메뉴 건너뛰기




Volumn 541, Issue 7638, 2017, Pages 500-505

Structure of a CLC chloride ion channel by cryo-electron microscopy

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE CHANNEL; CLC PROTEIN; PROTEIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; CHLORIDE; PROTON;

EID: 85016157531     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature20812     Document Type: Article
Times cited : (116)

References (77)
  • 1
    • 84941570211 scopus 로고    scopus 로고
    • Discovery of CLC transport proteins: Cloning, structure, function and pathophysiology
    • Jentsch, T. J. Discovery of CLC transport proteins: cloning, structure, function and pathophysiology. J. Physiol. 593, 4091-4109 (2015).
    • (2015) J. Physiol. , vol.593 , pp. 4091-4109
    • Jentsch, T.J.1
  • 2
    • 0033873930 scopus 로고    scopus 로고
    • A decade of CLC chloride channels: Structure, mechanism, many unsettled questions
    • Maduke, M., Miller, C., Mindell, J. A. A decade of CLC chloride channels: structure, mechanism, many unsettled questions. Annu. Rev. Biophys. Biomol. Struct. 29, 411-438 (2000).
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 411-438
    • Maduke, M.1    Miller, C.2    Mindell, J.A.3
  • 3
    • 33645296826 scopus 로고    scopus 로고
    • ClC chloride channels viewed through a transporter lens
    • Miller, C. ClC chloride channels viewed through a transporter lens. Nature 440, 484-489 (2006).
    • (2006) Nature , vol.440 , pp. 484-489
    • Miller, C.1
  • 4
    • 0026705098 scopus 로고
    • The skeletal muscle chloride channel in dominant and recessive human myotonia
    • Koch, M. C., et al. The skeletal muscle chloride channel in dominant and recessive human myotonia. Science 257, 797-800 (1992).
    • (1992) Science , vol.257 , pp. 797-800
    • Koch, M.C.1
  • 5
    • 16944366243 scopus 로고    scopus 로고
    • Mutations in the chloride channel gene, CLCNKB, cause Bartter's syndrome type III
    • Simon, D. B., et al. Mutations in the chloride channel gene, CLCNKB, cause Bartter's syndrome type III. Nature Genet. 17, 171-178 (1997).
    • (1997) Nature Genet. , vol.17 , pp. 171-178
    • Simon, D.B.1
  • 6
    • 0028033777 scopus 로고
    • Isolation and partial characterization of a chloride channel gene which is expressed in kidney and is a candidate for Dent's disease (an X-linked hereditary nephrolithiasis)
    • Fisher, S. E., et al. Isolation and partial characterization of a chloride channel gene which is expressed in kidney and is a candidate for Dent's disease (an X-linked hereditary nephrolithiasis). Hum. Mol. Genet. 3, 2053-2059 (1994).
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 2053-2059
    • Fisher, S.E.1
  • 7
    • 0035951282 scopus 로고    scopus 로고
    • Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and man
    • Kornak, U., et al. Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and man. Cell 104, 205-215 (2001).
    • (2001) Cell , vol.104 , pp. 205-215
    • Kornak, U.1
  • 8
    • 0021180163 scopus 로고
    • Dimeric structure of single chloride channels from Torpedo electroplax
    • Miller, C., White, M. M. Dimeric structure of single chloride channels from Torpedo electroplax. Proc. Natl Acad. Sci. USA 81, 2772-2775 (1984).
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 2772-2775
    • Miller, C.1    White, M.M.2
  • 9
    • 0025200567 scopus 로고
    • Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes
    • Jentsch, T. J., Steinmeyer, K., Schwarz, G. Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Nature 348, 510-514 (1990).
    • (1990) Nature , vol.348 , pp. 510-514
    • Jentsch, T.J.1    Steinmeyer, K.2    Schwarz, G.3
  • 10
    • 1542288949 scopus 로고    scopus 로고
    • Secondary active transport mediated by a prokaryotic homologue of ClC Cl channels
    • Accardi, A., Miller, C. Secondary active transport mediated by a prokaryotic homologue of ClC Cl channels. Nature 427, 803-807 (2004).
