메뉴 건너뛰기




Volumn 109, Issue 12, 2015, Pages 2452-2460

The Nucleotide-Binding Sites of SUR1: A Mechanistic Model

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOTIDE; SULFONYLUREA RECEPTOR;

EID: 84954186560     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.10.026     Document Type: Review
Times cited : (27)

References (64)
  • 1
    • 61749092746 scopus 로고    scopus 로고
    • Modeling K(ATP) channel gating and its regulation
    • P. Proks, and F.M. Ashcroft Modeling K(ATP) channel gating and its regulation Prog. Biophys. Mol. Biol. 99 2009 7 19
    • (2009) Prog. Biophys. Mol. Biol. , vol.99 , pp. 7-19
    • Proks, P.1    Ashcroft, F.M.2
  • 2
    • 0032499773 scopus 로고    scopus 로고
    • MgATP activates the beta cell KATP channel by interaction with its SUR1 subunit
    • F.M. Gribble, and S.J. Tucker F.M. Ashcroft MgATP activates the beta cell KATP channel by interaction with its SUR1 subunit Proc. Natl. Acad. Sci. USA 95 1998 7185 7190
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7185-7190
    • Gribble, F.M.1    Tucker, S.J.2    Ashcroft, F.M.3
  • 3
    • 0030016913 scopus 로고    scopus 로고
    • Adenosine diphosphate as an intracellular regulator of insulin secretion
    • C.G. Nichols, and S.L. Shyng J. Bryan Adenosine diphosphate as an intracellular regulator of insulin secretion Science 272 1996 1785 1787
    • (1996) Science , vol.272 , pp. 1785-1787
    • Nichols, C.G.1    Shyng, S.L.2    Bryan, J.3
  • 4
    • 0030609142 scopus 로고    scopus 로고
    • Regulation of KATP channel activity by diazoxide and MgADP. Distinct functions of the two nucleotide binding folds of the sulfonylurea receptor
    • S. Shyng, T. Ferrigni, and C.G. Nichols Regulation of KATP channel activity by diazoxide and MgADP. Distinct functions of the two nucleotide binding folds of the sulfonylurea receptor J. Gen. Physiol. 110 1997 643 654
    • (1997) J. Gen. Physiol. , vol.110 , pp. 643-654
    • Shyng, S.1    Ferrigni, T.2    Nichols, C.G.3
  • 5
    • 0031005755 scopus 로고    scopus 로고
    • Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor
    • S.J. Tucker, and F.M. Gribble F.M. Ashcroft Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor Nature 387 1997 179 183
    • (1997) Nature , vol.387 , pp. 179-183
    • Tucker, S.J.1    Gribble, F.M.2    Ashcroft, F.M.3
  • 6
    • 0028972501 scopus 로고
    • Reconstitution of IKATP: An inward rectifier subunit plus the sulfonylurea receptor
    • N. Inagaki, and T. Gonoi J. Bryan Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor Science 270 1995 1166 1170
    • (1995) Science , vol.270 , pp. 1166-1170
    • Inagaki, N.1    Gonoi, T.2    Bryan, J.3
  • 7
    • 77249133116 scopus 로고    scopus 로고
    • New uses for old drugs: Neonatal diabetes and sulphonylureas
    • F.M. Ashcroft New uses for old drugs: neonatal diabetes and sulphonylureas Cell Metab. 11 2010 179 181
    • (2010) Cell Metab. , vol.11 , pp. 179-181
    • Ashcroft, F.M.1
  • 8
    • 33746686369 scopus 로고    scopus 로고
    • Switching from insulin to oral sulfonylureas in patients with diabetes due to Kir6.2 mutations
    • E.R. Pearson, I. Flechtner A.T. Hattersley Neonatal Diabetes International Collaborative Group Switching from insulin to oral sulfonylureas in patients with diabetes due to Kir6.2 mutations N. Engl. J. Med. 355 2006 467 477
    • (2006) N. Engl. J. Med. , vol.355 , pp. 467-477
    • Pearson, E.R.1    Flechtner, I.2    Hattersley, A.T.3
  • 9
    • 0032949661 scopus 로고    scopus 로고
