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Volumn 61, Issue 3-4, 2015, Pages 209-226

13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1

Author keywords

Chemical modification; Conformational change; Lysine; Methionine; Nuclear magnetic resonance; Reductive methylation

Indexed keywords

ANTIPORTER; BICARBONATE CHLORIDE ANTIPORTER; CARBON; CLC-EC1 PROTEIN, E COLI; CYSTEINE; ESCHERICHIA COLI PROTEIN; LYSINE; METHIONINE;

EID: 84939963405     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-015-9898-7     Document Type: Article
Times cited : (19)

References (118)
  • 1
    • 54049135943 scopus 로고    scopus 로고
    • Detection of protein-ligand interactions by NMR using reductive methylation of lysine residues
    • Abraham SJ, Hoheisel S, Gaponenko V (2008) Detection of protein-ligand interactions by NMR using reductive methylation of lysine residues. J Biomol NMR 42:143-148. doi: 10.1007/s10858-008-9274-y
    • (2008) J Biomol NMR , vol.42 , pp. 143-148
    • Abraham, S.J.1    Hoheisel, S.2    Gaponenko, V.3
  • 4
    • 77953808359 scopus 로고    scopus 로고
    • CLC channels and transporters: Proteins with borderline personalities
    • Accardi A, Picollo A (2010) CLC channels and transporters: proteins with borderline personalities. Biochim Biophys Acta 1798:1457-1464. doi: 10.1016/j.bbamem.2010.02.022
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1457-1464
    • Accardi, A.1    Picollo, A.2
  • 7
    • 33748798473 scopus 로고    scopus 로고
    • Synergism between halide binding and proton transport in a CLC-type exchanger
    • Accardi A, Lobet S, Williams C, Miller C, Dutzler R (2006) Synergism between halide binding and proton transport in a CLC-type exchanger. J Mol Biol 362:691-699
    • (2006) J Mol Biol , vol.362 , pp. 691-699
    • Accardi, A.1    Lobet, S.2    Williams, C.3    Miller, C.4    Dutzler, R.5
  • 8
    • 84902107617 scopus 로고    scopus 로고
    • Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter
    • Basilio D, Noack K, Picollo A, Accardi A (2014) Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter. Nat Struct Mol Biol 21:456-463. doi: 10.1038/nsmb.2814
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 456-463
    • Basilio, D.1    Noack, K.2    Picollo, A.3    Accardi, A.4
  • 9
    • 0029665692 scopus 로고    scopus 로고
    • Interlobe communication in 13C-methionine-labeled human transferrin
    • Beatty EJ et al (1996) Interlobe communication in 13C-methionine-labeled human transferrin. Biochemistry 35:7635-7642. doi: 10.1021/bi960684g
    • (1996) Biochemistry , vol.35 , pp. 7635-7642
    • Beatty, E.J.1
  • 10
    • 33744950592 scopus 로고    scopus 로고
    • Site-directed fluorescence studies of a prokaryotic ClC antiporter
    • Bell SP, Curran PK, Choi S, Mindell JA (2006) Site-directed fluorescence studies of a prokaryotic ClC antiporter. Biochemistry 45:6773-6782
    • (2006) Biochemistry , vol.45 , pp. 6773-6782
    • Bell, S.P.1    Curran, P.K.2    Choi, S.3    Mindell, J.A.4
  • 11
    • 73849149844 scopus 로고    scopus 로고
    • Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor
    • Bokoch MP et al (2010) Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. Nature 463:108-112. doi: 10.1038/nature08650
    • (2010) Nature , vol.463 , pp. 108-112
    • Bokoch, M.P.1
  • 12
    • 0032483515 scopus 로고    scopus 로고
    • Changes in steady-state conformational equilibrium resulting from cytoplasmic mutations of the Na, K-ATPase alpha-subunit
    • Boxenbaum N, Daly SE, Javaid ZZ, Lane LK, Blostein R (1998) Changes in steady-state conformational equilibrium resulting from cytoplasmic mutations of the Na, K-ATPase alpha-subunit. J Biol Chem 273:23086-23092
    • (1998) J Biol Chem , vol.273 , pp. 23086-23092
    • Boxenbaum, N.1    Daly, S.E.2    Javaid, Z.Z.3    Lane, L.K.4    Blostein, R.5
  • 13
    • 0036792118 scopus 로고    scopus 로고
    • Evolution of amino acid frequencies in proteins over deep time: Inferred order of introduction of amino acids into the genetic code
    • Brooks DJ, Fresco JR, Lesk AM, Singh M (2002) Evolution of amino acid frequencies in proteins over deep time: inferred order of introduction of amino acids into the genetic code. Mol Biol Evol 19:1645-1655
    • (2002) Mol Biol Evol , vol.19 , pp. 1645-1655
    • Brooks, D.J.1    Fresco, J.R.2    Lesk, A.M.3    Singh, M.4
  • 14
    • 77956490320 scopus 로고    scopus 로고
    • Conformational dependence of 13C shielding and coupling constants for methionine methyl groups
    • Butterfoss GL et al (2010) Conformational dependence of 13C shielding and coupling constants for methionine methyl groups. J Biomol NMR 48:31-47. doi: 10.1007/s10858-010-9436-6
