메뉴 건너뛰기




Volumn 111, Issue 6, 2016, Pages 1180-1191

Ultraslow Water-Mediated Transmembrane Interactions Regulate the Activation of A2A Adenosine Receptor

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE A2 RECEPTOR AGONIST; ADENOSINE A2 RECEPTOR ANTAGONIST; ADENOSINE A2A RECEPTOR; PROTEIN BINDING; WATER;

EID: 84991624991     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2016.08.002     Document Type: Article
Times cited : (36)

References (74)
  • 1
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • 1 Rosenbaum, D.M., Rasmussen, S.G., Kobilka, B.K., The structure and function of G-protein-coupled receptors. Nature 459 (2009), 356–363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 3
    • 79959564813 scopus 로고    scopus 로고
    • 2A receptor structures reveal common features of GPCR activation
    • 2A receptor structures reveal common features of GPCR activation. Nature 474 (2011), 521–525.
    • (2011) Nature , vol.474 , pp. 521-525
    • Lebon, G.1    Warne, T.2    Tate, C.G.3
  • 4
    • 65449161390 scopus 로고    scopus 로고
    • Ligand binding and micro-switches in 7TM receptor structures
    • 4 Nygaard, R., Frimurer, T.M., et al., Schwartz, T.W., Ligand binding and micro-switches in 7TM receptor structures. Trends Pharmacol. Sci. 30 (2009), 249–259.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 249-259
    • Nygaard, R.1    Frimurer, T.M.2    Schwartz, T.W.3
  • 5
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G protein-coupled receptor superfamily
    • 5 Katritch, V., Cherezov, V., Stevens, R.C., Structure-function of the G protein-coupled receptor superfamily. Annu. Rev. Pharmacol. Toxicol. 53 (2013), 531–556.
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 7
    • 84898048030 scopus 로고    scopus 로고
    • Mapping the intramolecular signal transduction of G-protein coupled receptors
    • 7 Lee, Y., Choi, S., Hyeon, C., Mapping the intramolecular signal transduction of G-protein coupled receptors. Proteins 82 (2014), 727–743.
    • (2014) Proteins , vol.82 , pp. 727-743
    • Lee, Y.1    Choi, S.2    Hyeon, C.3
  • 8
    • 0033637521 scopus 로고    scopus 로고
    • The dynamics of protein hydration water: a quantitative comparison of molecular dynamics simulations and neutron-scattering experiments
    • 8 Tarek, M., Tobias, D.J., The dynamics of protein hydration water: a quantitative comparison of molecular dynamics simulations and neutron-scattering experiments. Biophys. J. 79 (2000), 3244–3257.
    • (2000) Biophys. J. , vol.79 , pp. 3244-3257
    • Tarek, M.1    Tobias, D.J.2
  • 9
    • 38849196324 scopus 로고    scopus 로고
    • Water as an active constituent in cell biology
    • 9 Ball, P., Water as an active constituent in cell biology. Chem. Rev. 108 (2008), 74–108.
    • (2008) Chem. Rev. , vol.108 , pp. 74-108
    • Ball, P.1
  • 11
    • 0033747018 scopus 로고    scopus 로고
    • Molecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study
    • 11 Tsai, A.M., Neumann, D.A., Bell, L.N., Molecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study. Biophys. J. 79 (2000), 2728–2732.
    • (2000) Biophys. J. , vol.79 , pp. 2728-2732
    • Tsai, A.M.1    Neumann, D.A.2    Bell, L.N.3
  • 12
    • 0037133342 scopus 로고    scopus 로고
    • Biological water at the protein surface: dynamical solvation probed directly with femtosecond resolution
    • 12 Pal, S.K., Peon, J., Zewail, A.H., Biological water at the protein surface: dynamical solvation probed directly with femtosecond resolution. Proc. Natl. Acad. Sci. USA 99 (2002), 1763–1768.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1763-1768
    • Pal, S.K.1    Peon, J.2    Zewail, A.H.3
  • 13
    • 84947751362 scopus 로고    scopus 로고
    • Biological water or rather water in biology?
