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Volumn 9, Issue 4, 2014, Pages

Intrinsic disorder in the BK channel and its interactome

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ACTIVATED POTASSIUM CHANNEL; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL BETA SUBUNIT; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL GAMMA SUBUNIT; POTASSIUM CHANNEL; UNCLASSIFIED DRUG; INTRINSICALLY DISORDERED PROTEIN; ISOPROTEIN; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; MUTANT PROTEIN; PROTEIN BINDING;

EID: 84899638023     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0094331     Document Type: Article
Times cited : (16)

References (94)
  • 2
    • 0034669882 scopus 로고    scopus 로고
    • Why are 'natively unfolded' proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL (2000) Why are 'natively unfolded' proteins unstructured under physiologic conditions? Proteins 41: 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 4
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • DOI 10.1016/S0968-0004(02)02169-2, PII S0968000402021692
    • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27: 527-533. (Pubitemid 35279598)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 5
  • 6
    • 68749093787 scopus 로고    scopus 로고
    • Predicting intrinsic disorder in proteins: An overview
    • He B, Wang K, Liu Y, Xue B, Uversky VN, et al. (2009) Predicting intrinsic disorder in proteins: an overview. Cell Res 19: 929-949.
    • (2009) Cell Res , vol.19 , pp. 929-949
    • He, B.1    Wang, K.2    Liu, Y.3    Xue, B.4    Uversky, V.N.5
  • 10
    • 77949328500 scopus 로고    scopus 로고
    • The mysterious unfoldome: Structureless, underappreciated, yet vital part of any given proteome
    • Uversky VN (2010) The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome. J Biomed Biotechnol 2010: 568068.
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 568068
    • Uversky, V.N.1
  • 11
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • DOI 10.1016/j.jmb.2004.02.002, PII S0022283604001482
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337: 635-645. (Pubitemid 38326883)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 12
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • DOI 10.1002/jmr.747
    • Uversky VN, Oldfield CJ, Dunker AK (2005) Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18: 343-384. (Pubitemid 41341287)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.5 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 13
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets: The roles of intrinsic disorder in protein interaction networks
    • DOI 10.1111/j.1742-4658.2005.04948.x
    • Dunker AK, Cortese MS, Romero P, Iakoucheva LM, Uversky VN (2005) Flexible nets: The roles of intrinsic disorder in protein interaction networks. FEBS Journal 272: 5129-5148. (Pubitemid 41503146)
    • (2005) FEBS Journal , vol.272 , Issue.20 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 14
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfield CJ, Meng J, Yang JY, Yang MQ, Uversky VN, et al. (2008) Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics 9 Suppl 1: S1.
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL. 1
    • Oldfield, C.J.1    Meng, J.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5
  • 15
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky VN, Oldfield CJ, Dunker AK (2008) Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 37: 215-246.
