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Volumn 485, Issue 7396, 2012, Pages 133-136

Erratum: Stereospecific binding of a disordered peptide segment mediates BK channel inactivation (Nature (2012) 485 (133-136) DOI: 10.1038/nature10994);Stereospecific binding of a disordered peptide segment mediates BK channel inactivation

Author keywords

[No Author keywords available]

Indexed keywords

VOLTAGE GATED CALCIUM CHANNEL; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 84860510422     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11457     Document Type: Erratum
Times cited : (18)

References (35)
  • 1
    • 80055012207 scopus 로고    scopus 로고
    • Expanding the proteome: Disordered and alternatively folded proteins
    • Dyson, H. J. Expanding the proteome: disordered and alternatively folded proteins. Q. Rev. Biophys. 44, 467-518 (2011).
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 467-518
    • Dyson, H.J.1
  • 2
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • DOI 10.1038/nature05858, PII NATURE05858
    • Sugase, K., Dyson, H. J.&Wright, P. E.Mechanismof coupled folding and binding of an intrinsically disordered protein. Nature 447, 1021-1025 (2007). (Pubitemid 46975749)
    • (2007) Nature , vol.447 , Issue.7147 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 3
    • 39049162291 scopus 로고    scopus 로고
    • Role of intrinsic flexibility in signal transduction mediated by the cell cycle regulator, p27 Kip1
    • Galea, C. A. et al. Role of intrinsic flexibility in signal transduction mediated by the cell cycle regulator, p27 Kip1. J. Mol. Biol. 376, 827-838 (2008).
    • (2008) J. Mol. Biol. , vol.376 , pp. 827-838
    • Galea, C.A.1
  • 4
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphismandstructural disorder in protein-protein interactions
    • Tompa, P.&Fuxreiter, M.Fuzzy complexes: polymorphismandstructural disorder in protein-protein interactions. Trends Biochem. Sci. 33, 2-8 (2008).
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 5
    • 82655179907 scopus 로고    scopus 로고
    • Modulation of an IDP binding mechanismand rates by helix propensity and non-native interactions: Association of HIF1a with CBP
    • De Sancho, D. & Best, R. B. Modulation of an IDP binding mechanismand rates by helix propensity and non-native interactions: association of HIF1a with CBP. Mol. Biosyst. 8, 256-267 (2012).
    • (2012) Mol. Biosyst. , vol.8 , pp. 256-267
    • De Sancho, D.1    Best, R.B.2
  • 6
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., Zagotta, W. N.& Aldrich, R. W. Biophysical andmolecularmechanisms of Shaker potassium channel inactivation. Science 250, 533-538 (1990). (Pubitemid 120031778)
    • (1990) Science , vol.250 , Issue.4980 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 7
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB
    • Zagotta, W. N., Hoshi, T. & Aldrich, R. W. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science 250, 568-571 (1990). (Pubitemid 120031789)
    • (1990) Science , vol.250 , Issue.4980 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 8
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • DOI 10.1038/35079500
    • Zhou, M., Morais-Cabral, J. H., Mann, S. & MacKinnon, R. Potassium channel receptor site for the inactivation gateandquaternary amine inhibitors.Nature411, 657-661 (2001). (Pubitemid 32531662)
    • (2001) Nature , vol.411 , Issue.6838 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4
