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Volumn 131, Issue 6, 2008, Pages 537-548

Position and role of the BK channel α subunit s0 helix inferred from disulfide crosslinking

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL ALPHA SUBUNIT;

EID: 44349137529     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200809968     Document Type: Article
Times cited : (45)

References (37)
  • 1
    • 25444519458 scopus 로고    scopus 로고
    • 2+ sensitivity is enhanced by its β1 subunit
    • 2+ sensitivity is enhanced by its β1 subunit. J. Gen. Physiol. 126:393-412.
    • (2005) J. Gen. Physiol , vol.126 , pp. 393-412
    • Bao, L.1    Cox, D.H.2
  • 2
    • 85058203003 scopus 로고    scopus 로고
    • The PICM chemical scanning method for identifying domain-domain and protein-protein interfaces: Applications to the core signaling complex of E. coli chemotaxis
    • Bass, R.B., A.S. Miller, S.L. Gloor, and J.J. Falke. 2007. The PICM chemical scanning method for identifying domain-domain and protein-protein interfaces: applications to the core signaling complex of E. coli chemotaxis. Methods Enzymol. 423:1-24.
    • (2007) Methods Enzymol , vol.423 , pp. 1-24
    • Bass, R.B.1    Miller, A.S.2    Gloor, S.L.3    Falke, J.J.4
  • 3
    • 33747505832 scopus 로고    scopus 로고
    • Catalysis of covalent Lp(a) assembly: Evidence for an extracellular enzyme activity that enhances disulfide bond formation
    • Becker, L., M.E. Nesheim, and M.L. Koschinsky. 2006. Catalysis of covalent Lp(a) assembly: evidence for an extracellular enzyme activity that enhances disulfide bond formation. Biochemistry. 45:9919-9928.
    • (2006) Biochemistry , vol.45 , pp. 9919-9928
    • Becker, L.1    Nesheim, M.E.2    Koschinsky, M.L.3
  • 4
    • 33845207422 scopus 로고    scopus 로고
    • Kinetics of internalization and degradation of N-type voltage-gated calcium channels: Role of the α2/δ subunit
    • Bernstein, G.M., and O.T. Jones. 2007. Kinetics of internalization and degradation of N-type voltage-gated calcium channels: role of the α2/δ subunit. Cell Calcium. 41:27-40.
    • (2007) Cell Calcium , vol.41 , pp. 27-40
    • Bernstein, G.M.1    Jones, O.T.2
  • 5
    • 0021675781 scopus 로고
    • Stereospecific cyclization of β-hydroxyl aryl amides to β-lactams
    • Bose, A.K., M.S. Manhas, D.P. Sahu, and V.R. Hedge. 1984. Stereospecific cyclization of β-hydroxyl aryl amides to β-lactams. Can. J. Chem. 62:2498-2505.
    • (1984) Can. J. Chem , vol.62 , pp. 2498-2505
    • Bose, A.K.1    Manhas, M.S.2    Sahu, D.P.3    Hedge, V.R.4
  • 6
    • 0029740032 scopus 로고    scopus 로고
    • Effects of protein stabilizing agents on thermal backbone motions: A disulfide trapping study
    • Butler, S.L., and J.J. Falke. 1996. Effects of protein stabilizing agents on thermal backbone motions: a disulfide trapping study. Biochemistry. 35:10595-10600.
    • (1996) Biochemistry , vol.35 , pp. 10595-10600
    • Butler, S.L.1    Falke, J.J.2
  • 7
    • 34249946312 scopus 로고    scopus 로고
    • Two atomic constraints unambiguously position the S4 segment relative to S1 and S2 segments in the closed state of Shaker K channel
    • Campos, F.V., B. Chanda, B. Roux, and F. Bezanilla. 2007. Two atomic constraints unambiguously position the S4 segment relative to S1 and S2 segments in the closed state of Shaker K channel. Proc. Natl. Acad. Sci. USA. 104:7904-7909.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7904-7909
    • Campos, F.V.1    Chanda, B.2    Roux, B.3    Bezanilla, F.4
  • 9
    • 17144409399 scopus 로고    scopus 로고
    • Increasing the reactivity of an artificial dithiol-disulfide pair through modification of the electrostatic milieu
    • Hansen, R.E., H. Ostergaard, and J.R. Winther. 2005. Increasing the reactivity of an artificial dithiol-disulfide pair through modification of the electrostatic milieu. Biochemistry. 44:5899-5906.
    • (2005) Biochemistry , vol.44 , pp. 5899-5906
    • Hansen, R.E.1    Ostergaard, H.2    Winther, J.R.3
  • 11
    • 33846849245 scopus 로고    scopus 로고
    • Disulfide trapping the mechanosensitive channel MscL into a gating-transition state
    • Iscla, I., G. Levin, R. Wray, and P. Blount. 2007. Disulfide trapping the mechanosensitive channel MscL into a gating-transition state. Biophys. J. 92:1224-1232.
    • (2007) Biophys. J , vol.92 , pp. 1224-1232
    • Iscla, I.1    Levin, G.2    Wray, R.3    Blount, P.4
  • 12
    • 33646828912 scopus 로고    scopus 로고
    • State-dependent cross-linking of the M2 and M3 segments: Functional basis for the alignment of GABAA and acetylcholine receptor M3 segments
    • Jansen, M., and M.H. Akabas. 2006. State-dependent cross-linking of the M2 and M3 segments: functional basis for the alignment of GABAA and acetylcholine receptor M3 segments. J. Neurosci. 26:4492-4499.
    • (2006) J. Neurosci , vol.26 , pp. 4492-4499