    • 13 Jungwirth, P., Biological water or rather water in biology?. J. Phys. Chem. Lett. 6 (2015), 2449–2451.
    • (2015) J. Phys. Chem. Lett. , vol.6 , pp. 2449-2451
    • Jungwirth, P.1
  • 14
    • 78651261665 scopus 로고    scopus 로고
    • Solid-state ²H NMR shows equivalence of dehydration and osmotic pressures in lipid membrane deformation
    • 14 Mallikarjunaiah, K.J., Leftin, A., et al., Brown, M.F., Solid-state ²H NMR shows equivalence of dehydration and osmotic pressures in lipid membrane deformation. Biophys. J. 100 (2011), 98–107.
    • (2011) Biophys. J. , vol.100 , pp. 98-107
    • Mallikarjunaiah, K.J.1    Leftin, A.2    Brown, M.F.3
  • 15
    • 84921026921 scopus 로고    scopus 로고
    • Activation of G-protein-coupled receptors correlates with the formation of a continuous internal water pathway
    • 15 Yuan, S., Filipek, S., et al., Vogel, H., Activation of G-protein-coupled receptors correlates with the formation of a continuous internal water pathway. Nat. Commun., 5, 2014, 4733.
    • (2014) Nat. Commun. , vol.5 , pp. 4733
    • Yuan, S.1    Filipek, S.2    Vogel, H.3
  • 16
    • 84884237285 scopus 로고    scopus 로고
    • The role of water and sodium ions in the activation of the μ-opioid receptor
    • 16 Yuan, S., Vogel, H., Filipek, S., The role of water and sodium ions in the activation of the μ-opioid receptor. Angew. Chem. Int. Ed. Engl. 52 (2013), 10112–10115.
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 10112-10115
    • Yuan, S.1    Vogel, H.2    Filipek, S.3
  • 17
    • 84926443535 scopus 로고    scopus 로고
    • Functional water molecules in rhodopsin activation
    • 17 Sun, X., Ågren, H., Tu, Y., Functional water molecules in rhodopsin activation. J. Phys. Chem. B 118 (2014), 10863–10873.
    • (2014) J. Phys. Chem. B , vol.118 , pp. 10863-10873
    • Sun, X.1    Ågren, H.2    Tu, Y.3
  • 18
    • 84924561288 scopus 로고    scopus 로고
    • Structural biology. Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor
    • 18 Burg, J.S., Ingram, J.R., et al., Garcia, K.C., Structural biology. Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor. Science 347 (2015), 1113–1117.
    • (2015) Science , vol.347 , pp. 1113-1117
    • Burg, J.S.1    Ingram, J.R.2    Garcia, K.C.3
  • 19
    • 84892685953 scopus 로고    scopus 로고
    • Retinal ligand mobility explains internal hydration and reconciles active rhodopsin structures
    • 19 Leioatts, N., Mertz, B., et al., Brown, M.F., Retinal ligand mobility explains internal hydration and reconciles active rhodopsin structures. Biochemistry 53 (2014), 376–385.
    • (2014) Biochemistry , vol.53 , pp. 376-385
    • Leioatts, N.1    Mertz, B.2    Brown, M.F.3
  • 20
    • 84860448544 scopus 로고    scopus 로고
    • 2A adenosine receptor
    • 2A adenosine receptor. Biophys. J. 102 (2012), 2114–2120.
    • (2012) Biophys. J. , vol.102 , pp. 2114-2120
    • Lee, J.Y.1    Lyman, E.2
  • 21
    • 84935894718 scopus 로고    scopus 로고
    • 6.48 opens a gate for a continuous intrinsic water pathway during activation of the adenosine A2A receptor
    • 6.48 opens a gate for a continuous intrinsic water pathway during activation of the adenosine A2A receptor. Angew. Chem. 127 (2015), 566–569.
