메뉴 건너뛰기




Volumn 8, Issue 2, 2013, Pages

Connexin43 Hemichannel-Mediated Regulation of Connexin43

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; CADMIUM; CONNEXIN 43; GLUTATHIONE; HEPTANOL; STRESS ACTIVATED PROTEIN KINASE;

EID: 84874528212     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0058057     Document Type: Article
Times cited : (27)

References (47)
  • 1
    • 17344390158 scopus 로고    scopus 로고
    • Plasma membrane channels formed by connexins: their regulation and functions
    • Saez JC, Berthoud VM, Branes MC, Martinez AD, Beyer EC, (2003) Plasma membrane channels formed by connexins: their regulation and functions. Physiol Rev 83: 1359-1400.
    • (2003) Physiol Rev , vol.83 , pp. 1359-1400
    • Saez, J.C.1    Berthoud, V.M.2    Branes, M.C.3    Martinez, A.D.4    Beyer, E.C.5
  • 2
    • 36349020799 scopus 로고    scopus 로고
    • Pathophysiological roles of gap junction in glomerular mesangial cells
    • Yao J, Zhu Y, Morioka T, Oite T, Kitamura M, (2007) Pathophysiological roles of gap junction in glomerular mesangial cells. J Membr Biol 217: 123-130.
    • (2007) J Membr Biol , vol.217 , pp. 123-130
    • Yao, J.1    Zhu, Y.2    Morioka, T.3    Oite, T.4    Kitamura, M.5
  • 3
    • 66049127141 scopus 로고    scopus 로고
    • Gap junctional intercellular communication in the juxtaglomerular apparatus
    • Yao J, Oite T, Kitamura M, (2009) Gap junctional intercellular communication in the juxtaglomerular apparatus. Am J Physiol Renal Physiol 296: F939-946.
    • (2009) Am J Physiol Renal Physiol , vol.296
    • Yao, J.1    Oite, T.2    Kitamura, M.3
  • 4
    • 58149091691 scopus 로고    scopus 로고
    • Oxidative stress, lens gap junctions, and cataracts
    • Berthoud VM, Beyer EC, (2009) Oxidative stress, lens gap junctions, and cataracts. Antioxid Redox Signal 11: 339-353.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 339-353
    • Berthoud, V.M.1    Beyer, E.C.2
  • 5
    • 58149092380 scopus 로고    scopus 로고
    • Oxidative-dependent integration of signal transduction with intercellular gap junctional communication in the control of gene expression
    • Upham BL, Trosko JE, (2009) Oxidative-dependent integration of signal transduction with intercellular gap junctional communication in the control of gene expression. Antioxid Redox Signal 11: 297-307.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 297-307
    • Upham, B.L.1    Trosko, J.E.2
  • 6
    • 79957480883 scopus 로고    scopus 로고
    • Connexin43 hemichannels contribute to cadmium-induced oxidative stress and cell injury
    • Fang X, Huang T, Zhu Y, Yan Q, Chi Y, et al. (2011) Connexin43 hemichannels contribute to cadmium-induced oxidative stress and cell injury. Antioxid Redox Signal 14: 2427-2439.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2427-2439
    • Fang, X.1    Huang, T.2    Zhu, Y.3    Yan, Q.4    Chi, Y.5
  • 7
    • 40249103337 scopus 로고    scopus 로고
    • A novel role for connexin hemichannel in oxidative stress and smoking-induced cell injury
    • Ramachandran S, Xie LH, John SA, Subramaniam S, Lal R, (2007) A novel role for connexin hemichannel in oxidative stress and smoking-induced cell injury. PLoS One 2: e712.
    • (2007) PLoS One , vol.2
    • Ramachandran, S.1    Xie, L.H.2    John, S.A.3    Subramaniam, S.4    Lal, R.5
  • 8
    • 33745528139 scopus 로고    scopus 로고
    • The gap junction cellular internet: connexin hemichannels enter the signalling limelight
    • Evans WH, De Vuyst E, Leybaert L, (2006) The gap junction cellular internet: connexin hemichannels enter the signalling limelight. Biochem J 397: 1-14.