  • 9
    • 0025925342 scopus 로고
    • K(A) channels reopen during recovery from inactivation
    • Ruppersberg, J. P., Frank, R., Pongs, O. & Stocker, M. Cloned neuronal IK(A) channels reopen during recovery frominactivation. Nature 353, 657-660 (1991). (Pubitemid 21912582)
    • (1991) Nature , vol.353 , Issue.6345 , pp. 657-660
    • Ruppersberg, J.P.1    Frank, R.2    Pongst, O.3    Stockert, M.4
  • 10
    • 0027788053 scopus 로고
    • Functional role of the NH2-terminal cytoplasmic domain of a mammalian A-type K channel
    • Tseng-Crank, J., Yao, J. A., Berman, M. F. & Tseng, G. N. Functional role of the NH2-terminal cytoplasmic domain of a mammalian A-type K channel. J. Gen. Physiol. 102, 1057-1083 (1993).
    • (1993) J. Gen. Physiol. , vol.102 , pp. 1057-1083
    • Tseng-Crank, J.1    Yao, J.A.2    Berman, M.F.3    Tseng, G.N.4
  • 12
    • 0030742577 scopus 로고    scopus 로고
    • + channel, Rat Kv1.4, Has two potential domains that could produce rapid inactivation
    • DOI 10.1074/jbc.272.31.19333
    • Kondoh, S., Ishii, K., Nakamura, Y. & Taira, N. A mammalian transient type K1 channel, rat Kv1.4, has two potential domains that could produce rapid inactivation. J. Biol. Chem. 272, 19333-19338 (1997). (Pubitemid 27337727)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.31 , pp. 19333-19338
    • Kondoh, S.-I.1    Ishii, K.2    Nakamura, Y.3    Taira, N.4
  • 13
    • 0027724707 scopus 로고
    • Interactions of amino terminal domains of Shaker K channels with a pore blocking site studied with synthetic peptides
    • DOI 10.1085/jgp.102.6.949
    • Murrell-Lagnado, R. D. & Aldrich, R. W. Interactions of amino terminal domains of ShakerK channels with a pore blocking site studied with synthetic peptides. J. Gen. Physiol. 102, 949-975 (1993). (Pubitemid 24004316)
    • (1993) Journal of General Physiology , vol.102 , Issue.6 , pp. 949-975
    • Murrell-Lagnado, R.D.1    Aldrich, R.W.2
  • 14
    • 0031940418 scopus 로고    scopus 로고
    • + channel analyzed by NMR spectroscopy
    • DOI 10.1007/s002490050115
    • Schott, M. K., Antz, C., Frank, R., Ruppersberg, J. P.&Kalbitzer, H. R. Structure of the inactivating gate from the Shaker voltage gated K1 channel analyzed by NMR spectroscopy. Eur. Biophys. J. 27, 99-104 (1998). (Pubitemid 28123530)
    • (1998) European Biophysics Journal , vol.27 , Issue.2 , pp. 99-104
    • Schott, M.K.1    Antz, C.2    Frank, R.3    Ruppersberg, J.P.4    Kalbitzer, H.R.5
  • 17
    • 0035834713 scopus 로고    scopus 로고
    • NMR structure of the 'balland-chain' domain of KCNMB2, the b2-subunit of large conductance Ca21-and voltage-activated potassium channels
    • Bentrop, D., Beyermann, M., Wissmann, R. & Fakler, B. NMR structure of the 'balland-chain' domain of KCNMB2, the b2-subunit of large conductance Ca21-and voltage-activated potassium channels. J. Biol. Chem. 276, 42116-42121 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 42116-42121
    • Bentrop, D.1    Beyermann, M.2    Wissmann, R.3    Fakler, B.4
  • 18
    • 0026045545 scopus 로고
    • The inactivation gate of the ShakerK1channel behaves like an open-channel blocker
    • Demo, S. D.&Yellen, G. The inactivation gate of the ShakerK1channel behaves like an open-channel blocker. Neuron 7, 743-753 (1991).
    • (1991) Neuron , vol.7 , pp. 743-753
    • Demo, S.D.1    Yellen, G.2
  • 19
    • 80052425130 scopus 로고    scopus 로고
    • Editing of human KV1.1 channel mRNAs disrupts binding of the N-terminus tip at the intracellular cavity
