메뉴 건너뛰기




Volumn 155, Issue 3, 2014, Pages 147-158

AMPK-sensitive cellular transport

Author keywords

AMPK; carrier; cellular transport; energy homeostasis; ion channel; pump

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE SENSITIVE POTASSIUM CHANNEL; CASPASE 2; CREATINE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; GAP JUNCTION PROTEIN; GLUCOSE TRANSPORTER; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; MONOCARBOXYLATE TRANSPORTER; POTASSIUM CHANNEL; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SHAB POTASSIUM CHANNEL; SODIUM CALCIUM EXCHANGE PROTEIN; SODIUM CHANNEL NAV1.5; SODIUM PROTON EXCHANGE PROTEIN; UBIQUITIN PROTEIN LIGASE NEDD4;

EID: 84896796936     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvu002     Document Type: Review
Times cited : (37)

References (91)
  • 1
    • 84876320551 scopus 로고    scopus 로고
    • LKB1 and AMPK and the cancer-metabolism link-ten years after
    • Hardie, D.G. and Alessi, D.R. (2013) LKB1 and AMPK and the cancer-metabolism link-ten years after. BMC. Biol. 11, 36
    • (2013) BMC. Biol. , vol.11 , pp. 36
    • Hardie, D.G.1    Alessi, D.R.2
  • 2
    • 84866753209 scopus 로고    scopus 로고
    • Regulation of Orai1/STIM1 by the kinases SGK1 and AMPK
    • Lang, F., Eylenstein, A., and Shumilina, E. (2012) Regulation of Orai1/STIM1 by the kinases SGK1 and AMPK. Cell Calcium 52, 347-354
    • (2012) Cell Calcium , vol.52 , pp. 347-354
    • Lang, F.1    Eylenstein, A.2    Shumilina, E.3
  • 3
    • 84863763440 scopus 로고    scopus 로고
    • AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress
    • Jeon, S.M., Chandel, N.S., and Hay, N. (2012) AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress. Nature 485, 661-665
    • (2012) Nature , vol.485 , pp. 661-665
    • Jeon, S.M.1    Chandel, N.S.2    Hay, N.3
  • 4
    • 57849090443 scopus 로고    scopus 로고
    • The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor
    • McBride, A., Ghilagaber, S., Nikolaev, A., and Hardie, D. G. (2009) The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor. Cell Metab. 9, 23-34
    • (2009) Cell Metab. , vol.9 , pp. 23-34
    • McBride, A.1    Ghilagaber, S.2    Nikolaev, A.3    Hardie, D.G.4
  • 5
    • 40749116561 scopus 로고    scopus 로고
    • Metformin inhibits hepatic gluconeogenesis through AMP-activated protein kinase-dependent regulation of the orphan nuclear receptor SH
    • Kim, Y.D., Park, K.G., Lee, Y.S., Park, Y.Y., Kim, D.K., Nedumaran, B., Jang, W.G., Cho, W.J., Ha, J., Lee, I.K., Lee, C.H., and Choi, H.S. (2008) Metformin inhibits hepatic gluconeogenesis through AMP-activated protein kinase-dependent regulation of the orphan nuclear receptor SHP. Diabetes 57, 306-314
    • (2008) Diabetes , vol.57 , pp. 306-314
    • Kim, Y.D.1    Park, K.G.2    Lee, Y.S.3    Park, Y.Y.4    Kim, D.K.5    Nedumaran, B.6    Jang, W.G.7    Cho, W.J.8    Ha, J.9    Lee, I.K.10    Lee, C.H.11    Choi, H.S.12
  • 6
    • 70449715072 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase (AMPK) inhibits fatty acid synthesis in bovine mammary epithelial cells
    • McFadden, J.W. and Corl, B.A. (2009) Activation of AMP-activated protein kinase (AMPK) inhibits fatty acid synthesis in bovine mammary epithelial cells. Biochem. Biophys. Res. Commun. 390, 388-393