    • Cardioprotection by opening of the K(ATP) channel in unstable angina. Is this a clinical manifestation of myocardial preconditioning? Results of a randomized study with nicorandil. CESAR 2 investigation. Clinical European studies in angina and revascularization
    • D.J. Patel, H.J. Purcell, and K.M. Fox Cardioprotection by opening of the K(ATP) channel in unstable angina. Is this a clinical manifestation of myocardial preconditioning? Results of a randomized study with nicorandil. CESAR 2 investigation. Clinical European studies in angina and revascularization Eur. Heart J. 20 1999 51 57
    • (1999) Eur. Heart J. , vol.20 , pp. 51-57
    • Patel, D.J.1    Purcell, H.J.2    Fox, K.M.3
  • 10
    • 0029024314 scopus 로고
    • Cloning of the beta cell high-affinity sulfonylurea receptor: A regulator of insulin secretion
    • L. Aguilar-Bryan, and C.G. Nichols D.A. Nelson Cloning of the beta cell high-affinity sulfonylurea receptor: a regulator of insulin secretion Science 268 1995 423 426
    • (1995) Science , vol.268 , pp. 423-426
    • Aguilar-Bryan, L.1    Nichols, C.G.2    Nelson, D.A.3
  • 11
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • A.L. Davidson, and E. Dassa J. Chen Structure, function, and evolution of bacterial ATP-binding cassette systems Microbiol. Mol. Biol. Rev. 72 2008 317 364
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Chen, J.3
  • 12
    • 61449341855 scopus 로고    scopus 로고
    • Review. Structure and mechanism of ATP-binding cassette transporters
    • K.P. Locher Review. Structure and mechanism of ATP-binding cassette transporters Philos. Trans. R. Soc. Lond. B Biol. Sci. 364 2009 239 245
    • (2009) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.364 , pp. 239-245
    • Locher, K.P.1
  • 13
    • 84921032443 scopus 로고    scopus 로고
    • ABC transporters in adaptive immunity
    • F. Seyffer, and R. Tampé ABC transporters in adaptive immunity Biochim. Biophys. Acta 1850 2015 449 460
    • (2015) Biochim. Biophys. Acta , vol.1850 , pp. 449-460
    • Seyffer, F.1    Tampé, R.2
  • 15
    • 84858767204 scopus 로고    scopus 로고
    • Role of the D-loops in allosteric control of ATP hydrolysis in an ABC transporter
    • P.M. Jones, and A.M. George Role of the D-loops in allosteric control of ATP hydrolysis in an ABC transporter J. Phys. Chem. A 116 2012 3004 3013
    • (2012) J. Phys. Chem. A , vol.116 , pp. 3004-3013
    • Jones, P.M.1    George, A.M.2
  • 16
    • 0034601811 scopus 로고    scopus 로고
    • Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein
    • I.L. Urbatsch, and K. Gimi A.E. Senior Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein Biochemistry 39 2000 11921 11927
    • (2000) Biochemistry , vol.39 , pp. 11921-11927
    • Urbatsch, I.L.1    Gimi, K.2    Senior, A.E.3
  • 17
    • 0033601321 scopus 로고    scopus 로고
    • ATP binding properties of the nucleotide-binding folds of SUR1
    • M. Matsuo, and N. Kioka K. Ueda ATP binding properties of the nucleotide-binding folds of SUR1 J. Biol. Chem. 274 1999 37479 37482
    • (1999) J. Biol. Chem. , vol.274 , pp. 37479-37482
    • Matsuo, M.1    Kioka, N.2    Ueda, K.3
  • 18
    • 84861310612 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
    • M. Hohl, and C. Briand M.A. Seeger Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation Nat. Struct. Mol. Biol. 19 2012 395 402
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 395-402
    • Hohl, M.1    Briand, C.2    Seeger, M.A.3
  • 19
    • 84905040016 scopus 로고    scopus 로고
    • Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter
    • M. Hohl, and L.M. Hürlimann M.A. Seeger Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter Proc. Natl. Acad. Sci. USA 111 2014 11025 11030