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 16
    • 33745617904 scopus 로고    scopus 로고
    • Intrinsically disordered C-terminal segments of voltage-activated potassium channels: A possible fishing rod-like mechanism for channel binding to scaffold proteins
    • DOI 10.1093/bioinformatics/btl137
    • Magidovich E, Fleishman SJ, Yifrach O (2006) Intrinsically disordered Cterminal segments of voltage-activated potassium channels: a possible fishing rod-like mechanism for channel binding to scaffold proteins. Bioinformatics 22: 1546-1550. (Pubitemid 43985286)
    • (2006) Bioinformatics , vol.22 , Issue.13 , pp. 1546-1550
    • Magidovich, E.1    Fleishman, S.J.2    Yifrach, O.3
  • 17
    • 33746354305 scopus 로고    scopus 로고
    • Unraveling the nature of the segmentation clock: Intrinsic disorder of clock proteins and their interaction map
    • DOI 10.1016/j.compbiolchem.2006.04.005, PII S1476927106000302
    • Roy S, Schnell S, Radivojac P (2006) Unraveling the nature of the segmentation clock: Intrinsic disorder of clock proteins and their interaction map. Comput Biol Chem 30: 241-248. (Pubitemid 44118829)
    • (2006) Computational Biology and Chemistry , vol.30 , Issue.4 , pp. 241-248
    • Roy, S.1    Schnell, S.2    Radivojac, P.3
  • 18
    • 34047113297 scopus 로고    scopus 로고
    • Intrinsically disordered regions of human plasma membrane proteins preferentially occur in the cytoplasmic segment
    • DOI 10.1016/j.jmb.2007.02.033, PII S0022283607002148
    • Minezaki Y, Homma K, Nishikawa K (2007) Intrinsically disordered regions of human plasma membrane proteins preferentially occur in the cytoplasmic segment. J Mol Biol 368: 902-913. (Pubitemid 46527614)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.3 , pp. 902-913
    • Minezaki, Y.1    Homma, K.2    Nishikawa, K.3
  • 19
    • 49849097024 scopus 로고    scopus 로고
    • Prevalence of intrinsic disorder in the intracellular region of human single-pass type i proteins: The case of the notch ligand Delta-4
    • De Biasio A, Guarnaccia C, Popovic M, Uversky VN, Pintar A, et al. (2008) Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: the case of the notch ligand Delta-4. J Proteome Res 7: 2496-2506.
    • (2008) J Proteome Res , vol.7 , pp. 2496-2506
    • De Biasio, A.1    Guarnaccia, C.2    Popovic, M.3    Uversky, V.N.4    Pintar, A.5
  • 20
    • 44449122934 scopus 로고    scopus 로고
    • Investigation of transmembrane proteins using a computational approach
    • Yang JY, Yang MQ, Dunker AK, Deng Y, Huang X (2008) Investigation of transmembrane proteins using a computational approach. BMC Genomics 9 Suppl 1: S7.
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL. 1
    • Yang, J.Y.1    Yang, M.Q.2    Dunker, A.K.3    Deng, Y.4    Huang, X.5
  • 21
    • 72949087534 scopus 로고    scopus 로고
    • Analysis of structured and intrinsically disordered regions of transmembrane proteins
    • Xue B, Li L, Meroueh SO, Uversky VN, Dunker AK (2009) Analysis of structured and intrinsically disordered regions of transmembrane proteins. Mol Biosyst 5: 1688-1702.
    • (2009) Mol Biosyst , vol.5 , pp. 1688-1702
    • Xue, B.1    Li, L.2    Meroueh, S.O.3    Uversky, V.N.4    Dunker, A.K.5
  • 22
    • 83055178106 scopus 로고    scopus 로고
    • Conserved BK channel-protein interactions reveal signals relevant to cell death and survival
    • Sokolowski B, Orchard S, Harvey M, Sridhar S, Sakai Y (2011) Conserved BK channel-protein interactions reveal signals relevant to cell death and survival. PLoS One 6: e28532.
    • (2011) PLoS One , vol.6
    • Sokolowski, B.1    Orchard, S.2    Harvey, M.3    Sridhar, S.4    Sakai, Y.5
  • 23
    • 68549107901 scopus 로고    scopus 로고
    • A protein interaction network for the large conductance Ca(2+)-activated K(+) channel in the mouse cochlea
    • Kathiresan T, Harvey M, Orchard S, Sakai Y, Sokolowski B (2009) A protein interaction network for the large conductance Ca(2+)-activated K(+) channel in the mouse cochlea. Mol Cell Proteomics 8: 1972-1987.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1972-1987
    • Kathiresan, T.1    Harvey, M.2    Orchard, S.3    Sakai, Y.4    Sokolowski, B.5
  • 24
    • 80052632039 scopus 로고    scopus 로고
    • Identification and quantification of fulllength BK channel variants in the developing mouse cochlea
    • Sakai Y, Harvey M, Sokolowski B (2011) Identification and quantification of fulllength BK channel variants in the developing mouse cochlea. J Neurosci Res 89: 1747-1760.