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 388-393
    • McFadden, J.W.1    Corl, B.A.2
  • 7
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An energy sensor that regulates all aspects of cell function
    • Hardie, D.G. (2011) AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. Genes Dev. 25, 1895-1908
    • (2011) Genes Dev. , vol.25 , pp. 1895-1908
    • Hardie, D.G.1
  • 8
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
    • DOI 10.1074/jbc.271.44.27879
    • Hawley, S.A., Davison, M., Woods, A., Davies, S.P., Beri, R.K., Carling, D., and Hardie, D.G. (1996) Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J. Biol. Chem. 271, 27879-27887 (Pubitemid 26367365)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 9
    • 0043210478 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis
    • DOI 10.1074/jbc.M303946200
    • Woods, A., Vertommen, D., Neumann, D., Turk, R., Bayliss, J., Schlattner, U., Wallimann, T., Carling, D., and Rider, M.H. (2003) Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by sitedirected mutagenesis. J. Biol. Chem. 278, 28434-28442 (Pubitemid 36935745)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28434-28442
    • Woods, A.1    Vertommen, D.2    Neumann, D.3    Turk, R.4    Bayliss, J.5    Schlattner, U.6    Wallimannll, T.7    Carling, D.8    Rider, M.H.9
  • 11
    • 70349896067 scopus 로고    scopus 로고
    • Association of AMP-activated protein kinase subunits with glycogen particles as revealed in situ by immunoelectron microscopy
    • Bendayan, M., Londono, I., Kemp, B.E., Hardie, G.D., Ruderman, N., and Prentki, M. (2009) Association of AMP-activated protein kinase subunits with glycogen particles as revealed in situ by immunoelectron microscopy. J. Histochem. Cytochem. 57, 963-971
    • (2009) J. Histochem. Cytochem. , vol.57 , pp. 963-971
    • Bendayan, M.1    Londono, I.2    Kemp, B.E.3    Hardie, G.D.4    Ruderman, N.5    Prentki, M.6
  • 13
    • 34147152841 scopus 로고    scopus 로고
    • Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    • DOI 10.1042/BJ20061520
    • Sanders, M.J., Grondin, P.O., Hegarty, B.D., Snowden, M.A., and Carling, D. (2007) Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade. Biochem. J. 403, 139-148 (Pubitemid 46569875)
    • (2007) Biochemical Journal , vol.403 , Issue.1 , pp. 139-148
    • Sanders, M.J.1    Grondin, P.O.2    Hegarty, B.D.3    Snowden, M.A.4    Carling, D.5
  • 14
    • 23844471263 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases
    • DOI 10.1074/jbc.M503824200
    • Hurley, R.L., Anderson, K.A., Franzone, J.M., Kemp, B.E., Means, A.R., and Witters, L.A. (2005) The Ca2\+/calmodulin-dependent protein kinase kinases are AMPactivated protein kinase kinases. J. Biol. Chem. 280, 29060-29066 (Pubitemid 41161355)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.32 , pp. 29060-29066
    • Hurley, R.L.1    Anderson, K.A.2    Franzone, J.M.3    Kemp, B.E.4    Means, A.R.5    Witters, L.A.6
  • 15
  • 18
    • 77950195325 scopus 로고    scopus 로고
    • Regulation of Na\+-coupled glucose carrier SGLT1 by AMP-activated protein kinase