    • (2004) Nature , vol.427 , pp. 803-807
    • Accardi, A.1    Miller, C.2
  • 11
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel, O., Zdebik, A. A., Lourdel, S., Jentsch, T. J. Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436, 424-427 (2005).
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 12
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo, A., Pusch, M. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436, 420-423 (2005).
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 13
    • 33947720910 scopus 로고    scopus 로고
    • Uncoupling and turnover in a Cl/H+ exchange transporter
    • Walden, M., et al. Uncoupling and turnover in a Cl/H+ exchange transporter. J. Gen. Physiol. 129, 317-329 (2007).
    • (2007) J. Gen. Physiol. , vol.129 , pp. 317-329
    • Walden, M.1
  • 14
    • 49649112453 scopus 로고    scopus 로고
    • Ion permeation through a Cl-selective channel designed from a CLC Cl/H+ exchanger
    • Jayaram, H., Accardi, A., Wu, F., Williams, C., Miller, C. Ion permeation through a Cl-selective channel designed from a CLC Cl/H+ exchanger. Proc. Natl Acad. Sci. USA 105, 11194-11199 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 11194-11199
    • Jayaram, H.1    Accardi, A.2    Wu, F.3    Williams, C.4    Miller, C.5
  • 15
    • 0029743660 scopus 로고    scopus 로고
    • Two physically distinct pores in the dimeric ClC-0 chloride channel
    • Ludewig, U., Pusch, M., Jentsch, T. J. Two physically distinct pores in the dimeric ClC-0 chloride channel. Nature 383, 340-343 (1996).
    • (1996) Nature , vol.383 , pp. 340-343
    • Ludewig, U.1    Pusch, M.2    Jentsch, T.J.3
  • 16
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3. 0 Å reveals the molecular basis of anion selectivity
    • Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T., MacKinnon, R. X-ray structure of a ClC chloride channel at 3. 0 Å reveals the molecular basis of anion selectivity. Nature 415, 287-294 (2002).
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 17
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., Campbell, E. B., MacKinnon, R. Gating the selectivity filter in ClC chloride channels. Science 300, 108-112 (2003).
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 18
    • 78049362741 scopus 로고    scopus 로고
    • Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle
    • Feng, L., Campbell, E. B., Hsiung, Y., MacKinnon, R. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330, 635-641 (2010).
    • (2010) Science , vol.330 , pp. 635-641
    • Feng, L.1    Campbell, E.B.2    Hsiung, Y.3    MacKinnon, R.4
  • 19
    • 0028292022 scopus 로고
    • Two isoforms of a chloride channel predominantly expressed in thick ascending limb of Henle's loop and collecting ducts of rat kidney
    • Adachi, S., et al. Two isoforms of a chloride channel predominantly expressed in thick ascending limb of Henle's loop and collecting ducts of rat kidney. J. Biol. Chem. 269, 17677-17683 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 17677-17683
    • Adachi, S.1
  • 20
    • 0028360729 scopus 로고
    • Two highly homologous members of the ClC chloride channel family in both rat and human kidney
    • Kieferle, S., Fong, P., Bens, M., Vandewalle, A., Jentsch, T. J. Two highly homologous members of the ClC chloride channel family in both rat and human kidney. Proc. Natl Acad. Sci. USA 91, 6943-6947 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6943-6947
    • Kieferle, S.1    Fong, P.2    Bens, M.3    Vandewalle, A.4    Jentsch, T.J.5
  • 22
    • 0035969520 scopus 로고    scopus 로고
    • Barttin is a Cl channel-subunit crucial for renal Cl reabsorption and inner ear K+ secretion
    • Estévez, R., et al. Barttin is a Cl channel-subunit crucial for renal Cl reabsorption and inner ear K+ secretion. Nature 414, 558-561 (2001).