    • (2010) J Biomol NMR , vol.48 , pp. 31-47
    • Butterfoss, G.L.1
  • 15
    • 84879628975 scopus 로고    scopus 로고
    • Application of reductive (1)(3)C-methylation of lysines to enhance the sensitivity of conventional NMR methods
    • Chavan TS, Abraham S, Gaponenko V (2013) Application of reductive (1)(3)C-methylation of lysines to enhance the sensitivity of conventional NMR methods. Molecules 18:7103-7119. doi: 10.3390/molecules18067103
    • (2013) Molecules , vol.18 , pp. 7103-7119
    • Chavan, T.S.1    Abraham, S.2    Gaponenko, V.3
  • 16
    • 84881106990 scopus 로고    scopus 로고
    • Molecular mechanism of the Escherichia coli maltose transporter
    • Chen J (2013) Molecular mechanism of the Escherichia coli maltose transporter. Curr Opin Struct Biol 23:492-498. doi: 10.1016/j.sbi.2013.03.011
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 492-498
    • Chen, J.1
  • 17
    • 42049096734 scopus 로고    scopus 로고
    • CLC-0 and CFTR: Chloride channels evolved from transporters
    • Chen TY, Hwang TC (2008) CLC-0 and CFTR: chloride channels evolved from transporters. Physiol Rev 88:351-387. doi: 10.1152/physrev.00058.2006
    • (2008) Physiol Rev , vol.88 , pp. 351-387
    • Chen, T.Y.1    Hwang, T.C.2
  • 18
    • 84884873854 scopus 로고    scopus 로고
    • 19F NMR: A valuable tool for studying biological events
    • Chen H, Viel S, Ziarelli F, Peng L (2013) 19F NMR: a valuable tool for studying biological events. Chem Soc Rev 42:7971-7982. doi: 10.1039/c3cs60129c
    • (2013) Chem Soc Rev , vol.42 , pp. 7971-7982
    • Chen, H.1    Viel, S.2    Ziarelli, F.3    Peng, L.4
  • 19
    • 84858758947 scopus 로고    scopus 로고
    • - and water transport through a eukaryotic CLC transporter
    • - and water transport through a eukaryotic CLC transporter. Biophys J 102:1363-1371. doi: 10.1016/j.bpj.2012.01.056
    • (2012) Biophys J , vol.102 , pp. 1363-1371
    • Cheng, M.H.1    Coalson, R.D.2
  • 21
    • 0029665619 scopus 로고    scopus 로고
    • Use of 19F NMR to probe protein structure and conformational changes
    • Danielson MA, Falke JJ (1996) Use of 19F NMR to probe protein structure and conformational changes. Annu Rev Biophys Biomol Struct 25:163-195
    • (1996) Annu Rev Biophys Biomol Struct , vol.25 , pp. 163-195
    • Danielson, M.A.1    Falke, J.J.2
  • 22
    • 34548844740 scopus 로고    scopus 로고
    • NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solution
    • DellaVecchia MJ et al (2007) NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solution. J Mol Biol 373:282-295. doi: 10.1016/j.jmb.2007.07.045
    • (2007) J Mol Biol , vol.373 , pp. 282-295
    • Dellavecchia, M.J.1
  • 24
    • 33746641711 scopus 로고    scopus 로고
    • The ClC family of chloride channels and transporters
    • Dutzler R (2006) The ClC family of chloride channels and transporters. Curr Opin Struct Biol 16:439-446
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 439-446
    • Dutzler, R.1
  • 25
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 reveals the molecular basis of anion selectivity
    • Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R (2002) X-ray structure of a ClC chloride channel at 3.0 reveals the molecular basis of anion selectivity. Nature 415:287-294
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 26
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler R, Campbell EB, MacKinnon R (2003) Gating the selectivity filter in ClC chloride channels. Science 300:108-112
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 27
    • 70350304561 scopus 로고    scopus 로고
    • Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR
    • Elvington SM, Liu CW, Maduke MC (2009) Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR. EMBO J 28:3090-3102
    • (2009) EMBO J , vol.28 , pp. 3090-3102
    • Elvington, S.M.1    Liu, C.W.2    Maduke, M.C.3
  • 28
    • 22244489419 scopus 로고    scopus 로고
    • Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule
    • Engh AM, Maduke M (2005) Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule. J Gen Physiol 125:601-617
    • (2005) J Gen Physiol , vol.125 , pp. 601-617
    • Engh, A.M.1    Maduke, M.2
  • 29
    • 34748824381 scopus 로고    scopus 로고
    • The role of a conserved lysine in chloride- and voltage-dependent ClC-0 fast gating
    • Engh AM, Faraldo-Gomez JD, Maduke M (2007) The role of a conserved lysine in chloride- and voltage-dependent ClC-0 fast gating. J Gen Physiol 130:351-363
    • (2007) J Gen Physiol , vol.130 , pp. 351-363
    • Engh, A.M.1    Faraldo-Gomez, J.D.2    Maduke, M.3
  • 30
    • 2542437774 scopus 로고    scopus 로고
