Pure Appl. Chem. , vol.68 , pp. 957-1000
    • Lehmann, H.P.1    Fuentes-Arderiu, X.2    Bertello, F.3
  • 43
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein-protein association kinetics
    • G. Schreiber, G. Haran, and H.X. Zhou Fundamental aspects of protein-protein association kinetics Chem. Rev. 109 2009 839 860
    • (2009) Chem. Rev. , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.X.3
  • 44
    • 0032557503 scopus 로고    scopus 로고
    • Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
    • DOI 10.1006/jmbi.1998.1747
    • M. Vijayakumar, and K.Y. Wong H.X. Zhou Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar J. Mol. Biol. 278 1998 1015 1024 (Pubitemid 28239701)
    • (1998) Journal of Molecular Biology , vol.278 , Issue.5 , pp. 1015-1024
    • Vijayakumar, M.1    Wong, K.-Y.2    Schreiber, G.3    Fersht, A.R.4    Szabo, A.5    Zhou, H.-X.6
  • 45
    • 0029873697 scopus 로고    scopus 로고
    • Rapid, electrostatically assisted association of proteins
    • DOI 10.1038/nsb0596-427
    • G. Schreiber, and A.R. Fersht Rapid, electrostatically assisted association of proteins Nat. Struct. Biol. 3 1996 427 431 (Pubitemid 26139441)
    • (1996) Nature Structural Biology , vol.3 , Issue.5 , pp. 427-431
    • Schreiber, G.1    Fersht, A.R.2
  • 46
    • 0033612226 scopus 로고    scopus 로고
    • Biophysical analysis of the interaction of human ifnar2 expressed in E. coli with IFNα2
    • DOI 10.1006/jmbi.1999.2726
    • J. Piehler, and G. Schreiber Biophysical analysis of the interaction of human ifnar2 expressed in E. coli with IFNα2 J. Mol. Biol. 289 1999 57 67 (Pubitemid 29278363)
    • (1999) Journal of Molecular Biology , vol.289 , Issue.1 , pp. 57-67
    • Piehler, J.1    Schreiber, G.2
  • 47
    • 0031012271 scopus 로고    scopus 로고
    • Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper
    • DOI 10.1021/bi961672y
    • H. Wendt, and L. Leder H.R. Bosshard Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper Biochemistry 36 1997 204 213 (Pubitemid 27024694)
    • (1997) Biochemistry , vol.36 , Issue.1 , pp. 204-213
    • Wendt, H.1    Leder, L.2    Harma, H.3    Jelesarov, I.4    Baici, A.5    Bosshard, H.R.6
  • 48
    • 0037357714 scopus 로고    scopus 로고
    • A novel correlation for protein diffusion coefficients based on molecular weight and radius of gyration
    • DOI 10.1021/bp0256059
    • L. He, and B. Niemeyer A novel correlation for protein diffusion coefficients based on molecular weight and radius of gyration Biotechnol. Prog. 19 2003 544 548 (Pubitemid 36421008)
    • (2003) Biotechnology Progress , vol.19 , Issue.2 , pp. 544-548
    • He, L.1    Niemeyer, B.2
  • 49
    • 0000267310 scopus 로고
    • Attempt at a mathematical theory of the kinetics of coagulation for colloidal solutions [Versuch einer mathematischen theorie der koagulationskinetik kolloidaler lösungen]
    • M. Smoluchowski Attempt at a mathematical theory of the kinetics of coagulation for colloidal solutions [Versuch einer mathematischen theorie der koagulationskinetik kolloidaler lösungen] Z. Phys. Chem. 92 1917 129 168
    • (1917) Z. Phys. Chem. , vol.92 , pp. 129-168
    • Smoluchowski, M.1
  • 52
    • 47849110347 scopus 로고    scopus 로고
    • Structural and energetic analysis of activation by a cyclic nucleotide binding domain
    • S.L. Altieri, and G.M. Clayton J.H. Morais-Cabral Structural and energetic analysis of activation by a cyclic nucleotide binding domain J. Mol. Biol. 381 2008 655 669
    • (2008) J. Mol. Biol. , vol.381 , pp. 655-669
    • Altieri, S.L.1    Clayton, G.M.2    Morais-Cabral, J.H.3
  • 53
    • 67650064749 scopus 로고    scopus 로고
    • Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP
    • S. Schünke, and M. Stoldt D. Willbold Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP EMBO Rep. 10 2009 729 735
    • (2009) EMBO Rep. , vol.10 , pp. 729-735
    • Schünke, S.1    Stoldt, M.2    Willbold, D.3
  • 54
    • 84855517288 scopus 로고    scopus 로고
    • Gating of the MlotiK1 potassium channel involves large rearrangements of the cyclic nucleotide-binding domains
    • S.A. Mari, and J. Pessoa D.J. Müller Gating of the MlotiK1 potassium channel involves large rearrangements of the cyclic nucleotide-binding domains Proc. Natl. Acad. Sci. USA 108 2011 20802 20807