    • Sopjani, M., Bhavsar, S.K., Fraser, S., Kemp, B.E., Foller, M., and Lang, F. (2010) Regulation of Na\+-coupled glucose carrier SGLT1 by AMP-activated protein kinase. Mol. Membr. Biol. 27, 137-144
    • (2010) Mol. Membr. Biol. , vol.27 , pp. 137-144
    • Sopjani, M.1    Bhavsar, S.K.2    Fraser, S.3    Kemp, B.E.4    Foller, M.5    Lang, F.6
  • 22
    • 0036535031 scopus 로고    scopus 로고
    • Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells
    • DOI 10.1042/0264-6021:3630167
    • Fryer, L.G., Foufelle, F., Barnes, K., Baldwin, S.A., Woods, A., and Carling, D. (2002) Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells. Biochem. J. 363, 167-174 (Pubitemid 34280623)
    • (2002) Biochemical Journal , vol.363 , Issue.1 , pp. 167-174
    • Fryer, L.G.D.1    Foufelle, F.2    Barnes, K.3    Baldwin, S.A.4    Woods, A.5    Carling, D.6
  • 24
    • 84859811001 scopus 로고    scopus 로고
    • Effect of the AMP-kinase modulators AICAR, metformin and compound C on insulin secretion of INS-1E rat insulinoma cells under standard cell culture conditions
    • Langelueddecke, C., Jakab, M., Ketterl, N., Lehner, L., Hufnagl, C., Schmidt, S., Geibel, J.P., Fuerst, J., and Ritter, M. (2012) Effect of the AMP-kinase modulators AICAR, metformin and compound C on insulin secretion of INS-1E rat insulinoma cells under standard cell culture conditions. Cell Physiol. Biochem. 29, 75-86
    • (2012) Cell Physiol. Biochem. , vol.29 , pp. 75-86
    • Langelueddecke, C.1    Jakab, M.2    Ketterl, N.3    Lehner, L.4    Hufnagl, C.5    Schmidt, S.6    Geibel, J.P.7    Fuerst, J.8    Ritter, M.9
  • 28
    • 84886401116 scopus 로고    scopus 로고
    • Possible involvement of AMPK in acute exercise-induced expression of monocarboxylate transporters MCT1 and MCT4 mRNA in fast-twitch skeletal muscle
    • Takimoto, M., Takeyama, M., and Hamada, T. (2013) Possible involvement of AMPK in acute exercise-induced expression of monocarboxylate transporters MCT1 and MCT4 mRNA in fast-twitch skeletal muscle. Metabolism 62, 1633-1640
    • (2013) Metabolism , vol.62 , pp. 1633-1640
    • Takimoto, M.1    Takeyama, M.2    Hamada, T.3
  • 29
    • 0037163076 scopus 로고    scopus 로고
    • The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase
    • DOI 10.1074/jbc.M205213200
    • Marsin, A.S., Bouzin, C., Bertrand, L., and Hue, L. (2002) The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase. J. Biol. Chem. 277, 30778-30783 (Pubitemid 34970775)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 30778-30783
    • Marsin, A.-S.1    Bouzin, C.2    Bertrand, L.3    Hue, L.4
  • 31
    • 50949087166 scopus 로고    scopus 로고
    • Malonyl-CoA, a key signaling molecule in mammalian cells
    • Saggerson, D. (2008) Malonyl-CoA, a key signaling molecule in mammalian cells. Annu. Rev. Nutr. 28, 253-272
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 253-272
    • Saggerson, D.1
  • 33
    • 0037461107 scopus 로고    scopus 로고
    • Constitutively active adenosine monophosphate-activated protein kinase regulates voltage-gated sodium channels in ventricular myocytes
    • DOI 10.1161/01.CIR.0000069269.60167.02