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 11025-11030
    • Hohl, M.1    Hürlimann, L.M.2    Seeger, M.A.3
  • 20
    • 84900449189 scopus 로고    scopus 로고
    • Refined structures of mouse P-glycoprotein
    • J. Li, K.F. Jaimes, and S.G. Aller Refined structures of mouse P-glycoprotein Protein Sci. 23 2014 34 46
    • (2014) Protein Sci. , vol.23 , pp. 34-46
    • Li, J.1    Jaimes, K.F.2    Aller, S.G.3
  • 21
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • A. Ward, and C.L. Reyes G. Chang Flexibility in the ABC transporter MsbA: alternating access with a twist Proc. Natl. Acad. Sci. USA 104 2007 19005 19010
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Chang, G.3
  • 22
    • 57649183334 scopus 로고    scopus 로고
    • Functional clustering of mutations in the dimer interface of the nucleotide binding folds of the sulfonylurea receptor
    • R. Masia, and C.G. Nichols Functional clustering of mutations in the dimer interface of the nucleotide binding folds of the sulfonylurea receptor J. Biol. Chem. 283 2008 30322 30329
    • (2008) J. Biol. Chem. , vol.283 , pp. 30322-30329
    • Masia, R.1    Nichols, C.G.2
  • 23
    • 28644435891 scopus 로고    scopus 로고
    • 3-D structural and functional characterization of the purified KATP channel complex Kir6.2-SUR1
    • M.V. Mikhailov, and J.D. Campbell F.M. Ashcroft 3-D structural and functional characterization of the purified KATP channel complex Kir6.2-SUR1 EMBO J. 24 2005 4166 4175
    • (2005) EMBO J. , vol.24 , pp. 4166-4175
    • Mikhailov, M.V.1    Campbell, J.D.2    Ashcroft, F.M.3
  • 24
    • 0034666295 scopus 로고    scopus 로고
    • Different binding properties and affinities for ATP and ADP among sulfonylurea receptor subtypes, SUR1, SUR2A, and SUR2B
    • M. Matsuo, and K. Tanabe K. Ueda Different binding properties and affinities for ATP and ADP among sulfonylurea receptor subtypes, SUR1, SUR2A, and SUR2B J. Biol. Chem. 275 2000 28757 28763
    • (2000) J. Biol. Chem. , vol.275 , pp. 28757-28763
    • Matsuo, M.1    Tanabe, K.2    Ueda, K.3
  • 25
    • 0033816117 scopus 로고    scopus 로고
    • ATPase activity of the sulfonylurea receptor: A catalytic function for the KATP channel complex
    • M. Bienengraeber, and A.E. Alekseev A. Terzic ATPase activity of the sulfonylurea receptor: a catalytic function for the KATP channel complex FASEB J. 14 2000 1943 1952
    • (2000) FASEB J. , vol.14 , pp. 1943-1952
    • Bienengraeber, M.1    Alekseev, A.E.2    Terzic, A.3
  • 26
    • 19444377691 scopus 로고    scopus 로고
    • KATP channel interaction with adenine nucleotides
    • M. Matsuo, Y. Kimura, and K. Ueda KATP channel interaction with adenine nucleotides J. Mol. Cell. Cardiol. 38 2005 907 916
    • (2005) J. Mol. Cell. Cardiol. , vol.38 , pp. 907-916
    • Matsuo, M.1    Kimura, Y.2    Ueda, K.3
  • 27
    • 0036714915 scopus 로고    scopus 로고
    • Coupling between voltage sensor activation, Ca2+ binding and channel opening in large conductance (BK) potassium channels
    • F.T. Horrigan, and R.W. Aldrich Coupling between voltage sensor activation, Ca2+ binding and channel opening in large conductance (BK) potassium channels J. Gen. Physiol. 120 2002 267 305
    • (2002) J. Gen. Physiol. , vol.120 , pp. 267-305
    • Horrigan, F.T.1    Aldrich, R.W.2
  • 28
  • 29
    • 1942519357 scopus 로고    scopus 로고
    • Concerted gating mechanism underlying KATP channel inhibition by ATP
    • P. Drain, X. Geng, and L. Li Concerted gating mechanism underlying KATP channel inhibition by ATP Biophys. J. 86 2004 2101 2112
    • (2004) Biophys. J. , vol.86 , pp. 2101-2112