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20802-20807
    • Mari, S.A.1    Pessoa, J.2    Müller, D.J.3
  • 55
    • 0020199402 scopus 로고
    • Role of diffusion in ligand binding to macromolecules and cell-bound receptors
    • D. Shoup, and A. Szabo Role of diffusion in ligand binding to macromolecules and cell-bound receptors Biophys. J. 40 1982 33 39
    • (1982) Biophys. J. , vol.40 , pp. 33-39
    • Shoup, D.1    Szabo, A.2
  • 56
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • DOI 10.1038/nrd2082, PII NRD2082
    • R.A. Copeland, D.L. Pompliano, and T.D. Meek Drug-target residence time and its implications for lead optimization Nat. Rev. Drug Discov. 5 2006 730 739 (Pubitemid 44323700)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.9 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 57
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor - Ligand complexes and its effect on biological function
    • DOI 10.1021/bi8002023
    • P.J. Tummino, and R.A. Copeland Residence time of receptor-ligand complexes and its effect on biological function Biochemistry 47 2008 5481 5492 (Pubitemid 351711169)
    • (2008) Biochemistry , vol.47 , Issue.20 , pp. 5481-5492
    • Tummino, P.J.1    Copeland, R.A.2
  • 58
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • DOI 10.1038/nature01922
    • W.N. Zagotta, and N.B. Olivier E. Gouaux Structural basis for modulation and agonist specificity of HCN pacemaker channels Nature 425 2003 200 205 (Pubitemid 37150901)
    • (2003) Nature , vol.425 , Issue.6954 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 60
    • 84856107576 scopus 로고    scopus 로고
    • How subunits cooperate in cAMP-induced activation of homotetrameric HCN2 channels
    • J. Kusch, and S. Thon K. Benndorf How subunits cooperate in cAMP-induced activation of homotetrameric HCN2 channels Nat. Chem. Biol. 8 2012 162 169
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 162-169
    • Kusch, J.1    Thon, S.2    Benndorf, K.3
  • 63
    • 45849114398 scopus 로고    scopus 로고
    • Pathway and endpoint free energy calculations for cyclic nucleotide binding to HCN channels
    • L. Zhou, and S.A. Siegelbaum Pathway and endpoint free energy calculations for cyclic nucleotide binding to HCN channels Biophys. J. 94 2008 L90 L92
    • (2008) Biophys. J. , vol.94
    • Zhou, L.1    Siegelbaum, S.A.2
  • 64
    • 66349083528 scopus 로고    scopus 로고
    • Structural basis for cAMP-mediated allosteric control of the catabolite activator protein
    • N. Popovych, and S.R. Tzeng C.G. Kalodimos Structural basis for cAMP-mediated allosteric control of the catabolite activator protein Proc. Natl. Acad. Sci. USA 106 2009 6927 6932
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6927-6932
    • Popovych, N.1    Tzeng, S.R.2    Kalodimos, C.G.3
  • 66
    • 70450191983 scopus 로고    scopus 로고
    • Dynamic activation of an allosteric regulatory protein
    • S.R. Tzeng, and C.G. Kalodimos Dynamic activation of an allosteric regulatory protein Nature 462 2009 368 372
    • (2009) Nature , vol.462 , pp. 368-372
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 67
    • 44449130112 scopus 로고    scopus 로고
    • Structural dynamics in the activation of Epac
    • S.M. Harper, and H. Wienk H. Rehmann Structural dynamics in the activation of Epac J. Biol. Chem. 283 2008 6501 6508
    • (2008) J. Biol. Chem. , vol.283 , pp. 6501-6508
    • Harper, S.M.1    Wienk, H.2    Rehmann, H.3
  • 68
    • 77951877209 scopus 로고    scopus 로고
    • Tracking G-protein-coupled receptor activation using genetically encoded infrared probes
    • S. Ye, and E. Zaitseva R. Vogel Tracking G-protein-coupled receptor activation using genetically encoded infrared probes Nature 464 2010 1386 1389
    • (2010) Nature , vol.464 , pp. 1386-1389
    • Ye, S.1    Zaitseva, E.2    Vogel, R.3
  • 69
    • 71149088976 scopus 로고    scopus 로고
    • Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR
    • M.D. Bridges, K. Hideg, and W.L. Hubbell Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR Appl. Magn. Reson. 37 2010 363 390
    • (2010) Appl. Magn. Reson. , vol.37 , pp. 363-390
    • Bridges, M.D.1    Hideg, K.2    Hubbell, W.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.