    • Electrostatics of ion stabilization in a ClC chloride channel homologue from Escherichia coli
    • Faraldo-Gomez JD, Roux B (2004) Electrostatics of ion stabilization in a ClC chloride channel homologue from Escherichia coli. J Mol Biol 339:981-1000. doi: 10.1016/j.jmb.2004.04.023
    • (2004) J Mol Biol , vol.339 , pp. 981-1000
    • Faraldo-Gomez, J.D.1    Roux, B.2
  • 31
    • 78049362741 scopus 로고    scopus 로고
    • Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle
    • Feng L, Campbell EB, Hsiung Y, MacKinnon R (2010) Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330:635-641. doi: 10.1126/science.1195230
    • (2010) Science , vol.330 , pp. 635-641
    • Feng, L.1    Campbell, E.B.2    Hsiung, Y.3    MacKinnon, R.4
  • 32
    • 84877262325 scopus 로고    scopus 로고
    • Neurotransmitter transporters: Structure meets function
    • Focke PJ, Wang X, Larsson HP (2013) Neurotransmitter transporters: structure meets function. Structure 21:694-705. doi: 10.1016/j.str.2013.03.002
    • (2013) Structure , vol.21 , pp. 694-705
    • Focke, P.J.1    Wang, X.2    Larsson, H.P.3
  • 33
    • 73949083478 scopus 로고    scopus 로고
    • The rocking bundle: A mechanism for ion-coupled solute flux by symmetrical transporters
    • Forrest LR, Rudnick G (2009) The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters. Physiology 24:377-386. doi: 10.1152/physiol.00030.2009
    • (2009) Physiology , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 34
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • Forrest LR, Kramer R, Ziegler C (2011) The structural basis of secondary active transport mechanisms. Biochim Biophys Acta 1807:167-188. doi: 10.1016/j.bbabio.2010.10.014
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Kramer, R.2    Ziegler, C.3
  • 35
    • 0020490394 scopus 로고
    • Intramolecular interactions of amino groups in 13C reductively methylated hen egg-white lysozyme
    • Gerken TA, Jentoft JE, Jentoft N, Dearborn DG (1982) Intramolecular interactions of amino groups in 13C reductively methylated hen egg-white lysozyme. J Biol Chem 257:2894-2900
    • (1982) J Biol Chem , vol.257 , pp. 2894-2900
    • Gerken, T.A.1    Jentoft, J.E.2    Jentoft, N.3    Dearborn, D.G.4
  • 36
    • 0025254028 scopus 로고
    • 13C-NMR of Clostridium pasteurianum ferredoxin after reductive methylation of the amines using [13C]formaldehyde
    • Gluck M, Sweeney WV (1990) 13C-NMR of Clostridium pasteurianum ferredoxin after reductive methylation of the amines using [13C]formaldehyde. Biochim Biophys Acta 1038:146-151
    • (1990) Biochim Biophys Acta , vol.1038 , pp. 146-151
    • Gluck, M.1    Sweeney, W.V.2
  • 37
  • 38
    • 34848888055 scopus 로고    scopus 로고
    • Structural determination of wild-type lactose permease
    • Guan L, Mirza O, Verner G, Iwata S, Kaback HR (2007) Structural determination of wild-type lactose permease. Proc Natl Acad Sci USA 104:15294-15298. doi: 10.1073/pnas.0707688104
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15294-15298
    • Guan, L.1    Mirza, O.2    Verner, G.3    Iwata, S.4    Kaback, H.R.5
  • 40
    • 84873057637 scopus 로고    scopus 로고
    • Utilization of lysine (1)(3)C-methylation NMR for protein-protein interaction studies
    • Hattori Y et al (2013) Utilization of lysine (1)(3)C-methylation NMR for protein-protein interaction studies. J Biomol NMR 55:19-31. doi: 10.1007/s10858-012-9675-9
    • (2013) J Biomol NMR , vol.55 , pp. 19-31
    • Hattori, Y.1
  • 41
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman K, Kern D (2007) Dynamic personalities of proteins. Nature 450:964-972
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 42
    • 0024286086 scopus 로고
    • 13C NMR studies of methylene and methine carbons of substrate bound to a 280,000-dalton protein, porphobilinogen synthase
    • Jaffe EK, Markham GD (1988) 13C NMR studies of methylene and methine carbons of substrate bound to a 280,000-dalton protein, porphobilinogen synthase. Biochemistry 27:4475-4481
    • (1988) Biochemistry , vol.27 , pp. 4475-4481
    • Jaffe, E.K.1    Markham, G.D.2
  • 43
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O (1966) Simple allosteric model for membrane pumps. Nature 211:969-970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 46
    • 20444419395 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease
    • Kaback HR (2005) Structure and mechanism of the lactose permease. C R Biol 328:557-567. doi: 10.1016/j.crvi.2005.03.008
    • (2005) C R Biol , vol.328 , pp. 557-567
    • Kaback, H.R.1
  • 47
    • 84901758511 scopus 로고    scopus 로고
    • TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor
    • Kalverda AP, Gowdy J, Thompson GS, Homans SW, Henderson PJ, Patching SG (2014) TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor. Mol Membr Biol 31:131-140. doi: 10.3109/09687688.2014.911980
    • (2014) Mol Membr Biol , vol.31 , pp. 131-140
    • Kalverda, A.P.1    Gowdy, J.2    Thompson, G.S.3    Homans, S.W.4    Henderson, P.J.5    Patching, S.G.6
  • 48
    • 79960977911 scopus 로고    scopus 로고
    • Solution NMR study of integral membrane proteins
    • Kang C, Li Q (2011) Solution NMR study of integral membrane proteins. Curr Opin Chem Biol 15:560-569. doi: 10.1016/j.cbpa.2011.05.025
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 560-569
    • Kang, C.1    Li, Q.2
  • 50
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D, Oldham ML, Orelle C, Davidson AL, Chen J (2009) Alternating access in maltose transporter mediated by rigid-body rotations. Mol Cell 33:528-536. doi: 10.1016/j.molcel.2009.01.035
    • (2009) Mol Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 51
    • 70349745154 scopus 로고    scopus 로고
    • Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteins
    • Kim HJ, Howell SC, Van Horn WD, Jeon YH, Sanders CR (2009) Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteins. Prog Nucl Magn Reson Spectrosc 55:335-360. doi: 10.1016/j.pnmrs.2009.07.002
    • (2009) Prog Nucl Magn Reson Spectrosc , vol.55 , pp. 335-360
    • Kim, H.J.1    Howell, S.C.2    Van Horn, W.D.3    Jeon, Y.H.4    Sanders, C.R.5
  • 52
    • 84857625337 scopus 로고    scopus 로고
    • Current applications of 19F NMR to studies of protein structure and dynamics
    • Kitevski-LeBlanc JL, Prosser RS (2012) Current applications of 19F NMR to studies of protein structure and dynamics. Prog Nucl Magn Reson Spectrosc 62:1-33. doi: 10.1016/j.pnmrs.2011.06.003
    • (2012) Prog Nucl Magn Reson Spectrosc , vol.62 , pp. 1-33
    • Kitevski-Leblanc, J.L.1    Prosser, R.S.2
  • 53
    • 77952766712 scopus 로고    scopus 로고
    • Secondary water pore formation for proton transport in a ClC exchanger revealed by an atomistic molecular-dynamics simulation
    • Ko YJ, Jo WH (2010) Secondary water pore formation for proton transport in a ClC exchanger revealed by an atomistic molecular-dynamics simulation. Biophys J 98:2163-2169. doi: 10.1016/j.bpj.2010.01.043
    • (2010) Biophys J , vol.98 , pp. 2163-2169
    • Ko, Y.J.1    Jo, W.H.2
  • 54
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • Krishnamurthy H, Gouaux E (2012) X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481:469-474. doi: 10.1038/nature10737
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 55
    • 84865396279 scopus 로고    scopus 로고
    • Partial least-squares functional mode analysis: Application to the membrane proteins AQP1, Aqy1, and CLC-ec1
    • Krivobokova T, Briones R, Hub JS, Munk A, de Groot BL (2012) Partial least-squares functional mode analysis: application to the membrane proteins AQP1, Aqy1, and CLC-ec1. Biophys J 103:786-796. doi: 10.1016/j.bpj.2012.07.022
    • (2012) Biophys J , vol.103 , pp. 786-796
    • Krivobokova, T.1    Briones, R.2    Hub, J.S.3    Munk, A.4    De Groot, B.L.5
  • 56
    • 34249897242 scopus 로고    scopus 로고
    • - stoichiometry in bacterial chloride transporters
    • - stoichiometry in bacterial chloride transporters. Proteins 68:26-33. doi: 10.1002/prot.21441
    • (2007) Proteins , vol.68 , pp. 26-33
    • Kuang, Z.1    Mahankali, U.2    Beck, T.L.3
  • 58
    • 0034726672 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of pokeweed antiviral protein-II after reductive methylation of lysine residues
    • Kurinov IV, Mao C, Irvin JD, Uckun FM (2000) X-ray crystallographic analysis of pokeweed antiviral protein-II after reductive methylation of lysine residues. Biochem Biophys Res Commun 275:549-552. doi: 10.1006/bbrc.2000.3329
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 549-552
    • Kurinov, I.V.1    Mao, C.2    Irvin, J.D.3    Uckun, F.M.4
  • 59
    • 84868204024 scopus 로고    scopus 로고
    • Lysine methylation strategies for characterizing protein conformations by NMR
    • Larda ST, Bokoch MP, Evanics F, Prosser RS (2012) Lysine methylation strategies for characterizing protein conformations by NMR. J Biomol NMR 54:199-209. doi: 10.1007/s10858-012-9664-z
    • (2012) J Biomol NMR , vol.54 , pp. 199-209
    • Larda, S.T.1    Bokoch, M.P.2    Evanics, F.3    Prosser, R.S.4
  • 60
    • 53849119555 scopus 로고    scopus 로고
    • Ins and outs of major facilitator superfamily antiporters
    • Law CJ, Maloney PC, Wang DN (2008) Ins and outs of major facilitator superfamily antiporters. Annu Rev Microbiol 62:289-305. doi: 10.1146/annurev.micro.61.080706.093329
    • (2008) Annu Rev Microbiol , vol.62 , pp. 289-305