    • (2015) Angew. Chem. , vol.127 , pp. 566-569
    • Yuan, S.1    Hu, Z.2    Vogel, H.3
  • 23
    • 84904104510 scopus 로고    scopus 로고
    • 2 adrenergic receptor from active to inactive conformation and its implication for the closed/open state of the water channel: insight from molecular dynamics simulation, free energy calculation and Markov state model analysis
    • 2 adrenergic receptor from active to inactive conformation and its implication for the closed/open state of the water channel: insight from molecular dynamics simulation, free energy calculation and Markov state model analysis. Phys. Chem. Chem. Phys. 16 (2014), 15874–15885.
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 15874-15885
    • Bai, Q.1    Pérez-Sánchez, H.2    Yao, X.3
  • 24
    • 47049084133 scopus 로고    scopus 로고
    • Internal hydration increases during activation of the G-protein-coupled receptor rhodopsin
    • 24 Grossfield, A., Pitman, M.C., et al., Gawrisch, K., Internal hydration increases during activation of the G-protein-coupled receptor rhodopsin. J. Mol. Biol. 381 (2008), 478–486.
    • (2008) J. Mol. Biol. , vol.381 , pp. 478-486
    • Grossfield, A.1    Pitman, M.C.2    Gawrisch, K.3
  • 25
    • 77958499673 scopus 로고    scopus 로고
    • Coupling of retinal, protein, and water dynamics in squid rhodopsin
    • 25 Jardón-Valadez, E., Bondar, A.-N., Tobias, D.J., Coupling of retinal, protein, and water dynamics in squid rhodopsin. Biophys. J. 99 (2010), 2200–2207.
    • (2010) Biophys. J. , vol.99 , pp. 2200-2207
    • Jardón-Valadez, E.1    Bondar, A.-N.2    Tobias, D.J.3
  • 26
    • 78049415021 scopus 로고    scopus 로고
    • Induced effects of sodium ions on dopaminergic G-protein coupled receptors
    • 26 Selent, J., Sanz, F., et al., De Fabritiis, G., Induced effects of sodium ions on dopaminergic G-protein coupled receptors. PLOS Comput. Biol., 6, 2010, e1000884.
    • (2010) PLOS Comput. Biol. , vol.6 , pp. e1000884
    • Selent, J.1    Sanz, F.2    De Fabritiis, G.3
  • 27
    • 84861961427 scopus 로고    scopus 로고
    • Structural basis for allosteric regulation of GPCRs by sodium ions
    • 27 Liu, W., Chun, E., et al., Stevens, R.C., Structural basis for allosteric regulation of GPCRs by sodium ions. Science 337 (2012), 232–236.
    • (2012) Science , vol.337 , pp. 232-236
    • Liu, W.1    Chun, E.2    Stevens, R.C.3
  • 28
    • 84873685831 scopus 로고    scopus 로고
    • Molecular signatures of G-protein-coupled receptors
    • 28 Venkatakrishnan, A.J., Deupi, X., et al., Babu, M.M., Molecular signatures of G-protein-coupled receptors. Nature 494 (2013), 185–194.
    • (2013) Nature , vol.494 , pp. 185-194
    • Venkatakrishnan, A.J.1    Deupi, X.2    Babu, M.M.3
  • 29
    • 70350316769 scopus 로고    scopus 로고
    • Characterization of water wires inside hydrophobic tubular peptide structures
    • 29 Raghavender, U.S., Aravinda, S., et al., Balaram, P., Characterization of water wires inside hydrophobic tubular peptide structures. J. Am. Chem. Soc. 131 (2009), 15130–15132.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15130-15132
    • Raghavender, U.S.1    Aravinda, S.2    Balaram, P.3
  • 30
    • 78650750083 scopus 로고    scopus 로고
    • Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires
    • 30 Reddy, G., Straub, J.E., Thirumalai, D., Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires. Proc. Natl. Acad. Sci. USA 107 (2010), 21459–21464.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 21459-21464
    • Reddy, G.1    Straub, J.E.2    Thirumalai, D.3
  • 31
    • 84855945574 scopus 로고    scopus 로고
    • Role of water in protein aggregation and amyloid polymorphism
    • 31 Thirumalai, D., Reddy, G., Straub, J.E., Role of water in protein aggregation and amyloid polymorphism. Acc. Chem. Res. 45 (2012), 83–92.