    • Drain, P.1    Geng, X.2    Li, L.3
  • 30
    • 13444274375 scopus 로고    scopus 로고
    • Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit
    • J.F. Antcliff, and S. Haider F.M. Ashcroft Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit EMBO J. 24 2005 229 239
    • (2005) EMBO J. , vol.24 , pp. 229-239
    • Antcliff, J.F.1    Haider, S.2    Ashcroft, F.M.3
  • 31
    • 0033624291 scopus 로고    scopus 로고
    • ATP4- mediates closure of pancreatic beta-cell ATP-sensitive potassium channels by interaction with 1 of 4 identical sites
    • E. Markworth, C. Schwanstecher, and M. Schwanstecher ATP4- mediates closure of pancreatic beta-cell ATP-sensitive potassium channels by interaction with 1 of 4 identical sites Diabetes 49 2000 1413 1418
    • (2000) Diabetes , vol.49 , pp. 1413-1418
    • Markworth, E.1    Schwanstecher, C.2    Schwanstecher, M.3
  • 32
    • 0242415358 scopus 로고    scopus 로고
    • Gating mechanism of KATP channels: Function fits form
    • D. Enkvetchakul, and C.G. Nichols Gating mechanism of KATP channels: function fits form J. Gen. Physiol. 122 2003 471 480
    • (2003) J. Gen. Physiol. , vol.122 , pp. 471-480
    • Enkvetchakul, D.1    Nichols, C.G.2
  • 33
    • 77957838073 scopus 로고    scopus 로고
    • Activation of the K(ATP) channel by Mg-nucleotide interaction with SUR1
    • P. Proks, H. de Wet, and F.M. Ashcroft Activation of the K(ATP) channel by Mg-nucleotide interaction with SUR1 J. Gen. Physiol. 136 2010 389 405
    • (2010) J. Gen. Physiol. , vol.136 , pp. 389-405
    • Proks, P.1    De Wet, H.2    Ashcroft, F.M.3
  • 34
    • 0030907755 scopus 로고    scopus 로고
    • The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide
    • F.M. Gribble, S.J. Tucker, and F.M. Ashcroft The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide EMBO J. 16 1997 1145 1152
    • (1997) EMBO J. , vol.16 , pp. 1145-1152
    • Gribble, F.M.1    Tucker, S.J.2    Ashcroft, F.M.3
  • 35
    • 0032505868 scopus 로고    scopus 로고
    • KATP channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit
    • P. Drain, L. Li, and J. Wang KATP channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit Proc. Natl. Acad. Sci. USA 95 1998 13953 13958
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13953-13958
    • Drain, P.1    Li, L.2    Wang, J.3
  • 36
    • 33847025257 scopus 로고    scopus 로고
    • An ATP-binding mutation (G334D) in KCNJ11 is associated with a sulfonylurea-insensitive form of developmental delay, epilepsy, and neonatal diabetes
    • R. Masia, and J.C. Koster F. Barbetti An ATP-binding mutation (G334D) in KCNJ11 is associated with a sulfonylurea-insensitive form of developmental delay, epilepsy, and neonatal diabetes Diabetes 56 2007 328 336
    • (2007) Diabetes , vol.56 , pp. 328-336
    • Masia, R.1    Koster, J.C.2    Barbetti, F.3
  • 37
    • 47249111325 scopus 로고    scopus 로고
    • Three C-terminal residues from the sulphonylurea receptor contribute to the functional coupling between the K(ATP) channel subunits SUR2A and Kir6.2
    • J.P. Dupuis, and J. Revilloud M. Vivaudou Three C-terminal residues from the sulphonylurea receptor contribute to the functional coupling between the K(ATP) channel subunits SUR2A and Kir6.2 J. Physiol. 586 2008 3075 3085
    • (2008) J. Physiol. , vol.586 , pp. 3075-3085
    • Dupuis, J.P.1    Revilloud, J.2    Vivaudou, M.3
  • 38
    • 0026649107 scopus 로고
    • Two sites for adenine-nucleotide regulation of ATP-sensitive potassium channels in mouse pancreatic beta-cells and HIT cells