    • (2001) Nature , vol.414 , pp. 558-561
    • Estévez, R.1
  • 23
    • 33746628034 scopus 로고    scopus 로고
    • Barttin modulates trafficking and function of ClC-K channels
    • Scholl, U., et al. Barttin modulates trafficking and function of ClC-K channels. Proc. Natl Acad. Sci. USA 103, 11411-11416 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 11411-11416
    • Scholl, U.1
  • 24
    • 0034637572 scopus 로고    scopus 로고
    • Functional and structural analysis of ClC-K chloride channels involved in renal disease
    • Waldegger, S., Jentsch, T. J. Functional and structural analysis of ClC-K chloride channels involved in renal disease. J. Biol. Chem. 275, 24527-24533 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 24527-24533
    • Waldegger, S.1    Jentsch, T.J.2
  • 25
    • 84882729940 scopus 로고    scopus 로고
    • Characterization of the mouse ClC-K1/Barttin chloride channel
    • L'Hoste, S., et al. Characterization of the mouse ClC-K1/Barttin chloride channel. Biochim. Biophys. Acta 1828, 2399-2409 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2399-2409
    • L'Hoste, S.1
  • 26
    • 0031468569 scopus 로고    scopus 로고
    • Pore-forming segments in voltage-gated chloride channels
    • Fahlke, C., Yu, H. T., Beck, C. L., Rhodes, T. H., George, A. L. Jr. Pore-forming segments in voltage-gated chloride channels. Nature 390, 529-532 (1997).
    • (1997) Nature , vol.390 , pp. 529-532
    • Fahlke, C.1    Yu, H.T.2    Beck, C.L.3    Rhodes, T.H.4    George, Jr.A.L.5
  • 27
    • 0033811517 scopus 로고    scopus 로고
    • Fast and slow gating relaxations in the muscle chloride channel CLC-1
    • Accardi, A., Pusch, M. Fast and slow gating relaxations in the muscle chloride channel CLC-1. J. Gen. Physiol. 116, 433-444 (2000).
    • (2000) J. Gen. Physiol. , vol.116 , pp. 433-444
    • Accardi, A.1    Pusch, M.2
  • 28
    • 0345146920 scopus 로고    scopus 로고
    • Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1
    • Estévez, R., Schroeder, B. C., Accardi, A., Jentsch, T. J., Pusch, M. Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1. Neuron 38, 47-59 (2003).
    • (2003) Neuron , vol.38 , pp. 47-59
    • Estévez, R.1    Schroeder, B.C.2    Accardi, A.3    Jentsch, T.J.4    Pusch, M.5
  • 29
    • 0036452353 scopus 로고    scopus 로고
    • Barttin increases surface expression and changes current properties of ClC-K channels
    • Waldegger, S., et al. Barttin increases surface expression and changes current properties of ClC-K channels. Pflugers Arch. 444, 411-418 (2002).
    • (2002) Pflugers Arch. , vol.444 , pp. 411-418
    • Waldegger, S.1
  • 30
    • 84863919933 scopus 로고    scopus 로고
    • Molecular mechanism of proton transport in CLC Cl/H+ exchange transporters
    • Feng, L., Campbell, E. B., MacKinnon, R. Molecular mechanism of proton transport in CLC Cl/H+ exchange transporters. Proc. Natl Acad. Sci. USA 109, 11699-11704 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 11699-11704
    • Feng, L.1    Campbell, E.B.2    MacKinnon, R.3
  • 31
    • 34249913169 scopus 로고    scopus 로고
    • The structure of the cytoplasmic domain of the chloride channel ClC-Ka reveals a conserved interaction interface
    • Markovic, S., Dutzler, R. The structure of the cytoplasmic domain of the chloride channel ClC-Ka reveals a conserved interaction interface. Structure 15, 715-725 (2007).
    • (2007) Structure , vol.15 , pp. 715-725
    • Markovic, S.1    Dutzler, R.2
  • 32
    • 78650171241 scopus 로고    scopus 로고
    • Design function and structure of a monomeric ClC transporter
    • Robertson, J. L., Kolmakova-Partensky, L., Miller, C. Design, function and structure of a monomeric ClC transporter. Nature 468, 844-847 (2010).