    • Law, C.J.1    Maloney, P.C.2    Wang, D.N.3
  • 66
    • 61449446545 scopus 로고    scopus 로고
    • Review. Proton-coupled gating in chloride channels
    • Lisal J, Maduke M (2009) Review. Proton-coupled gating in chloride channels. Philos Trans R Soc Lond B Biol Sci 364:181-187. doi: 10.1098/rstb.2008.0123
    • (2009) Philos Trans R Soc Lond B Biol Sci , vol.364 , pp. 181-187
    • Lisal, J.1    Maduke, M.2
  • 67
    • 0042206685 scopus 로고    scopus 로고
    • Substrate-induced conformational fit and headpiece closure in the Ca2 + ATPase (SERCA)
    • Ma H, Inesi G, Toyoshima C (2003) Substrate-induced conformational fit and headpiece closure in the Ca2 + ATPase (SERCA). J Biol Chem 278:28938-28943. doi: 10.1074/jbc.M304120200
    • (2003) J Biol Chem , vol.278 , pp. 28938-28943
    • Ma, H.1    Inesi, G.2    Toyoshima, C.3
  • 68
    • 0032692857 scopus 로고    scopus 로고
    • High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel
    • Maduke M, Pheasant DJ, Miller C (1999) High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel. J Gen Physiol 114:713-722
    • (1999) J Gen Physiol , vol.114 , pp. 713-722
    • Maduke, M.1    Pheasant, D.J.2    Miller, C.3
  • 69
    • 0033873930 scopus 로고    scopus 로고
    • A decade of CLC chloride channels: Structure, mechanism, and many unsettled questions
    • Maduke M, Miller C, Mindell JA (2000) A decade of CLC chloride channels: structure, mechanism, and many unsettled questions. Annu Rev Biophys Biomol Struct 29:411-438
    • (2000) Annu Rev Biophys Biomol Struct , vol.29 , pp. 411-438
    • Maduke, M.1    Miller, C.2    Mindell, J.A.3
  • 70
    • 84883171052 scopus 로고    scopus 로고
    • +antiporter NhaA from Escherichia coli
    • +antiporter NhaA from Escherichia coli. J Biol Chem 288:24666-24675. doi: 10.1074/jbc.M113.484071
    • (2013) J Biol Chem , vol.288 , pp. 24666-24675
    • Mager, T.1
  • 71
    • 84882400833 scopus 로고    scopus 로고
    • NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond
    • Mainz A, Religa TL, Sprangers R, Linser R, Kay LE, Reif B (2013) NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond. Angew Chem Int Ed Engl 52:8746-8751. doi: 10.1002/anie.201301215
    • (2013) Angew Chem Int Ed Engl , vol.52 , pp. 8746-8751
    • Mainz, A.1    Religa, T.L.2    Sprangers, R.3    Linser, R.4    Kay, L.E.5    Reif, B.6
  • 72
    • 0034093293 scopus 로고    scopus 로고
    • Substrate-induced exposure of an energy-coupling motif of a membrane transporter
    • Merianos HJ, Cadieux N, Lin CH, Kadner RJ, Cafiso DS (2000) Substrate-induced exposure of an energy-coupling motif of a membrane transporter. Nat Struct Biol 7:205-209. doi: 10.1038/73309
    • (2000) Nat Struct Biol , vol.7 , pp. 205-209
    • Merianos, H.J.1    Cadieux, N.2    Lin, C.H.3    Kadner, R.J.4    Cafiso, D.S.5
  • 73
    • 33645296826 scopus 로고    scopus 로고
    • ClC chloride channels viewed through a transporter lens
    • Miller C (2006) ClC chloride channels viewed through a transporter lens. Nature 440:484-489
    • (2006) Nature , vol.440 , pp. 484-489
    • Miller, C.1
  • 74
    • 84941600274 scopus 로고    scopus 로고
    • - channel"
    • - channel". J Physiol. doi: 10.1113/jphysiol.2014.286260
    • (2014) J Physiol
    • Miller, C.1
  • 76
    • 77949623101 scopus 로고    scopus 로고
    • Antiport mechanism for Cl(-)/H(+) in ClC-ec1 from normal-mode analysis
    • Miloshevsky GV, Hassanein A, Jordan PC (2010) Antiport mechanism for Cl(-)/H(+) in ClC-ec1 from normal-mode analysis. Biophys J 98:999-1008. doi: 10.1016/j.bpj.2009.11.035
    • (2010) Biophys J , vol.98 , pp. 999-1008
    • Miloshevsky, G.V.1    Hassanein, A.2    Jordan, P.C.3
  • 77
    • 84857260144 scopus 로고    scopus 로고
    • Lysosomal acidification mechanisms
    • Mindell JA (2012) Lysosomal acidification mechanisms. Annu Rev Physiol 74:69-86. doi: 10.1146/annurev-physiol-012110-142317
    • (2012) Annu Rev Physiol , vol.74 , pp. 69-86
    • Mindell, J.A.1
  • 78
    • 84886061681 scopus 로고    scopus 로고
    • Investigation of lysine side chain interactions of interleukin-8 with heparin and other glycosaminoglycans studied by a methylation-NMR approach
    • Mobius K et al (2013) Investigation of lysine side chain interactions of interleukin-8 with heparin and other glycosaminoglycans studied by a methylation-NMR approach. Glycobiology 23:1260-1269. doi: 10.1093/glycob/cwt062
    • (2013) Glycobiology , vol.23 , pp. 1260-1269
    • Mobius, K.1
  • 79
    • 78049501839 scopus 로고    scopus 로고
    • Determination of membrane protein structures using solution and solid-state NMR
    • J.J. Lacapere (eds) 654 Springer New York