    • (2006) Biochem J , vol.397 , pp. 1-14
    • Evans, W.H.1    De Vuyst, E.2    Leybaert, L.3
  • 9
    • 44849141495 scopus 로고    scopus 로고
    • Stimulated efflux of amino acids and glutathione from cultured hippocampal slices by omission of extracellular calcium: likely involvement of connexin hemichannels
    • Stridh MH, Tranberg M, Weber SG, Blomstrand F, Sandberg M, (2008) Stimulated efflux of amino acids and glutathione from cultured hippocampal slices by omission of extracellular calcium: likely involvement of connexin hemichannels. J Biol Chem 283: 10347-10356.
    • (2008) J Biol Chem , vol.283 , pp. 10347-10356
    • Stridh, M.H.1    Tranberg, M.2    Weber, S.G.3    Blomstrand, F.4    Sandberg, M.5
  • 10
    • 21844442343 scopus 로고    scopus 로고
    • Mechanical strain opens connexin 43 hemichannels in osteocytes: a novel mechanism for the release of prostaglandin
    • Cherian PP, Siller-Jackson AJ, Gu S, Wang X, Bonewald LF, et al. (2005) Mechanical strain opens connexin 43 hemichannels in osteocytes: a novel mechanism for the release of prostaglandin. Mol Biol Cell 16: 3100-3106.
    • (2005) Mol Biol Cell , vol.16 , pp. 3100-3106
    • Cherian, P.P.1    Siller-Jackson, A.J.2    Gu, S.3    Wang, X.4    Bonewald, L.F.5
  • 11
    • 33646584876 scopus 로고    scopus 로고
    • Ischemia opens neuronal gap junction hemichannels
    • Thompson RJ, Zhou N, MacVicar BA, (2006) Ischemia opens neuronal gap junction hemichannels. Science 312: 924-927.
    • (2006) Science , vol.312 , pp. 924-927
    • Thompson, R.J.1    Zhou, N.2    MacVicar, B.A.3
  • 12
    • 67649641505 scopus 로고    scopus 로고
    • Role of oxidative stress in cadmium toxicity and carcinogenesis
    • Liu J, Qu W, Kadiiska MB, (2009) Role of oxidative stress in cadmium toxicity and carcinogenesis. Toxicol Appl Pharmacol 238: 209-214.
    • (2009) Toxicol Appl Pharmacol , vol.238 , pp. 209-214
    • Liu, J.1    Qu, W.2    Kadiiska, M.B.3
  • 13
    • 41149169845 scopus 로고    scopus 로고
    • Involvement of selective reactive oxygen species upstream of proapoptotic branches of unfolded protein response
    • Yokouchi M, Hiramatsu N, Hayakawa K, Okamura M, Du S, et al. (2008) Involvement of selective reactive oxygen species upstream of proapoptotic branches of unfolded protein response. J Biol Chem 283: 4252-4260.
    • (2008) J Biol Chem , vol.283 , pp. 4252-4260
    • Yokouchi, M.1    Hiramatsu, N.2    Hayakawa, K.3    Okamura, M.4    Du, S.5
  • 14
    • 0037292110 scopus 로고    scopus 로고
    • Sensitive endpoints for evaluating cadmium-induced acute toxicity in LLC-PK1 cells
    • Gennari A, Cortese E, Boveri M, Casado J, Prieto P, (2003) Sensitive endpoints for evaluating cadmium-induced acute toxicity in LLC-PK1 cells. Toxicology 183: 211-220.
    • (2003) Toxicology , vol.183 , pp. 211-220
    • Gennari, A.1    Cortese, E.2    Boveri, M.3    Casado, J.4    Prieto, P.5
  • 15
    • 77956862551 scopus 로고    scopus 로고
    • Differential sensitivity and responsiveness of three human cell lines HepG2, 1321N1 and HEK 293 to cadmium
    • Lawal AO, Ellis E, (2010) Differential sensitivity and responsiveness of three human cell lines HepG2, 1321N1 and HEK 293 to cadmium. J Toxicol Sci 35: 465-478.
    • (2010) J Toxicol Sci , vol.35 , pp. 465-478
    • Lawal, A.O.1    Ellis, E.2
  • 16
    • 0028825972 scopus 로고
    • Effects of glutathione depletion on the cytotoxic actions of cadmium in LLC-PK1 cells
    • Prozialeck WC, Lamar PC, (1995) Effects of glutathione depletion on the cytotoxic actions of cadmium in LLC-PK1 cells. Toxicol Appl Pharmacol 134: 285-295.