    • (2010) Nature , vol.468 , pp. 844-847
    • Robertson, J.L.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 33
    • 84979547129 scopus 로고    scopus 로고
    • Revealing an outward-facing open conformational state in a CLC Cl/H+ exchange transporter
    • Khantwal, C. M., et al. Revealing an outward-facing open conformational state in a CLC Cl/H+ exchange transporter. eLife 5, e11189 (2016).
    • (2016) ELife , vol.5 , pp. e11189
    • Khantwal, C.M.1
  • 34
    • 0020440405 scopus 로고
    • Open-state substructure of single chloride channels from Torpedo electroplax
    • Miller, C. Open-state substructure of single chloride channels from Torpedo electroplax. Phil. Trans. R. Soc. Lond. B 299, 401-411 (1982).
    • (1982) Phil. Trans. R. Soc. Lond. B , vol.299 , pp. 401-411
    • Miller, C.1
  • 35
    • 0037327607 scopus 로고    scopus 로고
    • Involvement of helices at the dimer interface in ClC-1 common gating
    • Duffield, M., Rychkov, G., Bretag, A., Roberts, M. Involvement of helices at the dimer interface in ClC-1 common gating. J. Gen. Physiol. 121, 149-161 (2003).
    • (2003) J. Gen. Physiol. , vol.121 , pp. 149-161
    • Duffield, M.1    Rychkov, G.2    Bretag, A.3    Roberts, M.4
  • 36
    • 84870984329 scopus 로고    scopus 로고
    • Dissecting a regulatory calcium-binding site of CLC-K kidney chloride channels
    • Gradogna, A., Fenollar-Ferrer, C., Forrest, L. R., Pusch, M. Dissecting a regulatory calcium-binding site of CLC-K kidney chloride channels. J. Gen. Physiol. 140, 681-696 (2012).
    • (2012) J. Gen. Physiol. , vol.140 , pp. 681-696
    • Gradogna, A.1    Fenollar-Ferrer, C.2    Forrest, L.R.3    Pusch, M.4
  • 37
    • 79952074056 scopus 로고    scopus 로고
    • Structure of a slow CLC Cl/H+ antiporter from a cyanobacterium
    • Jayaram, H., Robertson, J. L., Wu, F., Williams, C., Miller, C. Structure of a slow CLC Cl/H+ antiporter from a cyanobacterium. Biochemistry 50, 788-794 (2011).
    • (2011) Biochemistry , vol.50 , pp. 788-794
    • Jayaram, H.1    Robertson, J.L.2    Wu, F.3    Williams, C.4    Miller, C.5
  • 38
    • 84886583065 scopus 로고    scopus 로고
    • Fluoride-dependent interruption of the transport cycle of a CLC Cl/H+ antiporter
    • Lim, H. H., Stockbridge, R. B., Miller, C. Fluoride-dependent interruption of the transport cycle of a CLC Cl/H+ antiporter. Nature Chem. Biol. 9, 721-725 (2013).
    • (2013) Nature Chem. Biol. , vol.9 , pp. 721-725
    • Lim, H.H.1    Stockbridge, R.B.2    Miller, C.3
  • 39
    • 33744950592 scopus 로고    scopus 로고
    • Site-directed fluorescence studies of a prokaryotic ClC antiporter
    • Bell, S. P., Curran, P. K., Choi, S., Mindell, J. A. Site-directed fluorescence studies of a prokaryotic ClC antiporter. Biochemistry 45, 6773-6782 (2006).
    • (2006) Biochemistry , vol.45 , pp. 6773-6782
    • Bell, S.P.1    Curran, P.K.2    Choi, S.3    Mindell, J.A.4
  • 40
    • 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. Conformational changes required for H+/Cl exchange mediated by a CLC transporter. Nature Struct. Mol. Biol. 21, 456-463 (2014).