    • (2012) Acc. Chem. Res. , vol.45 , pp. 83-92
    • Thirumalai, D.1    Reddy, G.2    Straub, J.E.3
  • 34
    • 79960181417 scopus 로고    scopus 로고
    • 2A receptor in complex with ZM241385 and the xanthines XAC and caffeine
    • 2A receptor in complex with ZM241385 and the xanthines XAC and caffeine. Structure 19 (2011), 1283–1293.
    • (2011) Structure , vol.19 , pp. 1283-1293
    • Doré, A.S.1    Robertson, N.2    Marshall, F.H.3
  • 35
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • 35 Phillips, J.C., Braun, R., et al., Schulten, K., Scalable molecular dynamics with NAMD. J. Comput. Chem. 26 (2005), 1781–1802.
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1    Braun, R.2    Schulten, K.3
  • 36
    • 33645786604 scopus 로고    scopus 로고
    • Importance of the CMAP correction to the CHARMM22 protein force field: dynamics of hen lysozyme
    • 36 Buck, M., Bouguet-Bonnet, S., et al., MacKerell, A.D. Jr., Importance of the CMAP correction to the CHARMM22 protein force field: dynamics of hen lysozyme. Biophys. J. 90 (2006), L36–L38.
    • (2006) Biophys. J. , vol.90 , pp. L36-L38
    • Buck, M.1    Bouguet-Bonnet, S.2    MacKerell, A.D.3
  • 37
    • 79958841703 scopus 로고    scopus 로고
    • SwissParam: a fast force field generation tool for small organic molecules
    • 37 Zoete, V., Cuendet, M.A., et al., Michielin, O., SwissParam: a fast force field generation tool for small organic molecules. J. Comput. Chem. 32 (2011), 2359–2368.
    • (2011) J. Comput. Chem. , vol.32 , pp. 2359-2368
    • Zoete, V.1    Cuendet, M.A.2    Michielin, O.3
  • 38
    • 80052268628 scopus 로고    scopus 로고
    • Fluid phase lipid areas and bilayer thicknesses of commonly used phosphatidylcholines as a function of temperature
    • 38 Kučerka, N., Nieh, M.-P., Katsaras, J., Fluid phase lipid areas and bilayer thicknesses of commonly used phosphatidylcholines as a function of temperature. Biochim. Biophys. Acta 1808 (2011), 2761–2771.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2761-2771
    • Kučerka, N.1    Nieh, M.-P.2    Katsaras, J.3
  • 39
    • 84876333477 scopus 로고    scopus 로고
    • A molecular dynamics study of the structural and dynamical properties of putative arsenic substituted lipid bilayers
    • 39 Tsai, H.-H.G., Lee, J.-B., et al., Juwita, R., A molecular dynamics study of the structural and dynamical properties of putative arsenic substituted lipid bilayers. Int. J. Mol. Sci. 14 (2013), 7702–7715.
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 7702-7715
    • Tsai, H.-H.G.1    Lee, J.-B.2    Juwita, R.3
  • 40
    • 0002300553 scopus 로고    scopus 로고
    • Hydrogen-bond kinetics in liquid water
    • 40 Luzar, A., Chandler, D., Hydrogen-bond kinetics in liquid water. Nature 379 (1996), 55–57.
    • (1996) Nature , vol.379 , pp. 55-57
    • Luzar, A.1    Chandler, D.2
  • 41
    • 84904558493 scopus 로고    scopus 로고
    • Dynamical transition and heterogeneous hydration dynamics in RNA
    • 41 Yoon, J., Lin, J.-C., et al., Thirumalai, D., Dynamical transition and heterogeneous hydration dynamics in RNA. J. Phys. Chem. B 118 (2014), 7910–7919.