    • Montaville P, Jamin N (2010) Determination of membrane protein structures using solution and solid-state NMR. In: Lacapere JJ (ed) Membrane protein structure determination: methods and protocols, vol 654. Springer, New York, pp 261-282
    • (2010) Membrane Protein Structure Determination: Methods and Protocols , pp. 261-282
    • Montaville, P.1    Jamin, N.2
  • 80
    • 38049132433 scopus 로고    scopus 로고
    • + transporters constrained by covalent cross-linking
    • + transporters constrained by covalent cross-linking. Proc Natl Acad Sci USA 104:20659-20665
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20659-20665
    • Nguitragool, W.1    Miller, C.2
  • 81
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450:515-521. doi: 10.1038/nature06264
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 82
    • 0242267427 scopus 로고    scopus 로고
    • Methyl TROSY: Explanation and experimental verification
    • Ollerenshaw JE, Tugarinov V, Kay LE (2003) Methyl TROSY: explanation and experimental verification. Magn Reson Chem 41:843-852
    • (2003) Magn Reson Chem , vol.41 , pp. 843-852
    • Ollerenshaw, J.E.1    Tugarinov, V.2    Kay, L.E.3
  • 83
    • 58149302956 scopus 로고    scopus 로고
    • Insights into the ClC-4 transport mechanism from studies of Zn2 + inhibition
    • Osteen JD, Mindell JA (2008) Insights into the ClC-4 transport mechanism from studies of Zn2 + inhibition. Biophys J 95:4668-4675
    • (2008) Biophys J , vol.95 , pp. 4668-4675
    • Osteen, J.D.1    Mindell, J.A.2
  • 84
    • 0037270065 scopus 로고    scopus 로고
    • Improved methods of cultivation and production of deuteriated proteins from E. Coli strains grown on fully deuteriated minimal medium
    • Paliy O, Bloor D, Brockwell D, Gilbert P, Barber J (2003) Improved methods of cultivation and production of deuteriated proteins from E. coli strains grown on fully deuteriated minimal medium. J Appl Microbiol 94:580-586
    • (2003) J Appl Microbiol , vol.94 , pp. 580-586
    • Paliy, O.1    Bloor, D.2    Brockwell, D.3    Gilbert, P.4    Barber, J.5
  • 85
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo A, Pusch M (2005) Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436:420-423
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 86
    • 84860739823 scopus 로고    scopus 로고
    • Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H(+)/Cl(-) exchanger
    • Picollo A, Xu Y, Johner N, Berneche S, Accardi A (2012) Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H(+)/Cl(-) exchanger. Nat Struct Mol Biol 19(525-531):S521. doi: 10.1038/nsmb.2277
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.525-531 , pp. 521
    • Picollo, A.1    Xu, Y.2    Johner, N.3    Berneche, S.4    Accardi, A.5
  • 87
    • 0031053054 scopus 로고    scopus 로고
    • Reductive alkylation of lysine residues to alter crystallization properties of proteins
    • Rayment I (1997) Reductive alkylation of lysine residues to alter crystallization properties of proteins. Methods Enzymol 276:171-179
    • (1997) Methods Enzymol , vol.276 , pp. 171-179
    • Rayment, I.1
  • 88
    • 77954717665 scopus 로고    scopus 로고
    • Optimal methyl labeling for studies of supra-molecular systems
    • Religa TL, Kay LE (2010) Optimal methyl labeling for studies of supra-molecular systems. J Biomol NMR 47:163-169. doi: 10.1007/s10858-010-9419-7
    • (2010) J Biomol NMR , vol.47 , pp. 163-169
    • Religa, T.L.1    Kay, L.E.2
  • 89
    • 77950497745 scopus 로고    scopus 로고
    • Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR
    • Religa TL, Sprangers R, Kay LE (2010) Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR. Science 328:98-102. doi: 10.1126/science.1184991
    • (2010) Science , vol.328 , pp. 98-102
    • Religa, T.L.1    Sprangers, R.2    Kay, L.E.3
  • 90
    • 79958789586 scopus 로고    scopus 로고
    • Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: Applications to the proteasome and to the ClpP protease
    • Religa TL, Ruschak AM, Rosenzweig R, Kay LE (2011) Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: applications to the proteasome and to the ClpP protease. J Am Chem Soc 133:9063-9068. doi: 10.1021/ja202259a
    • (2011) J Am Chem Soc , vol.133 , pp. 9063-9068
    • Religa, T.L.1    Ruschak, A.M.2    Rosenzweig, R.3    Kay, L.E.4
  • 91
    • 84908084088 scopus 로고    scopus 로고
    • Review of methods to assign the nuclear magnetic resonance peaks of reductively methylated proteins
    • Roberson KJ, Macnaughtan MA (2014) Review of methods to assign the nuclear magnetic resonance peaks of reductively methylated proteins. Anal Biochem 466C:76-82. doi: 10.1016/j.ab.2014.08.024