    • Jansen, M.1    Akabas, M.H.2
  • 13
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase
    • Jiang, X.M., M. Fitzgerald, C.M. Grant, and P.J. Hogg. 1999. Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase. J. Biol. Chem. 274:2416-2423.
    • (1999) J. Biol. Chem , vol.274 , pp. 2416-2423
    • Jiang, X.M.1    Fitzgerald, M.2    Grant, C.M.3    Hogg, P.J.4
  • 15
    • 0033966213 scopus 로고    scopus 로고
    • Internalization of the Kv1.4 potassium channel is suppressed by clustering interactions with PSD-95
    • Jugloff, D.G., R. Khanna, L.C. Schlichter, and O.T. Jones. 2000. Internalization of the Kv1.4 potassium channel is suppressed by clustering interactions with PSD-95. J. Biol. Chem. 275:1357-1364.
    • (2000) J. Biol. Chem , vol.275 , pp. 1357-1364
    • Jugloff, D.G.1    Khanna, R.2    Schlichter, L.C.3    Jones, O.T.4
  • 16
    • 2942560888 scopus 로고    scopus 로고
    • Transfer in SDS of biotinylated proteins from acrylamide gels to an avidin-coated membrane filter
    • Karlin, A., C. Wang, J. Li, and Q. Xu. 2004. Transfer in SDS of biotinylated proteins from acrylamide gels to an avidin-coated membrane filter. Biotechniques. 36:1010-1016.
    • (2004) Biotechniques , vol.36 , pp. 1010-1016
    • Karlin, A.1    Wang, C.2    Li, J.3    Xu, Q.4
  • 19
    • 33847340188 scopus 로고    scopus 로고
    • A role for the S0 transmembrane segment in voltage-dependent gating of BK channels
    • Koval, O.M., Y. Fan, and B.S. Rothberg. 2007. A role for the S0 transmembrane segment in voltage-dependent gating of BK channels. J. Gen. Physiol. 129:209-220.
    • (2007) J. Gen. Physiol , vol.129 , pp. 209-220
    • Koval, O.M.1    Fan, Y.2    Rothberg, B.S.3
  • 22
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • Lu, X., A.W. Gross, and H.F. Lodish. 2006. Active conformation of the erythropoietin receptor: random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains. J. Biol. Chem. 281:7002-7011.
    • (2006) J. Biol. Chem , vol.281 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 23
    • 16644396938 scopus 로고    scopus 로고
    • A specific interface between integrin transmembrane helices and affinity for ligand
    • Luo, B.H., T.A. Springer, and J. Takagi. 2004. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol. 2:e153.
    • (2004) PLoS Biol , vol.2
    • Luo, B.H.1    Springer, T.A.2    Takagi, J.3
  • 24
    • 0031457570 scopus 로고    scopus 로고
    • + 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
    • + 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. USA. 94:14066-14071.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14066-14071
    • Meera, P.1    Wallner, M.2    Song, M.3    Toro, L.4
  • 27
    • 0028902788 scopus 로고
    • Transmembrane helices predicted at 95% accuracy
    • Rost, B., R. Casadio, P. Fariselli, and C. Sander. 1995. Transmembrane helices predicted at 95% accuracy. Protein Sci. 4:521-533.
    • (1995) Protein Sci , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 30
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa, N.E., K. McCormack, M.A. Tanouye, and F.J. Sigworth. 1992. The size of gating charge in wild-type and mutant Shaker potassium channels. Science. 255:1712-1715.
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 32
    • 0029988261 scopus 로고    scopus 로고
    • + channels: An additional transmembrane region at the N terminus
    • + channels: an additional transmembrane region at the N terminus. Proc. Natl. Acad. Sci. USA. 93:14922-14927.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14922-14927
    • Wallner, M.1    Meera, P.2    Toro, L.3
  • 33
    • 0027317361 scopus 로고
    • Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping
    • Whitley, P., L. Nilsson, and G. von Heijne. 1993. Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping. Biochemistry. 32:8534-8539.
    • (1993) Biochemistry , vol.32 , pp. 8534-8539
    • Whitley, P.1    Nilsson, L.2    von Heijne, G.3
  • 35
    • 0034705079 scopus 로고    scopus 로고
    • Thiol cross-linking of transmembrane domains IV and V in the lactose permease of Escherichia coli
    • Wolin, C.D., and H.R. Kaback. 2000. Thiol cross-linking of transmembrane domains IV and V in the lactose permease of Escherichia coli. Biochemistry. 39:6130-6135.
    • (2000) Biochemistry , vol.39 , pp. 6130-6135
    • Wolin, C.D.1    Kaback, H.R.2
  • 37
    • 24744455900 scopus 로고    scopus 로고
    • Activation of the BK (SLO1) potassium channel by mallotoxin
    • Zakharov, S.I., J.P. Morrow, G. Liu, L. Yang, and S.O. Marx. 2005. Activation of the BK (SLO1) potassium channel by mallotoxin. J. Biol. Chem. 280:30882-30887.
    • (2005) J. Biol. Chem , vol.280 , pp. 30882-30887
    • Zakharov, S.I.1    Morrow, J.P.2    Liu, G.3    Yang, L.4    Marx, S.O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.