    • (2014) J. Phys. Chem. B , vol.118 , pp. 7910-7919
    • Yoon, J.1    Lin, J.-C.2    Thirumalai, D.3
  • 42
    • 33750177351 scopus 로고
    • Centrality in social networks conceptual clarification
    • 42 Freeman, L., Centrality in social networks conceptual clarification. Soc. Networks 1 (1979), 215–239.
    • (1979) Soc. Networks , vol.1 , pp. 215-239
    • Freeman, L.1
  • 43
    • 0035826155 scopus 로고    scopus 로고
    • Exploring complex networks
    • 43 Strogatz, S.H., Exploring complex networks. Nature 410 (2001), 268–276.
    • (2001) Nature , vol.410 , pp. 268-276
    • Strogatz, S.H.1
  • 44
    • 0034721164 scopus 로고    scopus 로고
    • Error and attack tolerance of complex networks
    • 44 Albert, R., Jeong, H., Barabási, A.L., Error and attack tolerance of complex networks. Nature 406 (2000), 378–382.
    • (2000) Nature , vol.406 , pp. 378-382
    • Albert, R.1    Jeong, H.2    Barabási, A.L.3
  • 45
    • 13944252976 scopus 로고    scopus 로고
    • A measure of betweenness centrality based on random walks
    • 45 Newman, M., A measure of betweenness centrality based on random walks. Soc. Networks 27 (2005), 39–54.
    • (2005) Soc. Networks , vol.27 , pp. 39-54
    • Newman, M.1
  • 46
    • 0242720597 scopus 로고    scopus 로고
    • Uncovering network systems within protein structures
    • 46 Greene, L.H., Higman, V.A., Uncovering network systems within protein structures. J. Mol. Biol. 334 (2003), 781–791.
    • (2003) J. Mol. Biol. , vol.334 , pp. 781-791
    • Greene, L.H.1    Higman, V.A.2
  • 47
    • 8544221118 scopus 로고    scopus 로고
    • Network analysis of protein structures identifies functional residues
    • 47 Amitai, G., Shemesh, A., et al., Pietrokovski, S., Network analysis of protein structures identifies functional residues. J. Mol. Biol. 344 (2004), 1135–1146.
    • (2004) J. Mol. Biol. , vol.344 , pp. 1135-1146
    • Amitai, G.1    Shemesh, A.2    Pietrokovski, S.3
  • 48
    • 33745461893 scopus 로고    scopus 로고
    • Residues crucial for maintaining short paths in network communication mediate signaling in proteins
    • 48 Del Sol, A., Fujihashi, H., et al., Nussinov, R., Residues crucial for maintaining short paths in network communication mediate signaling in proteins. Mol. Sys. Biol., 2, 2006, 2006.0019.
    • (2006) Mol. Sys. Biol. , vol.2 , pp. 2006.0019
    • Del Sol, A.1    Fujihashi, H.2    Nussinov, R.3
  • 49
    • 34547909602 scopus 로고    scopus 로고
    • Assortative mixing in protein contact networks and protein folding kinetics
    • 49 Bagler, G., Sinha, S., Assortative mixing in protein contact networks and protein folding kinetics. Bioinformatics 23 (2007), 1760–1767.
    • (2007) Bioinformatics , vol.23 , pp. 1760-1767
    • Bagler, G.1    Sinha, S.2
  • 52
    • 0035648637 scopus 로고    scopus 로고
    • A faster algorithm for betweenness centrality
    • 52 Brandes, U., A faster algorithm for betweenness centrality. J. Math. Sociol. 25 (2001), 163–177.