    • Light, P.E., Wallace, C.H., and Dyck, J.R. (2003) Constitutively active adenosine monophosphate-activated protein kinase regulates voltage-gated sodium channels in ventricular myocytes. Circulation 107, 1962-1965 (Pubitemid 36506067)
    • (2003) Circulation , vol.107 , Issue.15 , pp. 1962-1965
    • Light, P.E.1    Wallace, C.H.R.2    Dyck, J.R.B.3
  • 34
    • 67349132843 scopus 로고    scopus 로고
    • Serine-385 phosphorylation of inwardly rectifying K\+ channel subunit (Kir6.2) by AMP-dependent protein kinase plays a key role in rosiglitazone-induced closure of the K(ATP) channel and insulin secretion in rats
    • Chang, T.J., Chen, W.P., Yang, C., Lu, P.H., Liang, Y.C., Su, M.J., Lee, S.C., and Chuang, L.M. (2009) Serine-385 phosphorylation of inwardly rectifying K\+ channel subunit (Kir6.2) by AMP-dependent protein kinase plays a key role in rosiglitazone-induced closure of the K(ATP) channel and insulin secretion in rats. Diabetologia 52, 1112-1121
    • (2009) Diabetologia , vol.52 , pp. 1112-1121
    • Chang, T.J.1    Chen, W.P.2    Yang, C.3    Lu, P.H.4    Liang, Y.C.5    Su, M.J.6    Lee, S.C.7    Chuang, L.M.8
  • 35
    • 73249149131 scopus 로고    scopus 로고
    • Glucose deprivation regulates KATP channel trafficking via AMP-activated protein kinase in pancreatic beta-cells
    • Lim, A., Park, S.H., Sohn, J.W., Jeon, J.H., Park, J.H., Song, D.K., Lee, S.H., and Ho, W.K. (2009) Glucose deprivation regulates KATP channel trafficking via AMP-activated protein kinase in pancreatic beta-cells. Diabetes 58, 2813-2819
    • (2009) Diabetes , vol.58 , pp. 2813-2819
    • Lim, A.1    Park, S.H.2    Sohn, J.W.3    Jeon, J.H.4    Park, J.H.5    Song, D.K.6    Lee, S.H.7    Ho, W.K.8
  • 37
    • 6944251212 scopus 로고    scopus 로고
    • ATP channels
    • DOI 10.1096/fj.04-1602fje
    • Budas, G.R., Jovanovic, S., Crawford, R.M., and Jovanovic, A. (2004) Hypoxia-induced preconditioning in adult stimulated cardiomyocytes is mediated by the opening and trafficking of sarcolemmal KATP channels. FASEB J. 18, 1046-1048 (Pubitemid 39561520)
    • (2004) FASEB Journal , vol.18 , Issue.9 , pp. 1046-1048
    • Budas, G.R.1    Jovanovic, S.2    Crawford, R.M.3    Jovanovic, A.4
  • 38
    • 0030015194 scopus 로고    scopus 로고
    • Characterization of 5'AMP-activated protein kinase activity in the heart and its role in inhibiting acetyl-CoA carboxylase during reperfusion following ischemia
    • DOI 10.1016/0005-2760(96)00013-6
    • Kudo, N., Gillespie, J.G., Kung, L., Witters, L.A., Schulz, R., Clanachan, A.S., and Lopaschuk, G.D. (1996) Characterization of 5'AMP-activated protein kinase activity in the heart and its role in inhibiting acetyl-CoA carboxylase during reperfusion following ischemia. Biochim. Biophys. Acta 1301, 67-75 (Pubitemid 26193063)
    • (1996) Biochimica et Biophysica Acta - Lipids and Lipid Metabolism , vol.1301 , Issue.1-2 , pp. 67-75
    • Kudo, N.1    Gillespie, J.G.2    Kung, L.3    Witters, L.A.4    Schulz, R.5    Clanachan, A.S.6    Lopaschuk, G.D.7
  • 39
    • 17044377065 scopus 로고    scopus 로고
    • 5-amino-imidazole carboxamide riboside acutely potentiates glucose-stimulated insulin secretion from mouse pancreatic islets by KATP channel-dependent and-independent pathways