    • (2011) J Neurosci Res , vol.89 , pp. 1747-1760
    • Sakai, Y.1    Harvey, M.2    Sokolowski, B.3
  • 25
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • Consortium U (2012) Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Research 40: D71-D75.
    • (2012) Nucleic Acids Research , vol.40
    • Consortium, U.1
  • 28
    • 77956502766 scopus 로고    scopus 로고
    • Improved sequence-based prediction of disordered regions with multilayer fusion of multiple information sources
    • Mizianty MJ, Stach W, Chen K, Kedarisetti KD, Disfani FM, et al. (2010) Improved sequence-based prediction of disordered regions with multilayer fusion of multiple information sources. Bioinformatics 26: i489-496.
    • (2010) Bioinformatics , vol.26
    • Mizianty, M.J.1    Stach, W.2    Chen, K.3    Kedarisetti, K.D.4    Disfani, F.M.5
  • 30
    • 84857129811 scopus 로고    scopus 로고
    • Comprehensive comparative assessment of in-silico predictors of disordered regions
    • Peng ZL, Kurgan L (2012) Comprehensive comparative assessment of in-silico predictors of disordered regions. Curr Protein Pept Sci 13: 6-18.
    • (2012) Curr Protein Pept Sci , vol.13 , pp. 6-18
    • Peng, Z.L.1    Kurgan, L.2
  • 33
    • 74249104442 scopus 로고    scopus 로고
    • Assessment of disorder predictions in CASP8
    • Noivirt-Brik O, Prilusky J, Sussman JL (2009) Assessment of disorder predictions in CASP8. Proteins 77: 210-216.
    • (2009) Proteins , vol.77 , pp. 210-216
    • Noivirt-Brik, O.1    Prilusky, J.2    Sussman, J.L.3
  • 35
    • 65249102824 scopus 로고    scopus 로고
    • Close encounters of the third kind disordered domains and the interactions of proteins
    • Tompa P, Fuxreiter M, Oldfield CJ, Simon I, Dunker AK, et al. (2009) Close encounters of the third kind: disordered domains and the interactions of proteins. Bioessays 31: 328-335.
    • (2009) Bioessays , vol.31 , pp. 328-335
    • Tompa, P.1    Fuxreiter, M.2    Oldfield, C.J.3    Simon, I.4    Dunker, A.K.5
  • 38
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with α-helix-forming molecular recognition elements
    • DOI 10.1021/bi050736e
    • Oldfield CJ, Cheng Y, Cortese MS, Romero P, Uversky VN, et al. (2005) Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44: 12454-12470. (Pubitemid 41324337)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 40
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • DOI 10.1006/jmbi.1999.3091
    • Jones DT (1999) Protein secondary structure prediction based on positionspecific scoring matrices. Journal of Molecular Biology 292: 195-202. (Pubitemid 29435759)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 41
    • 67049119327 scopus 로고    scopus 로고
    • Prediction of protein binding regions in disordered proteins
    • Meszaros B, Simon I, Dosztanyi Z (2009) Prediction of protein binding regions in disordered proteins. PLoS Comput Biol 5: e1000376.
    • (2009) PLoS Comput Biol , vol.5
    • Meszaros, B.1    Simon, I.2    Dosztanyi, Z.3
  • 42
    • 70349996473 scopus 로고    scopus 로고
    • ANCHOR: Web server for predicting protein binding regions in disordered proteins
    • Dosztanyi Z, Meszaros B, Simon I (2009) ANCHOR: web server for predicting protein binding regions in disordered proteins. Bioinformatics 25: 2745-2746.
    • (2009) Bioinformatics , vol.25 , pp. 2745-2746
    • Dosztanyi, Z.1    Meszaros, B.2    Simon, I.3
  • 43
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • DOI 10.1093/bioinformatics/bti541
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21: 3433-3434. (Pubitemid 41222453)
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 44
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • DOI 10.1016/j.jmb.2005.01.071
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 347: 827-839. (Pubitemid 40357923)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.4 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 47
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: Recent updates and new developments
    • Letunic I, Doerks T, Bork P (2009) SMART 6: recent updates and new developments. Nucleic Acids Res 37: D229-232.