    • Gonzalez, C., Lopez-Rodriguez, A., Srikumar, D., Rosenthal, J. J. & Holmgren, M. Editing of human KV1.1 channel mRNAs disrupts binding of the N-terminus tip at the intracellular cavity. Nature Commun. 2, 436, http://dx.doi.org/10.1038/ncomms1446 (2011).
    • (2011) Nature Commun. , vol.2 , pp. 436
    • Gonzalez, C.1    Lopez-Rodriguez, A.2    Srikumar, D.3    Rosenthal, J.J.4    Holmgren, M.5
  • 20
    • 0034967181 scopus 로고    scopus 로고
    • 2 terminus of the β3b auxiliary subunit involves a two-step mechanism: Possible separation of binding and blockade
    • DOI 10.1085/jgp.117.6.583
    • Lingle, C. J., Zeng, X.-H., Ding, J.-P.&Xia, X.-M. InactivationofBKchannelsmediated by the N-terminus of the b3b auxiliary subunit involves a two-step mechanism: possible separation of binding and blockade. J. Gen. Physiol. 117, 583-605 (2001). (Pubitemid 32552266)
    • (2001) Journal of General Physiology , vol.117 , Issue.6 , pp. 583-605
    • Lingle, C.J.1    Zeng, X.-H.2    Ding, J.-P.3    Xia, X.-M.4
  • 21
    • 34247494332 scopus 로고    scopus 로고
    • BK channels with β3a subunits generate use-dependent slow afterhyperpolarizing currents by an inactivation-coupled mechanism
    • DOI 10.1523/JNEUROSCI.0758-07.2007
    • Zeng, X.-H., Xia, X. M. & Lingle, C. J. BK channels with b3a subunits generate usedependent slow afterhyperpolarizing currents by an inactivation-coupled mechanism. J. Neurosci. 27, 4707-4715 (2007). (Pubitemid 46663564)
    • (2007) Journal of Neuroscience , vol.27 , Issue.17 , pp. 4707-4715
    • Zeng, X.-H.1    Benzinger, G.R.2    Xia, X.-M.3    Lingle, C.J.4
  • 22
    • 0345298282 scopus 로고    scopus 로고
    • 2+- and voltage-dependent BK channels in adrenal chromaffin cells and rat insulinoma tumor cells
    • Xia, X.-M., Ding, J. P. & Lingle, C. J. Molecular basis for the inactivation of Ca21-and voltage-dependent BK channels in adrenal chromaffin cells and rat insulinoma tumor cells. J. Neurosci. 19, 5255-5264 (1999). (Pubitemid 29300193)
    • (1999) Journal of Neuroscience , vol.19 , Issue.13 , pp. 5255-5264
    • Xia, X.-M.1    Ding, J.P.2    Lingle, C.J.3
  • 24
    • 0034234522 scopus 로고    scopus 로고
    • 2+-activated, voltage-dependent BK currents: Consequences of rapid inactivation by a novel β subunit
    • Xia, X.-M., Ding, J.-P., Zeng, X.-H., Duan, K.-L. & Lingle, C. J. Rectification and rapid activation at low Ca21 of Ca21-activated, voltage-dependent BK currents: consequences of rapid inactivation by a novel b subunit. J. Neurosci. 20, 4890-4903 (2000). (Pubitemid 30421693)
    • (2000) Journal of Neuroscience , vol.20 , Issue.13 , pp. 4890-4903
    • Xia, X.-M.1    Ding, J.-P.2    Zeng, X.-H.3    Duan, K.-L.4    Lingle, C.J.5
  • 25
    • 67649938992 scopus 로고    scopus 로고
    • Multiple intermediate states precede pore block during N-type inactivation of a voltage-gated potassium channel
    • Prince-Carter, A.&Pfaffinger, P. J. Multiple intermediate states precede pore block during N-type inactivation of a voltage-gated potassium channel. J. Gen. Physiol. 134, 15-34 (2009).
    • (2009) J. Gen. Physiol. , vol.134 , pp. 15-34
    • Prince-Carter, A.1    Pfaffinger, P.J.2
  • 27
    • 3142682254 scopus 로고    scopus 로고
    • Unique inner pore properties of BK channels revealed by quaternary ammonium block
    • DOI 10.1085/jgp.200409067