    • (1995) Toxicol Appl Pharmacol , vol.134 , pp. 285-295
    • Prozialeck, W.C.1    Lamar, P.C.2
  • 17
    • 0035892367 scopus 로고    scopus 로고
    • Potentiation of cadmium-induced cytotoxicity by sulfur amino acid deprivation through activation of extracellular signal-regulated kinase1/2 (ERK1/2) in conjunction with p38 kinase or c-jun N-terminal kinase (JNK). Complete inhibition of the potentiated toxicity by U0126 an ERK1/2 and p38 kinase inhibitor
    • Son MH, Kang KW, Lee CH, Kim SG, (2001) Potentiation of cadmium-induced cytotoxicity by sulfur amino acid deprivation through activation of extracellular signal-regulated kinase1/2 (ERK1/2) in conjunction with p38 kinase or c-jun N-terminal kinase (JNK). Complete inhibition of the potentiated toxicity by U0126 an ERK1/2 and p38 kinase inhibitor. Biochem Pharmacol 62: 1379-1390.
    • (2001) Biochem Pharmacol , vol.62 , pp. 1379-1390
    • Son, M.H.1    Kang, K.W.2    Lee, C.H.3    Kim, S.G.4
  • 18
    • 0034695660 scopus 로고    scopus 로고
    • Up-regulation of multidrug resistance P-glycoprotein via nuclear factor-kappaB activation protects kidney proximal tubule cells from cadmium- and reactive oxygen species-induced apoptosis
    • Thevenod F, Friedmann JM, Katsen AD, Hauser IA, (2000) Up-regulation of multidrug resistance P-glycoprotein via nuclear factor-kappaB activation protects kidney proximal tubule cells from cadmium- and reactive oxygen species-induced apoptosis. J Biol Chem 275: 1887-1896.
    • (2000) J Biol Chem , vol.275 , pp. 1887-1896
    • Thevenod, F.1    Friedmann, J.M.2    Katsen, A.D.3    Hauser, I.A.4
  • 19
    • 0031431657 scopus 로고    scopus 로고
    • Hydrogen peroxide inhibits gap junctional intercellular communication in glutathione sufficient but not glutathione deficient cells
    • Upham BL, Kang KS, Cho HY, Trosko JE, (1997) Hydrogen peroxide inhibits gap junctional intercellular communication in glutathione sufficient but not glutathione deficient cells. Carcinogenesis 18: 37-42.
    • (1997) Carcinogenesis , vol.18 , pp. 37-42
    • Upham, B.L.1    Kang, K.S.2    Cho, H.Y.3    Trosko, J.E.4
  • 20
    • 18144427507 scopus 로고    scopus 로고
    • Divergent roles for glutathione in lindane-induced acute and delayed-onset inhibition of rat myometrial gap junctions
    • Loch-Caruso R, Upham BL, Harris C, Trosko JE, (2005) Divergent roles for glutathione in lindane-induced acute and delayed-onset inhibition of rat myometrial gap junctions. Toxicol Sci 85: 694-702.
    • (2005) Toxicol Sci , vol.85 , pp. 694-702
    • Loch-Caruso, R.1    Upham, B.L.2    Harris, C.3    Trosko, J.E.4
  • 21
    • 33947492471 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase mediates AML1-ETO protein-induced connexin-43 expression
    • Gao FH, Wang Q, Wu YL, Li X, Zhao KW, et al. (2007) c-Jun N-terminal kinase mediates AML1-ETO protein-induced connexin-43 expression. Biochem Biophys Res Commun 356: 505-511.
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 505-511
    • Gao, F.H.1    Wang, Q.2    Wu, Y.L.3    Li, X.4    Zhao, K.W.5
  • 22
    • 45749133478 scopus 로고    scopus 로고
    • Signal transduction and transcriptional control of cardiac connexin43 up-regulation after alpha 1-adrenoceptor stimulation
    • Salameh A, Krautblatter S, Baessler S, Karl S, Rojas Gomez D, et al. (2008) Signal transduction and transcriptional control of cardiac connexin43 up-regulation after alpha 1-adrenoceptor stimulation. J Pharmacol Exp Ther 326: 315-322.