    • (2009) Nucleic Acids Res , vol.37
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 48
    • 33748505263 scopus 로고    scopus 로고
    • Incorporating background frequency improves entropy-based residue conservation measures
    • Wang K, Samudrala R (2006) Incorporating background frequency improves entropy-based residue conservation measures. BMC Bioinformatics 7.
    • (2006) BMC Bioinformatics , vol.7
    • Wang, K.1    Samudrala, R.2
  • 50
  • 51
    • 84897112748 scopus 로고    scopus 로고
    • A creature with a hundred waggly tails: Intrinsically disordered proteins in the ribosome
    • Peng Z, Oldfield CJ, Xue B, Mizianty MJ, Dunker AK, et al. (2013) A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome. Cell Mol Life Sci.
    • (2013) Cell Mol Life Sci
    • Peng, Z.1    Oldfield, C.J.2    Xue, B.3    Mizianty, M.J.4    Dunker, A.K.5
  • 52
    • 84882279043 scopus 로고    scopus 로고
    • Resilience of death intrinsic disorder in proteins involved in the programmed cell death
    • Peng Z, Xue B, Kurgan L, Uversky VN (2013) Resilience of death: intrinsic disorder in proteins involved in the programmed cell death. Cell Death Differ 20: 1257-1267.
    • (2013) Cell Death Differ , vol.20 , pp. 1257-1267
    • Peng, Z.1    Xue, B.2    Kurgan, L.3    Uversky, V.N.4
  • 53
    • 84856577919 scopus 로고    scopus 로고
    • Prediction and analysis of nucleotidebinding residues using sequence and sequence-derived structural descriptors
    • Chen K, Mizianty MJ, Kurgan L (2012) Prediction and analysis of nucleotidebinding residues using sequence and sequence-derived structural descriptors. Bioinformatics 28: 331-341.
    • (2012) Bioinformatics , vol.28 , pp. 331-341
    • Chen, K.1    Mizianty, M.J.2    Kurgan, L.3
  • 54
    • 77954686958 scopus 로고    scopus 로고
    • A comparative study of conservation and variation scores
    • Johansson F, Toh H (2010) A comparative study of conservation and variation scores. BMC Bioinformatics 11.
    • (2010) BMC Bioinformatics , vol.11
    • Johansson, F.1    Toh, H.2
  • 61
    • 84879490227 scopus 로고    scopus 로고
    • RAPID: Fast and accurate sequence-based prediction of intrinsic disorder content on proteomic scale
    • Yan J, Mizianty MJ, Filipow PL, Uversky VN, Kurgan L (2013) RAPID: fast and accurate sequence-based prediction of intrinsic disorder content on proteomic scale. Biochim Biophys Acta 1834: 1671-1680.
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 1671-1680
    • Yan, J.1    Mizianty, M.J.2    Filipow, P.L.3    Uversky, V.N.4    Kurgan, L.5
  • 63
    • 77954591491 scopus 로고    scopus 로고
    • Structure of the human BK channel Ca2+-activation apparatus at 3 0 A resolution
    • Yuan P, Leonetti MD, Pico AR, Hsiung Y, MacKinnon R (2010) Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution. Science 329: 182-186.
    • (2010) Science , vol.329 , pp. 182-186
    • Yuan, P.1    Leonetti, M.D.2    Pico, A.R.3    Hsiung, Y.4    Mackinnon, R.5
  • 65
    • 84860510422 scopus 로고    scopus 로고
    • Stereospecific binding of a disordered peptide segment mediates BK channel inactivation
    • Gonzalez-Perez V, Zeng XH, Henzler-Wildman K, Lingle CJ (2012) Stereospecific binding of a disordered peptide segment mediates BK channel inactivation. Nature 485: 133-136.