    • Wang, C.Z., Wang, Y., Di, A., Magnuson, M.A., Ye, H., Roe, M.W., Nelson, D.J., Bell, G.I., and Philipson, L.H. (2005) 5-amino-imidazole carboxamide riboside acutely potentiates glucose-stimulated insulin secretion from mouse pancreatic islets by KATP channel-dependent and-independent pathways. Biochem. Biophys. Res. Commun. 330, 1073-1079
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 1073-1079
    • Wang, C.Z.1    Wang Di Y, A.2    Magnuson, M.A.3    Ye, H.4    Roe, M.W.5    Nelson, D.J.6    Bell, G.I.7    Philipson, L.H.8
  • 43
    • 84863211075 scopus 로고    scopus 로고
    • Enhanced Ca(2)(\+) entry and Na\+/Ca(2)(\+) exchanger activity in dendritic cells from AMP-activated protein kinase-deficient mice
    • Nurbaeva, M. K., Schmid, E., Szteyn, K., Yang, W., Viollet, B., Shumilina, E., and Lang, F. (2012) Enhanced Ca(2)(\+) entry and Na\+/Ca(2)(\+) exchanger activity in dendritic cells from AMP-activated protein kinase-deficient mice. FASEB J. 26, 3049-3058
    • (2012) FASEB J. , vol.26 , pp. 3049-3058
    • Nurbaeva, M.K.1    Schmid, E.2    Szteyn, K.3    Yang, W.4    Viollet, B.5    Shumilina, E.6    Lang, F.7
  • 50
    • 83255185042 scopus 로고    scopus 로고
    • AMP-activated protein kinase downregulates Kv7.1 cell surface expression
    • Andersen, M.N., Krzystanek, K., Jespersen, T., Olesen, S.P., and Rasmussen, H.B. (2012) AMP-activated protein kinase downregulates Kv7.1 cell surface expression. Traffic 13, 143-156
    • (2012) Traffic , vol.13 , pp. 143-156
    • Andersen, M.N.1    Krzystanek, K.2    Jespersen, T.3    Olesen, S.P.4    Rasmussen, H.B.5
  • 55
    • 77953105547 scopus 로고    scopus 로고
    • Downregulation of Na\+-coupled glutamate transporter EAAT3 and EAAT4 by AMP-activated protein kinase
    • Sopjani, M., Alesutan, I., Dermaku-Sopjani, M., Fraser, S., Kemp, B.E., Foller, M., and Lang, F. (2010) Downregulation of Na\+-coupled glutamate transporter EAAT3 and EAAT4 by AMP-activated protein kinase. J. Neurochem. 113, 1426-1435
    • (2010) J. Neurochem. , vol.113 , pp. 1426-1435
    • Sopjani, M.1    Alesutan, I.2    Dermaku-Sopjani, M.3    Fraser, S.4    Kemp, B.E.5    Foller, M.6    Lang, F.7
  • 57
    • 72549116753 scopus 로고    scopus 로고
    • AMP-activated protein kinase inhibits TREK channels
    • Kreneisz, O., Benoit, J.P., Bayliss, D.A., and Mulkey, D.K. (2009) AMP-activated protein kinase inhibits TREK channels. J. Physiol. 587, 5819-5830
    • (2009) J. Physiol. , vol.587 , pp. 5819-5830
    • Kreneisz, O.1    Benoit, J.P.2    Bayliss, D.A.3    Mulkey, D.K.4
  • 62
    • 0033933777 scopus 로고    scopus 로고
    • Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase
    • Hallows, K.R., Raghuram, V., Kemp, B.E., Witters, L.A., and Foskett, J.K. (2000) Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase. J. Clin. Invest. 105, 1711-1721 (Pubitemid 30421752)
    • (2000) Journal of Clinical Investigation , vol.105 , Issue.12 , pp. 1711-1721
    • Hallows, K.R.1    Raghuram, V.2    Kemp, B.E.3    Witters, L.A.4    Foskett, J.K.5
  • 64
    • 33645231670 scopus 로고    scopus 로고