    • (2008) J Pharmacol Exp Ther , vol.326 , pp. 315-322
    • Salameh, A.1    Krautblatter, S.2    Baessler, S.3    Karl, S.4    Rojas Gomez, D.5
  • 23
    • 2942604430 scopus 로고    scopus 로고
    • Amphetamine activates connexin43 gene expression in cultured neonatal rat cardiomyocytes through JNK and AP-1 pathway
    • Shyu KG, Wang BW, Yang YH, Tsai SC, Lin S, et al. (2004) Amphetamine activates connexin43 gene expression in cultured neonatal rat cardiomyocytes through JNK and AP-1 pathway. Cardiovasc Res 63: 98-108.
    • (2004) Cardiovasc Res , vol.63 , pp. 98-108
    • Shyu, K.G.1    Wang, B.W.2    Yang, Y.H.3    Tsai, S.C.4    Lin, S.5
  • 24
    • 82355184480 scopus 로고    scopus 로고
    • Reciprocal regulation between proinflammatory cytokine-induced inducible NO synthase (iNOS) and connexin43 in bladder smooth muscle cells
    • Li K, Yao J, Shi L, Sawada N, Chi Y, et al. (2011) Reciprocal regulation between proinflammatory cytokine-induced inducible NO synthase (iNOS) and connexin43 in bladder smooth muscle cells. J Biol Chem 286: 41552-41562.
    • (2011) J Biol Chem , vol.286 , pp. 41552-41562
    • Li, K.1    Yao, J.2    Shi, L.3    Sawada, N.4    Chi, Y.5
  • 25
    • 0042358675 scopus 로고    scopus 로고
    • ATP-dependent mechanism for coordination of intercellular Ca2+ signaling and renin secretion in rat juxtaglomerular cells
    • Yao J, Suwa M, Li B, Kawamura K, Morioka T, et al. (2003) ATP-dependent mechanism for coordination of intercellular Ca2+ signaling and renin secretion in rat juxtaglomerular cells. Circ Res 93: 338-345.
    • (2003) Circ Res , vol.93 , pp. 338-345
    • Yao, J.1    Suwa, M.2    Li, B.3    Kawamura, K.4    Morioka, T.5
  • 26
    • 77949652115 scopus 로고    scopus 로고
    • Gap junctions sensitize cancer cells to proteasome inhibitor MG132-induced apoptosis
    • Huang T, Zhu Y, Fang X, Chi Y, Kitamura M, et al. (2010) Gap junctions sensitize cancer cells to proteasome inhibitor MG132-induced apoptosis. Cancer Sci 101: 713-721.
    • (2010) Cancer Sci , vol.101 , pp. 713-721
    • Huang, T.1    Zhu, Y.2    Fang, X.3    Chi, Y.4    Kitamura, M.5
  • 29
    • 54049142938 scopus 로고    scopus 로고
    • TGF-beta induces connexin43 gene expression in normal murine mammary gland epithelial cells via activation of p38 and PI3K/AKT signaling pathways
    • Tacheau C, Fontaine J, Loy J, Mauviel A, Verrecchia F, (2008) TGF-beta induces connexin43 gene expression in normal murine mammary gland epithelial cells via activation of p38 and PI3K/AKT signaling pathways. J Cell Physiol 217: 759-768.
    • (2008) J Cell Physiol , vol.217 , pp. 759-768
    • Tacheau, C.1    Fontaine, J.2    Loy, J.3    Mauviel, A.4    Verrecchia, F.5
  • 30
    • 0035757441 scopus 로고    scopus 로고
    • Regulation of connexin43 expression by c-fos and c-jun in myometrial cells
    • Mitchell JA, Lye SJ, (2001) Regulation of connexin43 expression by c-fos and c-jun in myometrial cells. Cell Commun Adhes 8: 299-302.
    • (2001) Cell Commun Adhes , vol.8 , pp. 299-302
    • Mitchell, J.A.1    Lye, S.J.2
  • 31
    • 0030789179 scopus 로고    scopus 로고
    • The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents
    • Wilhelm D, Bender K, Knebel A, Angel P, (1997) The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents. Mol Cell Biol 17: 4792-4800.