    • (2012) Nature , vol.485 , pp. 133-136
    • Gonzalez-Perez, V.1    Zeng, X.H.2    Henzler-Wildman, K.3    Lingle, C.J.4
  • 66
    • 80051941216 scopus 로고    scopus 로고
    • Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein
    • Choi UB, Xiao S, Wollmuth LP, Bowen ME (2011) Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein. J Biol Chem 286: 29904-29912.
    • (2011) J Biol Chem , vol.286 , pp. 29904-29912
    • Choi, U.B.1    Xiao, S.2    Wollmuth, L.P.3    Bowen, M.E.4
  • 67
    • 84863894629 scopus 로고    scopus 로고
    • Hair cell BK channels interact with RACK1, and PKC increases its expression on the cell surface by indirect phosphorylation
    • Surguchev A, Bai JP, Joshi P, Navaratnam D (2012) Hair cell BK channels interact with RACK1, and PKC increases its expression on the cell surface by indirect phosphorylation. Am J Physiol Cell Physiol 303: C143-150.
    • (2012) Am J Physiol Cell Physiol , vol.303
    • Surguchev, A.1    Bai, J.P.2    Joshi, P.3    Navaratnam, D.4
  • 68
    • 77954659083 scopus 로고    scopus 로고
    • Structure of the gating ring from the human large-conductance Ca(2+)-gated K(+) channel
    • Wu Y, Yang Y, Ye S, Jiang Y (2010) Structure of the gating ring from the human large-conductance Ca(2+)-gated K(+) channel. Nature 466: 393-397.
    • (2010) Nature , vol.466 , pp. 393-397
    • Wu, Y.1    Yang, Y.2    Ye, S.3    Jiang, Y.4
  • 70
    • 84862992463 scopus 로고    scopus 로고
    • Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks
    • Buljan M, Chalancon G, Eustermann S, Wagner GP, Fuxreiter M, et al. (2012) Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks. Mol Cell 46: 871-883.
    • (2012) Mol Cell , vol.46 , pp. 871-883
    • Buljan, M.1    Chalancon, G.2    Eustermann, S.3    Wagner, G.P.4    Fuxreiter, M.5
  • 71
    • 84879143595 scopus 로고    scopus 로고
    • Alternative splicing of intrinsically disordered regions and rewiring of protein interactions
    • Buljan M, Chalancon G, Dunker AK, Bateman A, Balaji S, et al. (2013) Alternative splicing of intrinsically disordered regions and rewiring of protein interactions. Curr Opin Struct Biol 23: 443-450.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 443-450
    • Buljan, M.1    Chalancon, G.2    Dunker, A.K.3    Bateman, A.4    Balaji, S.5
  • 72
    • 34249044569 scopus 로고    scopus 로고
    • Alternatively spliced C-terminal domains regulate the surface expression of large conductance calcium-activated potassium channels
    • DOI 10.1016/j.neuroscience.2007.03.038, PII S0306452207003375
    • Kim EY, Ridgway LD, Zou S, Chiu YH, Dryer SE (2007) Alternatively spliced C-terminal domains regulate the surface expression of large conductance calcium-activated potassium channels. Neuroscience 146: 1652-1661. (Pubitemid 46783216)
    • (2007) Neuroscience , vol.146 , Issue.4 , pp. 1652-1661
    • Kim, E.Y.1    Ridgway, L.D.2    Zou, S.3    Chiu, Y.-H.4    Dryer, S.E.5
  • 74
    • 70249124205 scopus 로고    scopus 로고
    • Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy
    • Wang L, Sigworth FJ (2009) Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy. Nature 461: 292-295.
    • (2009) Nature , vol.461 , pp. 292-295
    • Wang, L.1    Sigworth, F.J.2
  • 75
    • 68949092127 scopus 로고    scopus 로고
    • Modulation of the conductance-voltage relationship of the BK(Ca) channel by shortening the cytosolic loop connecting two RCK domains
    • Lee JH, Kim HJ, Kim HD, Lee BC, Chun JS, et al. (2009) Modulation of the conductance-voltage relationship of the BK(Ca) channel by shortening the cytosolic loop connecting two RCK domains. Biophysical Journal 97: 730-737.