    • W.F. Hopkins, and S. Fatherazi D.L. Cook Two sites for adenine-nucleotide regulation of ATP-sensitive potassium channels in mouse pancreatic beta-cells and HIT cells J. Membr. Biol. 129 1992 287 295
    • (1992) J. Membr. Biol. , vol.129 , pp. 287-295
    • Hopkins, W.F.1    Fatherazi, S.2    Cook, D.L.3
  • 39
    • 84909602192 scopus 로고    scopus 로고
    • Sulfonylureas suppress the stimulatory action of Mg-nucleotides on Kir6.2/SUR1 but not Kir6.2/SUR2A KATP channels: A mechanistic study
    • P. Proks, H. de Wet, and F.M. Ashcroft Sulfonylureas suppress the stimulatory action of Mg-nucleotides on Kir6.2/SUR1 but not Kir6.2/SUR2A KATP channels: a mechanistic study J. Gen. Physiol. 144 2014 469 486
    • (2014) J. Gen. Physiol. , vol.144 , pp. 469-486
    • Proks, P.1    De Wet, H.2    Ashcroft, F.M.3
  • 40
    • 43549101085 scopus 로고    scopus 로고
    • A novel ABCC8 (SUR1)-dependent mechanism of metabolism-excitation uncoupling
    • A.P. Babenko A novel ABCC8 (SUR1)-dependent mechanism of metabolism-excitation uncoupling J. Biol. Chem. 283 2008 8778 8782
    • (2008) J. Biol. Chem. , vol.283 , pp. 8778-8782
    • Babenko, A.P.1
  • 41
    • 84893581896 scopus 로고    scopus 로고
    • The unusual stoichiometry of ADP activation of the KATP channel
    • E. Hosy, and M. Vivaudou The unusual stoichiometry of ADP activation of the KATP channel Front. Physiol. 5 2014 11
    • (2014) Front. Physiol. , vol.5 , pp. 11
    • Hosy, E.1    Vivaudou, M.2
  • 42
    • 22744438517 scopus 로고    scopus 로고
    • Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions
    • P. Tammaro, and C. Girard F.M. Ashcroft Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions EMBO J. 24 2005 2318 2330
    • (2005) EMBO J. , vol.24 , pp. 2318-2330
    • Tammaro, P.1    Girard, C.2    Ashcroft, F.M.3
  • 43
    • 0035797455 scopus 로고    scopus 로고
    • Signaling in channel/enzyme multimers: ATPase transitions in sur module gate ATP-sensitive K+ conductance
    • L.V. Zingman, and A.E. Alekseev A. Terzic Signaling in channel/enzyme multimers: ATPase transitions in SUR module gate ATP-sensitive K+ conductance Neuron 31 2001 233 245
    • (2001) Neuron , vol.31 , pp. 233-245
    • Zingman, L.V.1    Alekseev, A.E.2    Terzic, A.3
  • 44
    • 0037134527 scopus 로고    scopus 로고
    • Tandem function of nucleotide binding domains confers competence to sulfonylurea receptor in gating ATP-sensitive K+ channels
    • L.V. Zingman, and D.M. Hodgson A. Terzic Tandem function of nucleotide binding domains confers competence to sulfonylurea receptor in gating ATP-sensitive K+ channels J. Biol. Chem. 277 2002 14206 14210
    • (2002) J. Biol. Chem. , vol.277 , pp. 14206-14210
    • Zingman, L.V.1    Hodgson, D.M.2    Terzic, A.3
  • 45
    • 75749153312 scopus 로고    scopus 로고
    • Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations
    • L. Csanády, P. Vergani, and D.C. Gadsby Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations Proc. Natl. Acad. Sci. USA 107 2010 1241 1246
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1241-1246
    • Csanády, L.1    Vergani, P.2    Gadsby, D.C.3
  • 46
    • 0141513675 scopus 로고    scopus 로고
    • Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating
    • C. Basso, and P. Vergani D.C. Gadsby Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating J. Gen. Physiol. 122 2003 333 348
    • (2003) J. Gen. Physiol. , vol.122 , pp. 333-348
    • Basso, C.1    Vergani, P.2    Gadsby, D.C.3
  • 47
    • 77951706563 scopus 로고    scopus 로고
    • Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel
    • M.F. Tsai, M. Li, and T.C. Hwang Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel J. Gen. Physiol. 135 2010 399 414
    • (2010) J. Gen. Physiol. , vol.135 , pp. 399-414
    • Tsai, M.F.1    Li, M.2    Hwang, T.C.3
  • 48
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • P. Vergani, and S.W. Lockless D.C. Gadsby CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains Nature 433 2005 876 880
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Gadsby, D.C.3
  • 49
    • 0030611865 scopus 로고    scopus 로고
    • MgADP antagonism to Mg2+-independent ATP binding of the sulfonylurea receptor SUR1
    • K. Ueda, N. Inagaki, and S. Seino MgADP antagonism to Mg2+-independent ATP binding of the sulfonylurea receptor SUR1 J. Biol. Chem. 272 1997 22983 22986
    • (1997) J. Biol. Chem. , vol.272 , pp. 22983-22986
    • Ueda, K.1    Inagaki, N.2    Seino, S.3
  • 50
    • 23644434998 scopus 로고    scopus 로고
    • Differential nucleotide regulation of KATP channels by SUR1 and SUR2A
    • R. Masia, D. Enkvetchakul, and C.G. Nichols Differential nucleotide regulation of KATP channels by SUR1 and SUR2A J. Mol. Cell. Cardiol. 39 2005 491 501
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , pp. 491-501
    • Masia, R.1    Enkvetchakul, D.2    Nichols, C.G.3
  • 51
    • 0034634289 scopus 로고    scopus 로고
    • C-terminal tails of sulfonylurea receptors control ADP-induced activation and diazoxide modulation of ATP-sensitive K(+) channels
    • T. Matsuoka, and K. Matsushita Y. Kurachi C-terminal tails of sulfonylurea receptors control ADP-induced activation and diazoxide modulation of ATP-sensitive K(+) channels Circ. Res. 87 2000 873 880
    • (2000) Circ. Res. , vol.87 , pp. 873-880
    • Matsuoka, T.1    Matsushita, K.2    Kurachi, Y.3
  • 52
    • 0033664249 scopus 로고    scopus 로고
    • Differential response of K(ATP) channels containing SUR2A or SUR2B subunits to nucleotides and pinacidil
    • F. Reimann, F.M. Gribble, and F.M. Ashcroft Differential response of K(ATP) channels containing SUR2A or SUR2B subunits to nucleotides and pinacidil Mol. Pharmacol. 58 2000 1318 1325
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1318-1325
    • Reimann, F.1    Gribble, F.M.2    Ashcroft, F.M.3
  • 53
    • 34447306630 scopus 로고    scopus 로고
    • Studies of the ATPase activity of the ABC protein SUR1
    • H. de Wet, and M.V. Mikhailov F.M. Ashcroft Studies of the ATPase activity of the ABC protein SUR1 FEBS J. 274 2007 3532 3544
    • (2007) FEBS J. , vol.274 , pp. 3532-3544
    • De Wet, H.1    Mikhailov, M.V.2    Ashcroft, F.M.3
  • 54
    • 53049105327 scopus 로고    scopus 로고
    • Regulation of KATP channel expression and activity by the SUR1 nucleotide binding fold 1
    • R. Masia, G. Caputa, and C.G. Nichols Regulation of KATP channel expression and activity by the SUR1 nucleotide binding fold 1 Channels (Austin) 1 2007 315 323
    • (2007) Channels (Austin) , vol.1 , pp. 315-323
    • Masia, R.1    Caputa, G.2    Nichols, C.G.3
  • 55
    • 77953189433 scopus 로고    scopus 로고
    • The ATPase activities of sulfonylurea receptor 2A and sulfonylurea receptor 2B are influenced by the C-terminal 42 amino acids
    • H. de Wet, and C. Fotinou F.M. Ashcroft The ATPase activities of sulfonylurea receptor 2A and sulfonylurea receptor 2B are influenced by the C-terminal 42 amino acids FEBS J. 277 2010 2654 2662
    • (2010) FEBS J. , vol.277 , pp. 2654-2662
    • De Wet, H.1    Fotinou, C.2    Ashcroft, F.M.3
  • 56
    • 84879577910 scopus 로고    scopus 로고
    • Reinterpreting the action of ATP analogs on K(ATP) channels
    • D. Ortiz, and L. Gossack J. Bryan Reinterpreting the action of ATP analogs on K(ATP) channels J. Biol. Chem. 288 2013 18894 18902