    • (2014) Nature Struct. Mol. Biol. , vol.21 , pp. 456-463
    • Basilio, D.1    Noack, K.2    Picollo, A.3    Accardi, A.4
  • 41
    • 34547529693 scopus 로고    scopus 로고
    • A preference for edgewise interactions between aromatic rings and carboxylate anions: The biological relevance of anion-quadrupole interactions
    • Jackson, M. R., et al. A preference for edgewise interactions between aromatic rings and carboxylate anions: the biological relevance of anion-quadrupole interactions. J. Phys. Chem. B 111, 8242-8249 (2007).
    • (2007) J. Phys. Chem. B , vol.111 , pp. 8242-8249
    • Jackson, M.R.1
  • 42
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. Simple allosteric model for membrane pumps. Nature 211, 969-970 (1966).
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 43
    • 33748310543 scopus 로고    scopus 로고
    • Uncoupling of a CLC Cl/H+ exchange transporter by polyatomic anions
    • Nguitragool, W., Miller, C. Uncoupling of a CLC Cl/H+ exchange transporter by polyatomic anions. J. Mol. Biol. 362, 682-690 (2006).
    • (2006) J. Mol. Biol. , vol.362 , pp. 682-690
    • Nguitragool, W.1    Miller, C.2
  • 44
    • 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. Synergism between halide binding and proton transport in a CLC-type exchanger. J. Mol. Biol. 362, 691-699 (2006).
    • (2006) J. Mol. Biol. , vol.362 , pp. 691-699
    • Accardi, A.1    Lobet, S.2    Williams, C.3    Miller, C.4    Dutzler, R.5
  • 45
    • 71449123048 scopus 로고    scopus 로고
    • Basis of substrate binding and conservation of selectivity in the CLC family of channels and transporters
    • Picollo, A., Malvezzi, M., Houtman, J. C., Accardi, A. Basis of substrate binding and conservation of selectivity in the CLC family of channels and transporters. Nature Struct. Mol. Biol. 16, 1294-1301 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 1294-1301
    • Picollo, A.1    Malvezzi, M.2    Houtman, J.C.3    Accardi, A.4
  • 46
    • 66449133262 scopus 로고    scopus 로고
    • Residues important for nitrate/proton coupling in plant and mammalian CLC transporters
    • Bergsdorf, E. Y., Zdebik, A. A., Jentsch, T. J. Residues important for nitrate/proton coupling in plant and mammalian CLC transporters. J. Biol. Chem. 284, 11184-11193 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 11184-11193
    • Bergsdorf, E.Y.1    Zdebik, A.A.2    Jentsch, T.J.3
  • 47
    • 59649097040 scopus 로고    scopus 로고
    • Conversion of the 2 Cl/1 H+ antiporter ClC-5 in a NO3/H+ antiporter by a single point mutation
    • Zifarelli, G., Pusch, M. Conversion of the 2 Cl/1 H+ antiporter ClC-5 in a NO3/H+ antiporter by a single point mutation. EMBO J. 28, 175-182 (2009).
    • (2009) EMBO J. , vol.28 , pp. 175-182
    • Zifarelli, G.1    Pusch, M.2
  • 48
    • 33747858034 scopus 로고    scopus 로고
    • The nitrate/proton antiporter AtCLCa mediates nitrate accumulation in plant vacuoles
    • De Angeli, A., et al. The nitrate/proton antiporter AtCLCa mediates nitrate accumulation in plant vacuoles. Nature 442, 939-942 (2006).
    • (2006) Nature , vol.442 , pp. 939-942
    • De Angeli, A.1
  • 49
    • 79955707349 scopus 로고    scopus 로고
    • High cleavage efficiency of a 2A peptide derived from porcine teschovirus-1 in human cell lines, zebrafish and mice
    • Kim, J. H., et al. High cleavage efficiency of a 2A peptide derived from porcine teschovirus-1 in human cell lines, zebrafish and mice. PLoS One 6, e18556 (2011).