    • (2014) Anal Biochem , vol.466 , pp. 76-82
    • Roberson, K.J.1    MacNaughtan, M.A.2
  • 92
    • 78650171241 scopus 로고    scopus 로고
    • Design, function and structure of a monomeric ClC transporter
    • Robertson JL, Kolmakova-Partensky L, Miller C (2010) Design, function and structure of a monomeric ClC transporter. Nature 468:844-847. doi: 10.1038/nature09556
    • (2010) Nature , vol.468 , pp. 844-847
    • Robertson, J.L.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 93
    • 84902209981 scopus 로고    scopus 로고
    • Bringing dynamic molecular machines into focus by methyl-TROSY NMR
    • Rosenzweig R, Kay LE (2014) Bringing dynamic molecular machines into focus by methyl-TROSY NMR. Annu Rev Biochem 83:291-315
    • (2014) Annu Rev Biochem , vol.83 , pp. 291-315
    • Rosenzweig, R.1    Kay, L.E.2
  • 94
    • 0027482860 scopus 로고
    • Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: An X-ray analysis at 1.8-A resolution
    • Rypniewski WR, Holden HM, Rayment I (1993) Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8-A resolution. Biochemistry (Mosc) 32:9851-9858
    • (1993) Biochemistry (Mosc) , vol.32 , pp. 9851-9858
    • Rypniewski, W.R.1    Holden, H.M.2    Rayment, I.3
  • 96
    • 33746217557 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins: Practice and challenges
    • Spec No
    • Sanders CR, Sonnichsen F (2006) Solution NMR of membrane proteins: practice and challenges. Magn Reson Chem: MRC 44 Spec No:S24-S40 doi: 10.1002/mrc.1816
    • (2006) Magn Reson Chem: MRC 44 , pp. S24-S40
    • Sanders, C.R.1    Sonnichsen, F.2
  • 97
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel O, Zdebik AA, Lourdel S, Jentsch TJ (2005) Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436:424-427
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 98
    • 84874249804 scopus 로고    scopus 로고
    • Common folds and transport mechanisms of secondary active transporters
    • Shi Y (2013) Common folds and transport mechanisms of secondary active transporters. Annu Rev Biophys 42:51-72. doi: 10.1146/annurev-biophys-083012-130429
    • (2013) Annu Rev Biophys , vol.42 , pp. 51-72
    • Shi, Y.1
  • 99
    • 84892670970 scopus 로고    scopus 로고
    • Structural and mechanistic insights into prokaryotic energy-coupling factor transporters
    • Slotboom DJ (2014) Structural and mechanistic insights into prokaryotic energy-coupling factor transporters. Nat Rev Microbiol 12:79-87. doi: 10.1038/nrmicro3175
    • (2014) Nat Rev Microbiol , vol.12 , pp. 79-87
    • Slotboom, D.J.1
  • 100
    • 0016638276 scopus 로고
    • Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes
    • Smith DJ, Maggio ET, Kenyon GL (1975) Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes. Biochemistry 14:766-771
    • (1975) Biochemistry , vol.14 , pp. 766-771
    • Smith, D.J.1    Maggio, E.T.2    Kenyon, G.L.3
  • 101
    • 84868129315 scopus 로고    scopus 로고
    • Cell biology and physiology of CLC chloride channels and transporters
    • Stauber T, Weinert S, Jentsch TJ (2012) Cell biology and physiology of CLC chloride channels and transporters. Compr Physiol 2:1701-1744. doi: 10.1002/cphy.c110038
    • (2012) Compr Physiol , vol.2 , pp. 1701-1744
    • Stauber, T.1    Weinert, S.2    Jentsch, T.J.3
  • 102
    • 0020669965 scopus 로고
    • Mechanism of free energy coupling in active transport
    • Tanford C (1983) Mechanism of free energy coupling in active transport. Annu Rev Biochem 52:379-409. doi: 10.1146/annurev.bi.52.070183.002115
    • (1983) Annu Rev Biochem , vol.52 , pp. 379-409
    • Tanford, C.1
  • 103
    • 84862954608 scopus 로고    scopus 로고
    • Physiology and pathophysiology of CLC-1: Mechanisms of a chloride channel disease, myotonia
    • Tang CY, Chen TY (2011) Physiology and pathophysiology of CLC-1: mechanisms of a chloride channel disease, myotonia. J Biomed Biotechnol 2011:685328. doi: 10.1155/2011/685328
    • (2011) J Biomed Biotechnol , vol.2011 , pp. 685328
    • Tang, C.Y.1    Chen, T.Y.2
  • 104
    • 51749087029 scopus 로고    scopus 로고
    • A simple method for amino acid selective isotope labeling of recombinant proteins in E. Coli
    • Tong KI, Yamamoto M, Tanaka T (2008) A simple method for amino acid selective isotope labeling of recombinant proteins in E. coli. J Biomol NMR 42:59-67. doi: 10.1007/s10858-008-9264-0
    • (2008) J Biomol NMR , vol.42 , pp. 59-67
    • Tong, K.I.1    Yamamoto, M.2    Tanaka, T.3
  • 105
    • 0034079112 scopus 로고    scopus 로고
    • Selective constraints, amino acid composition, and the rate of protein evolution
    • Tourasse NJ, Li WH (2000) Selective constraints, amino acid composition, and the rate of protein evolution. Mol Biol Evol 17:656-664