    • (2013) J. Biol. Chem. , vol.288 , pp. 18894-18902
    • Ortiz, D.1    Gossack, L.2    Bryan, J.3
  • 57
    • 84861538639 scopus 로고    scopus 로고
    • Two neonatal diabetes mutations on transmembrane helix 15 of SUR1 increase affinity for ATP and ADP at nucleotide binding domain 2
    • D. Ortiz, and P. Voyvodic J. Bryan Two neonatal diabetes mutations on transmembrane helix 15 of SUR1 increase affinity for ATP and ADP at nucleotide binding domain 2 J. Biol. Chem. 287 2012 17985 17995
    • (2012) J. Biol. Chem. , vol.287 , pp. 17985-17995
    • Ortiz, D.1    Voyvodic, P.2    Bryan, J.3
  • 58
    • 0037113899 scopus 로고    scopus 로고
    • SUR-dependent modulation of KATP channels by an N-terminal KIR6.2 peptide. Defining intersubunit gating interactions
    • A.P. Babenko, and J. Bryan SUR-dependent modulation of KATP channels by an N-terminal KIR6.2 peptide. Defining intersubunit gating interactions J. Biol. Chem. 277 2002 43997 44004
    • (2002) J. Biol. Chem. , vol.277 , pp. 43997-44004
    • Babenko, A.P.1    Bryan, J.2
  • 59
    • 0042025073 scopus 로고    scopus 로고
    • N-terminal transmembrane domain of the sur controls trafficking and gating of Kir6 channel subunits
    • K.W. Chan, H. Zhang, and D.E. Logothetis N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits EMBO J. 22 2003 3833 3843
    • (2003) EMBO J. , vol.22 , pp. 3833-3843
    • Chan, K.W.1    Zhang, H.2    Logothetis, D.E.3
  • 60
    • 84915748092 scopus 로고    scopus 로고
    • Sulfonylurea receptors regulate the channel pore in ATP-sensitive potassium channels via an intersubunit salt bridge
    • D. Lodwick, and R.D. Rainbow R.I. Norman Sulfonylurea receptors regulate the channel pore in ATP-sensitive potassium channels via an intersubunit salt bridge Biochem. J. 464 2014 343 354
    • (2014) Biochem. J. , vol.464 , pp. 343-354
    • Lodwick, D.1    Rainbow, R.D.2    Norman, R.I.3
  • 61
    • 84866172544 scopus 로고    scopus 로고
    • Engineered interaction between SUR1 and Kir6.2 that enhances ATP sensitivity in KATP channels
    • E.B. Pratt, and Q. Zhou S.L. Shyng Engineered interaction between SUR1 and Kir6.2 that enhances ATP sensitivity in KATP channels J. Gen. Physiol. 140 2012 175 187
    • (2012) J. Gen. Physiol. , vol.140 , pp. 175-187
    • Pratt, E.B.1    Zhou, Q.2    Shyng, S.L.3
  • 62
    • 11144356128 scopus 로고    scopus 로고
    • Proximal C-terminal domain of sulphonylurea receptor 2A interacts with pore-forming Kir6 subunits in KATP channels
    • R.D. Rainbow, and M. James R.I. Norman Proximal C-terminal domain of sulphonylurea receptor 2A interacts with pore-forming Kir6 subunits in KATP channels Biochem. J. 379 2004 173 181
    • (2004) Biochem. J. , vol.379 , pp. 173-181
    • Rainbow, R.D.1    James, M.2    Norman, R.I.3
  • 63
    • 0344466801 scopus 로고    scopus 로고
    • Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor
    • F. Reimann, and S.J. Tucker F.M. Ashcroft Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor J. Physiol. 518 1999 325 336
    • (1999) J. Physiol. , vol.518 , pp. 325-336
    • Reimann, F.1    Tucker, S.J.2    Ashcroft, F.M.3
  • 64
    • 84903478669 scopus 로고    scopus 로고
    • Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state
    • H.G. Choudhury, and Z. Tong K. Beis Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state Proc. Natl. Acad. Sci. USA 111 2014 9145 9150
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 9145-9150
    • Choudhury, H.G.1    Tong, Z.2    Beis, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.