    • Li, W. & Aldrich, R. W. Unique inner pore properties of BK channels revealed by quaternary ammonium block. J. Gen. Physiol. 124, 43-57 (2004). (Pubitemid 38931929)
    • (2004) Journal of General Physiology , vol.124 , Issue.1 , pp. 43-57
    • Li, W.1    Aldrich, R.W.2
  • 28
    • 33748094494 scopus 로고    scopus 로고
    • State-independent block of BK channels by an intracellular quaternary ammonium
    • DOI 10.1085/jgp.200609579
    • Wilkens, C. M. & Aldrich, R. W. State-independent block of BK channels by an intracellular quaternary ammonium. J. Gen. Physiol. 128, 347-364 (2006). (Pubitemid 44306713)
    • (2006) Journal of General Physiology , vol.128 , Issue.3 , pp. 347-364
    • Wilkens, C.M.1    Aldrich, R.W.2
  • 29
    • 23744472418 scopus 로고    scopus 로고
    • Probing the geometry of the inner vestibule of BK channels with sugars
    • DOI 10.1085/jgp.200509286
    • Brelidze, T. I. & Magleby, K. L. Probing the geometry of the inner vestibule of BK channels with sugars. J. Gen. Physiol. 126, 105-121 (2005). (Pubitemid 41124188)
    • (2005) Journal of General Physiology , vol.126 , Issue.2 , pp. 105-121
    • Brelidze, T.I.1    Magleby, K.L.2
  • 30
    • 79961055467 scopus 로고    scopus 로고
    • Cysteine scanning and modification reveal major differences between BK channels and Kv channels in the inner pore region
    • Zhou, Y., Xia, X. M. & Lingle, C. J. Cysteine scanning and modification reveal major differences between BK channels and Kv channels in the inner pore region. Proc. Natl Acad. Sci. USA 108, 12161-12166 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 12161-12166
    • Zhou, Y.1    Xia, X.M.2    Lingle, C.J.3
  • 31
    • 70350465140 scopus 로고    scopus 로고
    • Closed channel block of BK potassiumchannels by bbTBA requires partial activation
    • Tang, Q., Zeng, X.-H. & Lingle, C. J. Closed channel block of BK potassiumchannels by bbTBA requires partial activation. J. Gen. Physiol. 134, 409-436 (2009).
    • (2009) J. Gen. Physiol. , vol.134 , pp. 409-436
    • Tang, Q.1    Zeng, X.-H.2    Lingle, C.J.3
  • 32
    • 48749112359 scopus 로고    scopus 로고
    • Species-specific differences among KCNMB3 BK b3 auxiliary subunits: Some b3 variants may be primate-specific subunits
    • Zeng, X., Xia, X. M. & Lingle, C. J. Species-specific differences among KCNMB3 BK b3 auxiliary subunits: some b3 variants may be primate-specific subunits. J. Gen. Physiol. 132, 115-129 (2008).
    • (2008) J. Gen. Physiol. , vol.132 , pp. 115-129
    • Zeng, X.1    Xia, X.M.2    Lingle, C.J.3
  • 33
    • 0038103596 scopus 로고    scopus 로고
    • Redox-sensitive extracellular gates formed by auxiliary β subunits of calcium-activated potassium channels
    • DOI 10.1038/nsb932
    • Zeng, X.-H., Xia, X.-M. & Lingle, C. J. Redox-sensitive extracellular gates formed by auxiliary b subunits of calcium-activated potassium channels. Nature Struct. Biol. 10, 448-454 (2003). (Pubitemid 36637642)
    • (2003) Nature Structural Biology , vol.10 , Issue.6 , pp. 448-454
    • Zeng, X.-H.1    Xia, X.-M.2    Lingle, C.J.3
  • 35
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • DOI 10.1007/BF00656997
    • Hamill, O. P., Marty, A., Neher, E., Sakmann, B. & Sigworth, F. J. Improved patchclamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflügers Arch. 391, 85-100 (1981). (Pubitemid 11012976)
    • (1981) Pflugers Archiv European Journal of Physiology , vol.391 , Issue.2 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3


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