    • (2000) Mol Biol Evol , vol.17 , pp. 656-664
    • Tourasse, N.J.1    Li, W.H.2
  • 106
    • 84870470187 scopus 로고    scopus 로고
    • Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins
    • Verardi R, Traaseth NJ, Masterson LR, Vostrikov VV, Veglia G (2012) Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins. Adv Exp Med Biol 992:35-62. doi: 10.1007/978-94-007-4954-2-3
    • (2012) Adv Exp Med Biol , vol.992 , pp. 35-62
    • Verardi, R.1    Traaseth, N.J.2    Masterson, L.R.3    Vostrikov, V.V.4    Veglia, G.5
  • 107
    • 84901049540 scopus 로고    scopus 로고
    • Coupled ion binding and structural transitions along the transport cycle of glutamate transporters
    • Verdon G, Oh S, Serio RN, Boudker O (2014) Coupled ion binding and structural transitions along the transport cycle of glutamate transporters. Elife 3:e02283. doi: 10.7554/eLife.02283
    • (2014) Elife , vol.3 , pp. 02283
    • Verdon, G.1    Oh, S.2    Serio, R.N.3    Boudker, O.4
  • 109
    • 33846298499 scopus 로고    scopus 로고
    • Lysine methylation as a routine rescue strategy for protein crystallization
    • Walter TS et al (2006) Lysine methylation as a routine rescue strategy for protein crystallization. Structure 14:1617-1622. doi: 10.1016/j.str.2006.09.005
    • (2006) Structure , vol.14 , pp. 1617-1622
    • Walter, T.S.1
  • 110
    • 0027417905 scopus 로고
    • Unnatural amino acid packing mutants of Escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques
    • Wynn R, Richards FM (1993) Unnatural amino acid packing mutants of Escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques. Protein Sci 2:395-403. doi: 10.1002/pro.5560020311
    • (1993) Protein Sci , vol.2 , pp. 395-403
    • Wynn, R.1    Richards, F.M.2
  • 111
    • 84921324831 scopus 로고    scopus 로고
    • A selective NMR probe to monitor the conformational transition from inactive to active kinase
    • Xie Q, Fulton DB, Andreotti AH (2014) A selective NMR probe to monitor the conformational transition from inactive to active kinase. ACS Chem Biol. doi: 10.1021/cb5004702
    • (2014) ACS Chem Biol
    • Xie, Q.1    Fulton, D.B.2    Andreotti, A.H.3
  • 112
    • 84893140063 scopus 로고    scopus 로고
    • TROSY NMR spectroscopy of large soluble proteins
    • Xu Y, Matthews S (2013) TROSY NMR spectroscopy of large soluble proteins. Top Curr Chem 335:97-119. doi: 10.1007/128-2011-228
    • (2013) Top Curr Chem , vol.335 , pp. 97-119
    • Xu, Y.1    Matthews, S.2
  • 113
    • 84874258738 scopus 로고    scopus 로고
    • Structural advances for the major facilitator superfamily (MFS) transporters
    • Yan N (2013) Structural advances for the major facilitator superfamily (MFS) transporters. Trends Biochem Sci 38:151-159. doi: 10.1016/j.tibs.2013.01.003
    • (2013) Trends Biochem Sci , vol.38 , pp. 151-159
    • Yan, N.1
  • 115
    • 81255164758 scopus 로고    scopus 로고
    • The coupled proton transport in the ClC-ec1 Cl(-)/H(+) antiporter
    • Zhang Y, Voth GA (2011) The coupled proton transport in the ClC-ec1 Cl(-)/H(+) antiporter. Biophys J 101:L47-L49. doi: 10.1016/j.bpj.2011.10.021
    • (2011) Biophys J , vol.101 , pp. 47-L49
    • Zhang, Y.1    Voth, G.A.2
  • 116
    • 33645304847 scopus 로고    scopus 로고
    • Roles of K149, G352, and H401 in the channel functions of ClC-0: Testing the predictions from theoretical calculations
    • Zhang XD, Li Y, Yu WP, Chen TY (2006) Roles of K149, G352, and H401 in the channel functions of ClC-0: testing the predictions from theoretical calculations. J Gen Physiol 127:435-447
    • (2006) J Gen Physiol , vol.127 , pp. 435-447
    • Zhang, X.D.1    Li, Y.2    Yu, W.P.3    Chen, T.Y.4
  • 117
    • 79957935490 scopus 로고    scopus 로고
    • Substrate-modulated gating dynamics in a Na+ -coupled neurotransmitter transporter homologue
    • Zhao Y, Terry DS, Shi L, Quick M, Weinstein H, Blanchard SC, Javitch JA (2011) Substrate-modulated gating dynamics in a Na+ -coupled neurotransmitter transporter homologue. Nature 474:109-113. doi: 10.1038/nature09971
    • (2011) Nature , vol.474 , pp. 109-113
    • Zhao, Y.1    Terry, D.S.2    Shi, L.3    Quick, M.4    Weinstein, H.5    Blanchard, S.C.6    Javitch, J.A.7
  • 118
    • 34548852606 scopus 로고    scopus 로고
    • CLC chloride channels and transporters: A biophysical and physiological perspective
    • Zifarelli G, Pusch M (2007) CLC chloride channels and transporters: a biophysical and physiological perspective. Rev Physiol Biochem Pharmacol 158:23-76
    • (2007) Rev Physiol Biochem Pharmacol , vol.158 , pp. 23-76
    • Zifarelli, G.1    Pusch, M.2


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