    • (2009) Biophysical Journal , vol.97 , pp. 730-737
    • Lee, J.H.1    Kim, H.J.2    Kim, H.D.3    Lee, B.C.4    Chun, J.S.5
  • 76
    • 33845623249 scopus 로고    scopus 로고
    • A noncanonical SH3 domain binding motif links BK channels to the actin cytoskeleton via the SH3 adapter cortactin
    • Tian L, Chen L, McClafferty H, Sailer CA, Ruth P, et al. (2006) A noncanonical SH3 domain binding motif links BK channels to the actin cytoskeleton via the SH3 adapter cortactin. FASEB J 20: 2588-2590.
    • (2006) FASEB J , vol.20 , pp. 2588-2590
    • Tian, L.1    Chen, L.2    McClafferty, H.3    Sailer, C.A.4    Ruth, P.5
  • 77
    • 0029988261 scopus 로고    scopus 로고
    • Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: An additional transmembrane region at the N terminus
    • Wallner M, Meera P, Toro L (1996) Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N terminus. Proc Natl Acad Sci U S A 93: 14922-14927.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 14922-14927
    • Wallner, M.1    Meera, P.2    Toro, L.3
  • 78
    • 0031457570 scopus 로고    scopus 로고
    • Large conductance voltage-and calcium-dependent K+ channel, a distinct member of voltage-dependent ion channels with seven N-terminal transmembrane segments (S0-S6), an extracellular N terminus, and an intracellular (S9-S10) C terminus
    • Meera P, Wallner M, Song M, Toro L (1997) Large conductance voltage-and calcium-dependent K+ channel, a distinct member of voltage-dependent ion channels with seven N-terminal transmembrane segments (S0-S6), an extracellular N terminus, and an intracellular (S9-S10) C terminus. Proc Natl Acad Sci U S A 94: 14066-14071.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 14066-14071
    • Meera, P.1    Wallner, M.2    Song, M.3    Toro, L.4
  • 79
    • 0001671930 scopus 로고    scopus 로고
    • Maxi-K(Ca), a Unique Member of the Voltage-Gated K Channel Superfamily
    • Toro L, Wallner M, Meera P, Tanaka Y (1998) Maxi-K(Ca), a Unique Member of the Voltage-Gated K Channel Superfamily. News Physiol Sci 13: 112-117.
    • (1998) News Physiol Sci , vol.13 , pp. 112-117
    • Toro, L.1    Wallner, M.2    Meera, P.3    Tanaka, Y.4
  • 80
    • 33847340188 scopus 로고    scopus 로고
    • A role for the S0 transmembrane segment in voltage-dependent gating of BK channels
    • DOI 10.1085/jgp.200609662
    • Koval OM, Fan Y, Rothberg BS (2007) A role for the S0 transmembrane segment in voltage-dependent gating of BK channels. J Gen Physiol 129: 209-220. (Pubitemid 46333923)
    • (2007) Journal of General Physiology , vol.129 , Issue.3 , pp. 209-220
    • Koval, O.M.1    Fan, Y.2    Rothberg, B.S.3
  • 81
    • 55549119918 scopus 로고    scopus 로고
    • Activation of Slo1 BK channels by Mg2+ coordinated between the voltage sensor and RCK1 domains
    • Yang H, Shi J, Zhang G, Yang J, Delaloye K, et al. (2008) Activation of Slo1 BK channels by Mg2+ coordinated between the voltage sensor and RCK1 domains. Nat Struct Mol Biol 15: 1152-1159.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1152-1159
    • Yang, H.1    Shi, J.2    Zhang, G.3    Yang, J.4    Delaloye, K.5
  • 82
    • 84855495074 scopus 로고    scopus 로고
    • Mg(2+) binding to open and closed states can activate BK channels provided that the voltage sensors are elevated
    • Chen RS, Geng Y, Magleby KL (2011) Mg(2+) binding to open and closed states can activate BK channels provided that the voltage sensors are elevated. J Gen Physiol 138: 593-607.