    • (2001) J. Math. Sociol. , vol.25 , pp. 163-177
    • Brandes, U.1
  • 53
    • 84903720389 scopus 로고    scopus 로고
    • Probing water density and dynamics in the chaperonin GroEL cavity
    • 53 Franck, J.M., Sokolovski, M., et al., Horovitz, A., Probing water density and dynamics in the chaperonin GroEL cavity. J. Am. Chem. Soc. 136 (2014), 9396–9403.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 9396-9403
    • Franck, J.M.1    Sokolovski, M.2    Horovitz, A.3
  • 54
    • 84942342339 scopus 로고    scopus 로고
    • Anomalously rapid hydration water diffusion dynamics near DNA surfaces
    • 54 Franck, J.M., Ding, Y., et al., Han, S., Anomalously rapid hydration water diffusion dynamics near DNA surfaces. J. Am. Chem. Soc. 137 (2015), 12013–12023.
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 12013-12023
    • Franck, J.M.1    Ding, Y.2    Han, S.3
  • 55
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: a program for the analysis of the pore dimensions of ion channel structural models
    • 376
    • 55 Smart, O.S., Neduvelil, J.G., et al., Sansom, M.S., HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14 (1996), 354–360 376.
    • (1996) J. Mol. Graph. , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Sansom, M.S.3
  • 57
    • 84903954822 scopus 로고    scopus 로고
    • A hydrophobic barrier deep within the inner pore of the TWIK-1 K2P potassium channel
    • 57 Aryal, P., Abd-Wahab, F., et al., Tucker, S.J., A hydrophobic barrier deep within the inner pore of the TWIK-1 K2P potassium channel. Nat. Commun., 5, 2014, 4377.
    • (2014) Nat. Commun. , vol.5 , pp. 4377
    • Aryal, P.1    Abd-Wahab, F.2    Tucker, S.J.3
  • 58
    • 2142715470 scopus 로고    scopus 로고
    • Water dynamics and dewetting transitions in the small mechanosensitive channel MscS
    • 58 Anishkin, A., Sukharev, S., Water dynamics and dewetting transitions in the small mechanosensitive channel MscS. Biophys. J. 86 (2004), 2883–2895.
    • (2004) Biophys. J. , vol.86 , pp. 2883-2895
    • Anishkin, A.1    Sukharev, S.2
  • 59
    • 84929001600 scopus 로고    scopus 로고
    • Buried ionizable networks are an ancient hallmark of G protein-coupled receptor activation
    • 59 Isom, D.G., Dohlman, H.G., Buried ionizable networks are an ancient hallmark of G protein-coupled receptor activation. Proc. Natl. Acad. Sci. USA 112 (2015), 5702–5707.
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 5702-5707
    • Isom, D.G.1    Dohlman, H.G.2
  • 60
    • 84919650170 scopus 로고    scopus 로고
    • Hydrophobic gating in ion channels
    • 60 Aryal, P., Sansom, M.S., Tucker, S.J., Hydrophobic gating in ion channels. J. Mol. Biol. 427 (2015), 121–130.
    • (2015) J. Mol. Biol. , vol.427 , pp. 121-130
    • Aryal, P.1    Sansom, M.S.2    Tucker, S.J.3
  • 61
    • 83455222535 scopus 로고    scopus 로고
    • Electric-field-induced wetting and dewetting in single hydrophobic nanopores
    • 61 Powell, M.R., Cleary, L., et al., Siwy, Z.S., Electric-field-induced wetting and dewetting in single hydrophobic nanopores. Nat. Nanotechnol. 6 (2011), 798–802.
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 798-802
    • Powell, M.R.1    Cleary, L.2    Siwy, Z.S.3
  • 62
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • 62 Kobilka, B.K., Deupi, X., Conformational complexity of G-protein-coupled receptors. Trends Pharmacol. Sci. 28 (2007), 397–406.
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 63
  • 64
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • 64 Motlagh, H.N., Wrabl, J.O., et al., Hilser, V.J., The ensemble nature of allostery. Nature 508 (2014), 331–339.