    • Up-regulation of AMP-activated kinase by dysfunctional cystic fibrosis transmembrane conductance regulator in cystic fibrosis airway epithelial cells mitigates excessive inflammation
    • DOI 10.1074/jbc.M511029200
    • Hallows, K.R., Fitch, A.C., Richardson, C.A., Reynolds, P.R., Clancy, J.P., Dagher, P.C., Witters, L.A., Kolls, J.K., and Pilewski, J.M. (2006) Up-regulation of AMPactivated kinase by dysfunctional cystic fibrosis transmembrane conductance regulator in cystic fibrosis airway epithelial cells mitigates excessive inflammation. J. Biol. Chem. 281, 4231-4241 (Pubitemid 43847852)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 4231-4241
    • Hallows, K.R.1    Fitch, A.C.2    Richardson, C.A.3    Reynolds, P.R.4    Clancy, J.P.5    Dagher, P.C.6    Witters, L.A.7    Kolls, J.K.8    Pilewski, J.M.9
  • 65
    • 0029898733 scopus 로고    scopus 로고
    • Acidification of the male reproductive tract by a proton pumping (H\+)-ATPase
    • Breton, S., Smith, P.J., Lui, B., and Brown, D. (1996) Acidification of the male reproductive tract by a proton pumping (H\+)-ATPase. Nat. Med. 2, 470-472
    • (1996) Nat. Med. , vol.2 , pp. 470-472
    • Breton, S.1    Smith, P.J.2    Lui, B.3    Brown, D.4
  • 68
    • 0030945484 scopus 로고    scopus 로고
    • Epithelial sodium channels: Function, structure and regulation
    • Garty, H. and Palmer, L.G. (1997) Epithelial sodium channels: function, structure, and regulation. Physiol Rev. 77, 359-396 (Pubitemid 27184343)
    • (1997) Physiological Reviews , vol.77 , Issue.2 , pp. 359-396
    • Garty, H.1    Palmer, L.G.2
  • 72
    • 0033910376 scopus 로고    scopus 로고
    • The Long QT Syndromes: Genetic basis and clinical implications
    • DOI 10.1016/S0735-1097(00)00716-6, PII S0735109700007166
    • Chiang, C.E. and Roden, D.M. (2000) The long QT syndromes: genetic basis and clinical implications. J. Am. Coll. Cardiol. 36, 1-12 (Pubitemid 30466104)
    • (2000) Journal of the American College of Cardiology , vol.36 , Issue.1 , pp. 1-12
    • Chiang, C.-E.1    Roden, D.M.2
  • 73
    • 0030799943 scopus 로고    scopus 로고
    • + channel mutations in Romano-Ward and Jervell and Lange-Nielsen inherited cardiac arrhythmias
    • DOI 10.1093/emboj/16.17.5472
    • Chouabe, C., Neyroud, N., Guicheney, P., Lazdunski, M., Romey, G., and Barhanin, J. (1997) Properties of KvLQT1 K\+ channel mutations in Romano-Ward and Jervell and Lange-Nielsen inherited cardiac arrhythmias. EMBO J. 16, 5472-5479 (Pubitemid 27380154)
    • (1997) EMBO Journal , vol.16 , Issue.17 , pp. 5472-5479
    • Chouabe, C.1    Neyroud, N.2    Guicheney, P.3    Lazdunski, M.4    Romey, G.5    Barhanin, J.6
  • 77
    • 34247163179 scopus 로고    scopus 로고
    • + conduction pathway
    • DOI 10.1074/jbc.M608776200
    • Ma, D., Tang, X.D., Rogers, T.B., and Welling, P.A. (2007) An andersen-Tawil syndrome mutation in Kir2.1 (V302M) alters the G-loop cytoplasmic K\+ conduction pathway. J. Biol. Chem. 282, 5781-5789 (Pubitemid 47093767)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5781-5789
    • Ma, D.1    Tang, X.D.2    Rogers, T.B.3    Welling, P.A.4
  • 79
    • 33749500123 scopus 로고    scopus 로고