    • (2011) PLoS One , vol.6 , pp. e18556
    • Kim, J.H.1
  • 50
    • 0028857849 scopus 로고
    • Efficient gene transfer into human hepatocytes by baculovirus vectors
    • Hofmann, C., et al. Efficient gene transfer into human hepatocytes by baculovirus vectors. Proc. Natl Acad. Sci. USA 92, 10099-10103 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10099-10103
    • Hofmann, C.1
  • 51
    • 84908199292 scopus 로고    scopus 로고
    • Screening and large-scale expression of membrane proteins in mammalian cells for structural studies
    • Goehring, A., et al. Screening and large-scale expression of membrane proteins in mammalian cells for structural studies. Nat. Protoc. 9, 2574-2585 (2014).
    • (2014) Nat. Protoc. , vol.9 , pp. 2574-2585
    • Goehring, A.1
  • 52
    • 77449102676 scopus 로고    scopus 로고
    • Modulation of protein properties in living cells using nanobodies
    • Kirchhofer, A., et al. Modulation of protein properties in living cells using nanobodies. Nature Struct. Mol. Biol. 17, 133-138 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 133-138
    • Kirchhofer, A.1
  • 53
    • 80052546018 scopus 로고    scopus 로고
    • High-efficiency screening of monoclonal antibodies for membrane protein crystallography
    • Lim, H. H., Fang, Y., Williams, C. High-efficiency screening of monoclonal antibodies for membrane protein crystallography. PLoS One 6, e24653 (2011).
    • (2011) PLoS One , vol.6 , pp. e24653
    • Lim, H.H.1    Fang, Y.2    Williams, C.3
  • 54
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36-51 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 55
    • 84930634509 scopus 로고    scopus 로고
    • Measuring the optimal exposure for single particle cryo-EM using a 2. 6 Å reconstruction of rotavirus VP6
    • Grant, T., Grigorieff, N. Measuring the optimal exposure for single particle cryo-EM using a 2. 6 Å reconstruction of rotavirus VP6. eLife 4, e06980 (2015).
    • (2015) ELife , vol.4 , pp. e06980
    • Grant, T.1    Grigorieff, N.2
  • 56
    • 84946488108 scopus 로고    scopus 로고
    • CTFFIND4: Fast and accurate defocus estimation from electron micrographs
    • Rohou, A., Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216-221 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 216-221
    • Rohou, A.1    Grigorieff, N.2
  • 57
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 58
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G., et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 59
    • 84946473054 scopus 로고    scopus 로고
    • Alignment of cryo-EM movies of individual particles by optimization of image translations
    • Rubinstein, J. L., Brubaker, M. A. Alignment of cryo-EM movies of individual particles by optimization of image translations. J. Struct. Biol. 192, 188-195 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 188-195
    • Rubinstein, J.L.1    Brubaker, M.A.2
  • 60
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F., et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 61
    • 84887242753 scopus 로고    scopus 로고
    • One number does not fit all: Mapping local variations in resolution in cryo-EM reconstructions
    • Cardone, G., Heymann, J. B., Steven, A. C. One number does not fit all: mapping local variations in resolution in cryo-EM reconstructions. J. Struct. Biol. 184, 226-236 (2013).
    • (2013) J. Struct. Biol. , vol.184 , pp. 226-236
    • Cardone, G.1    Heymann, J.B.2    Steven, A.C.3
  • 62
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J., Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63-65 (2014).
    • (2014) Nature Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 64
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N., et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 65
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown, A., et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D 71, 136-153 (2015).
    • (2015) Acta Crystallogr. D , vol.71 , pp. 136-153
    • Brown, A.1
  • 67
    • 84900435661 scopus 로고    scopus 로고
    • Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome
    • Fernández, I. S., Bai, X. C., Murshudov, G., Scheres, S. H., Ramakrishnan, V. Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell 157, 823-831 (2014).