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Hilser, V.J.3
  • 65
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • 65 Lockless, S.W., Ranganathan, R., Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286 (1999), 295–299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 66
    • 68749107059 scopus 로고    scopus 로고
    • Protein sectors: evolutionary units of three-dimensional structure
    • 66 Halabi, N., Rivoire, O., et al., Ranganathan, R., Protein sectors: evolutionary units of three-dimensional structure. Cell 138 (2009), 774–786.
    • (2009) Cell , vol.138 , pp. 774-786
    • Halabi, N.1    Rivoire, O.2    Ranganathan, R.3
  • 67
    • 17044427535 scopus 로고    scopus 로고
    • Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved
    • 67 Zheng, W., Brooks, B.R., et al., Thirumalai, D., Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved. Structure 13 (2005), 565–577.
    • (2005) Structure , vol.13 , pp. 565-577
    • Zheng, W.1    Brooks, B.R.2    Thirumalai, D.3
  • 68
    • 84898439664 scopus 로고    scopus 로고
    • Determination of signaling pathways in proteins through network theory: importance of the topology
    • 68 Ribeiro, A.A., Ortiz, V., Determination of signaling pathways in proteins through network theory: importance of the topology. J. Chem. Theory Comput. 10 (2014), 1762–1769.
    • (2014) J. Chem. Theory Comput. , vol.10 , pp. 1762-1769
    • Ribeiro, A.A.1    Ortiz, V.2
  • 69
    • 84896484176 scopus 로고    scopus 로고
    • Computational approaches to mapping allosteric pathways
    • 69 Feher, V.A., Durrant, J.D., et al., Amaro, R.E., Computational approaches to mapping allosteric pathways. Curr. Opin. Struct. Biol. 25 (2014), 98–103.
    • (2014) Curr. Opin. Struct. Biol. , vol.25 , pp. 98-103
    • Feher, V.A.1    Durrant, J.D.2    Amaro, R.E.3
  • 70
    • 84928311409 scopus 로고    scopus 로고
    • Protein contact network topology: a natural language for allostery
    • 70 Di Paola, L., Giuliani, A., Protein contact network topology: a natural language for allostery. Curr. Opin. Struct. Biol. 31 (2015), 43–48.
    • (2015) Curr. Opin. Struct. Biol. , vol.31 , pp. 43-48
    • Di Paola, L.1    Giuliani, A.2
  • 71
    • 84969545678 scopus 로고    scopus 로고
    • Water-mediated energy dynamics in a homodimeric hemoglobin
    • 71 Leitner, D.M., Water-mediated energy dynamics in a homodimeric hemoglobin. J. Phys. Chem. B 120 (2016), 4019–4027.
    • (2016) J. Phys. Chem. B , vol.120 , pp. 4019-4027
    • Leitner, D.M.1
  • 72
    • 84882246260 scopus 로고    scopus 로고
    • Urea-induced denaturation of preQ1-riboswitch
    • 72 Yoon, J., Thirumalai, D., Hyeon, C., Urea-induced denaturation of preQ1-riboswitch. J. Am. Chem. Soc. 135 (2013), 12112–12121.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12112-12121
    • Yoon, J.1    Thirumalai, D.2    Hyeon, C.3
  • 73
    • 0034730143 scopus 로고    scopus 로고
    • Solvent dependence of dynamic transitions in protein solutions
    • 73 Réat, V., Dunn, R., et al., Smith, J.C., Solvent dependence of dynamic transitions in protein solutions. Proc. Natl. Acad. Sci. USA 97 (2000), 9961–9966.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9961-9966
    • Réat, V.1    Dunn, R.2    Smith, J.C.3
  • 74
    • 0029836757 scopus 로고    scopus 로고
    • Internal molecular motions of bacteriorhodopsin: hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes
    • 74 Fitter, J., Lechner, R.E., et al., Dencher, N.A., Internal molecular motions of bacteriorhodopsin: hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes. Proc. Natl. Acad. Sci. USA 93 (1996), 7600–7605.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7600-7605
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.