    • (Patho)physiological significance of the serum- and glucocorticoid- inducible kinase isoforms
    • DOI 10.1152/physrev.00050.2005
    • Lang, F., Bohmer, C., Palmada, M., Seebohm, G., Strutz-Seebohm, N., and Vallon, V. (2006) (Patho)physiological significance of the serum-and glucocorticoid-inducible kinase isoforms. Physiol. Rev. 86, 1151-1178 (Pubitemid 44521650)
    • (2006) Physiological Reviews , vol.86 , Issue.4 , pp. 1151-1178
    • Lang, F.1    Bohmer, C.2    Palmada, M.3    Seebohm, G.4    Strutz-Seebohm, N.5    Vallon, V.6
  • 80
    • 79551479336 scopus 로고    scopus 로고
    • Regulation of voltage-gated ion channels in excitable cells by the ubiquitin ligases Nedd4 and Nedd4-2
    • Bongiorno, D., Schuetz, F., Poronnik, P., and Adams, D.J. (2011) Regulation of voltage-gated ion channels in excitable cells by the ubiquitin ligases Nedd4 and Nedd4-2. Channels 5, 79-88
    • (2011) Channels , vol.5 , pp. 79-88
    • Bongiorno, D.1    Schuetz, F.2    Poronnik, P.3    Adams, D.J.4
  • 83
    • 32344451369 scopus 로고    scopus 로고
    • Stimulation of the creatine transporter SLC6A8 by the protein kinase mTOR
    • DOI 10.1016/j.bbrc.2006.01.055, PII S0006291X06001380
    • Shojaiefard, M., Christie, D.L., and Lang, F. (2006) Stimulation of the creatine transporter SLC6A8 by the protein kinase mTOR. Biochem. Biophys. Res. Commun. 341, 945-949 (Pubitemid 43221757)
    • (2006) Biochemical and Biophysical Research Communications , vol.341 , Issue.4 , pp. 945-949
    • Shojaiefard, M.1    Christie, D.L.2    Lang, F.3
  • 85
    • 0037046804 scopus 로고    scopus 로고
    • Targeted ablation of connexin26 in the inner ear epithelial gap junction network causes hearing impairment and cell death
    • DOI 10.1016/S0960-9822(02)00904-1, PII S0960982202009041
    • Cohen-Salmon, M., Ott, T., Michel, V., Hardelin, J.P., Perfettini, I., Eybalin, M., Wu, T., Marcus, D. C., Wangemann, P., Willecke, K., and Petit, C. (2002) Targeted ablation of connexin26 in the inner ear epithelial gap junction network causes hearing impairment and cell death. Curr. Biol. 12, 1106-1111 (Pubitemid 34766932)
    • (2002) Current Biology , vol.12 , Issue.13 , pp. 1106-1111
    • Cohen-Salmon, M.1    Ott, T.2    Michel, V.3    Hardelin, J.-P.4    Perfettini, I.5    Eybalin, M.6    Wu, T.7    Marcus, D.C.8    Wangemann, P.9    Willecke, K.10    Petit, C.11
  • 91
    • 84862916384 scopus 로고    scopus 로고
    • Transcription factor NF-kappaB regulates expression of pore-forming Ca2\+ channel unit, Orai1, and its activator, STIM1, to control Ca2\+ entry and affect cellular functions
    • Eylenstein, A., Schmidt, S., Gu, S., Yang, W., Schmid, E., Schmidt, E.M., Alesutan, I., Szteyn, K., Regel, I., Shumilina, E., and Lang, F. (2012) Transcription factor NF-kappaB regulates expression of pore-forming Ca2\+ channel unit, Orai1, and its activator, STIM1, to control Ca2\+ entry and affect cellular functions. J. Biol. Chem. 287, 2719-2730
    • (2012) J. Biol. Chem. , vol.287 , pp. 2719-2730
    • Eylenstein, A.1    Schmidt, S.2    Gu, S.3    Yang, W.4    Schmid, E.5    Schmidt, E.M.6    Alesutan, I.7    Szteyn, K.8    Regel, I.9    Shumilina, E.10    Lang, F.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.