    • (2011) J Gen Physiol , vol.138 , pp. 593-607
    • Chen, R.S.1    Geng, Y.2    Magleby, K.L.3
  • 83
    • 84880950055 scopus 로고    scopus 로고
    • Intracellular segment between transmembrane helices S0 and S1 of BK channel alpha subunit contains two amphipathic helices connected by a flexible loop
    • Shi P, Li D, Lai C, Zhang L, Tian C (2013) Intracellular segment between transmembrane helices S0 and S1 of BK channel alpha subunit contains two amphipathic helices connected by a flexible loop. Biochem Biophys Res Commun 437: 408-412.
    • (2013) Biochem Biophys Res Commun , vol.437 , pp. 408-412
    • Shi, P.1    Li, D.2    Lai, C.3    Zhang, L.4    Tian, C.5
  • 84
    • 0030801892 scopus 로고    scopus 로고
    • + channel α- and β-subunits in HEK293 cells
    • DOI 10.1016/S0014-5793(97)01096-X, PII S001457939701096X
    • Ahring PK, Strobaek D, Christophersen P, Olesen SP, Johansen TE (1997) Stable expression of the human large-conductance Ca2+-activated K+ channel alpha-and beta-subunits in HEK293 cells. FEBS Lett 415: 67-70. (Pubitemid 27402051)
    • (1997) FEBS Letters , vol.415 , Issue.1 , pp. 67-70
    • Ahring, P.K.1    Strobaek, D.2    Christophersen, P.3    Olesen, S.-P.4    Johansen, T.E.5
  • 86
    • 77954954506 scopus 로고    scopus 로고
    • LRRC26 auxiliary protein allows BK channel activation at resting voltage without calcium
    • Yan J, Aldrich RW (2010) LRRC26 auxiliary protein allows BK channel activation at resting voltage without calcium. Nature 466: 513-516.
    • (2010) Nature , vol.466 , pp. 513-516
    • Yan, J.1    Aldrich, R.W.2
  • 87
    • 84861209847 scopus 로고    scopus 로고
    • BK potassium channel modulation by leucine-rich repeat-containing proteins
    • Yan J, Aldrich RW (2012) BK potassium channel modulation by leucine-rich repeat-containing proteins. Proc Natl Acad Sci U S A 109: 7917-7922.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 7917-7922
    • Yan, J.1    Aldrich, R.W.2
  • 88
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil A, Nakamura H (2006) Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett 580: 2041-2045.
    • (2006) FEBS Lett , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 91
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • DOI 10.1016/S0962-8924(00)01800-6, PII S0962892400018006
    • Chin D, Means AR (2000) Calmodulin: a prototypical calcium sensor. Trends Cell Biol 10: 322-328. (Pubitemid 30445239)
    • (2000) Trends in Cell Biology , vol.10 , Issue.8 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 92
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • Barbato G, Ikura M, Kay LE, Pastor RW, Bax A (1992) Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 31: 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 93
    • 0031574184 scopus 로고    scopus 로고
    • Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering
    • Wall ME, Clarage JB, Phillips GN (1997) Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering. Structure 5: 1599-1612. (Pubitemid 28051974)
    • (1997) Structure , vol.5 , Issue.12 , pp. 1599-1612
    • Wall, M.E.1    Clarage, J.B.2    Phillips Jr., G.N.3
  • 94
    • 33645292569 scopus 로고    scopus 로고
    • Calmodulin signaling: Analysis and prediction of a disorder-dependent molecular recognition
    • Radivojac P, Vucetic S, O'Connor TR, Uversky VN, Obradovic Z, et al. (2006) Calmodulin signaling: analysis and prediction of a disorder-dependent molecular recognition. Proteins 63: 398-410.
    • (2006) Proteins , vol.63 , pp. 398-410
    • Radivojac, P.1    Vucetic, S.2    O'connor, T.R.3    Uversky, V.N.4    Obradovic, Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.