    • (2014) Cell , vol.157 , pp. 823-831
    • Fernández, I.S.1    Bai, X.C.2    Murshudov, G.3    Scheres, S.H.4    Ramakrishnan, V.5
  • 68
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: Generating accurate representations of channel and interior surfaces in molecular structures
    • Ho, B. K., Gruswitz, F. HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct. Biol. 8, 49 (2008).
    • (2008) BMC Struct. Biol. , vol.8 , pp. 49
    • Ho, B.K.1    Gruswitz, F.2
  • 69
    • 84868156224 scopus 로고    scopus 로고
    • CAVER 3. 0: A tool for the analysis of transport pathways in dynamic protein structures
    • Chovancova, E., et al. CAVER 3. 0: a tool for the analysis of transport pathways in dynamic protein structures. PLOS Comput. Biol. 8, e1002708 (2012).
    • (2012) PLOS Comput. Biol. , vol.8 , pp. e1002708
    • Chovancova, E.1
  • 70
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A., Sept, D., Joseph, S., Holst, M. J., McCammon, J. A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 71
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence, M. C., Colman, P. M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 72
    • 36749015585 scopus 로고    scopus 로고
    • Chloride channel myotonia: Exon 8 hot-spot for dominantnegative interactions
    • Fialho, D., et al. Chloride channel myotonia: exon 8 hot-spot for dominantnegative interactions. Brain 130, 3265-3274 (2007).
    • (2007) Brain , vol.130 , pp. 3265-3274
    • Fialho, D.1
  • 73
    • 84954381540 scopus 로고    scopus 로고
    • Identification and functional characterization of CLCN1 mutations found in nondystrophic myotonia patients
    • Vindas-Smith, R., et al. Identification and functional characterization of CLCN1 mutations found in nondystrophic myotonia patients. Hum. Mutat. 37, 74-83 (2016).
    • (2016) Hum. Mutat. , vol.37 , pp. 74-83
    • Vindas-Smith, R.1
  • 74
    • 0030032336 scopus 로고    scopus 로고
    • Novel muscle chloride channel mutations and their effects on heterozygous carriers
    • Mailänder, V., Heine, R., Deymeer, F., Lehmann-Horn, F. Novel muscle chloride channel mutations and their effects on heterozygous carriers. Am. J. Hum. Genet. 58, 317-324 (1996).
    • (1996) Am. J. Hum. Genet. , vol.58 , pp. 317-324
    • Mailänder, V.1    Heine, R.2    Deymeer, F.3    Lehmann-Horn, F.4
  • 75
    • 48249104688 scopus 로고    scopus 로고
    • In tandem analysis of CLCN1 and SCN4A greatly enhances mutation detection in families with non-dystrophic myotonia
    • Trip, J., et al. In tandem analysis of CLCN1 and SCN4A greatly enhances mutation detection in families with non-dystrophic myotonia. Eur. J. Hum. Genet. 16, 921-929 (2008).
    • (2008) Eur. J. Hum. Genet. , vol.16 , pp. 921-929
    • Trip, J.1
  • 76
    • 67349266304 scopus 로고    scopus 로고
    • Clinical, electrophysiologic, genetic study of non-dystrophic myotonia in French-Canadians
    • Dupré, N., et al. Clinical, electrophysiologic, genetic study of non-dystrophic myotonia in French-Canadians. Neuromuscul. Disord. 19, 330-334 (2009).
    • (2009) Neuromuscul. Disord. , vol.19 , pp. 330-334
    • Dupré, N.1
  • 77
    • 0028307668 scopus 로고
    • Genomic organization of the human muscle chloride channel CIC-1 and analysis of novel mutations leading to Becker-type myotonia
    • Lorenz, C., Meyer-Kleine, C., Steinmeyer, K., Koch, M. C., Jentsch, T. J. Genomic organization of the human muscle chloride channel CIC-1 and analysis of novel mutations leading to Becker-type myotonia. Hum. Mol. Genet. 3, 941-946 (1994).
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 941-946
    • Lorenz, C.1    Meyer-Kleine, C.2    Steinmeyer, K.3    Koch, M.C.4    Jentsch, T.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.