    • (1997) Mol Cell Biol , vol.17 , pp. 4792-4800
    • Wilhelm, D.1    Bender, K.2    Knebel, A.3    Angel, P.4
  • 32
    • 84857482073 scopus 로고    scopus 로고
    • Glutathione precursor N-acetyl-cysteine modulates EEG synchronization in schizophrenia patients: a double-blind, randomized, placebo-controlled trial
    • Carmeli C, Knyazeva MG, Cuenod M, Do KQ, (2012) Glutathione precursor N-acetyl-cysteine modulates EEG synchronization in schizophrenia patients: a double-blind, randomized, placebo-controlled trial. PLoS One 7: e29341.
    • (2012) PLoS One , vol.7
    • Carmeli, C.1    Knyazeva, M.G.2    Cuenod, M.3    Do, K.Q.4
  • 33
    • 33846909572 scopus 로고    scopus 로고
    • Thrombin inhibits intercellular calcium wave propagation in corneal endothelial cells by modulation of hemichannels and gap junctions
    • D'Hondt C, Ponsaerts R, Srinivas SP, Vereecke J, Himpens B, (2007) Thrombin inhibits intercellular calcium wave propagation in corneal endothelial cells by modulation of hemichannels and gap junctions. Invest Ophthalmol Vis Sci 48: 120-133.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 120-133
    • D'Hondt, C.1    Ponsaerts, R.2    Srinivas, S.P.3    Vereecke, J.4    Himpens, B.5
  • 34
    • 77955559707 scopus 로고    scopus 로고
    • Enhanced glutathione efflux from astrocytes in culture by low extracellular Ca2+ and curcumin
    • Stridh MH, Correa F, Nodin C, Weber SG, Blomstrand F, et al. (2010) Enhanced glutathione efflux from astrocytes in culture by low extracellular Ca2+ and curcumin. Neurochem Res 35: 1231-1238.
    • (2010) Neurochem Res , vol.35 , pp. 1231-1238
    • Stridh, M.H.1    Correa, F.2    Nodin, C.3    Weber, S.G.4    Blomstrand, F.5
  • 35
    • 0030610108 scopus 로고    scopus 로고
    • Cadmium (Cd2+) disrupts E-cadherin-dependent cell-cell junctions in MDCK cells
    • Prozialeck WC, Lamar PC, (1997) Cadmium (Cd2+) disrupts E-cadherin-dependent cell-cell junctions in MDCK cells. In Vitro Cell Dev Biol Anim 33: 516-526.
    • (1997) In Vitro Cell Dev Biol Anim , vol.33 , pp. 516-526
    • Prozialeck, W.C.1    Lamar, P.C.2
  • 36
    • 0031759026 scopus 로고    scopus 로고
    • Comparison of the cytotoxic effects of cadmium (Cd(2+)) in high and low resistance strains of MDCK cells that express different levels of E-Cadherin
    • Prozialeck WC, Lamar PC, (1998) Comparison of the cytotoxic effects of cadmium (Cd(2+)) in high and low resistance strains of MDCK cells that express different levels of E-Cadherin. Toxicol In Vitro 12: 633-647.
    • (1998) Toxicol In Vitro , vol.12 , pp. 633-647
    • Prozialeck, W.C.1    Lamar, P.C.2
  • 37
    • 1942503184 scopus 로고    scopus 로고
    • Gap junctions and connexin-interacting proteins
    • Giepmans BN, (2004) Gap junctions and connexin-interacting proteins. Cardiovasc Res 62: 233-245.
    • (2004) Cardiovasc Res , vol.62 , pp. 233-245
    • Giepmans, B.N.1
  • 38
    • 0035188530 scopus 로고    scopus 로고
    • Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels
    • Martin PE, Blundell G, Ahmad S, Errington RJ, Evans WH, (2001) Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels. J Cell Sci 114: 3845-3855.
    • (2001) J Cell Sci , vol.114 , pp. 3845-3855
    • Martin, P.E.1    Blundell, G.2    Ahmad, S.3    Errington, R.J.4    Evans, W.H.5
  • 39
  • 40
    • 27644547807 scopus 로고    scopus 로고
    • Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration
    • Thomas T, Jordan K, Simek J, Shao Q, Jedeszko C, et al. (2005) Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration. J Cell Sci 118: 4451-4462.
    • (2005) J Cell Sci , vol.118 , pp. 4451-4462
    • Thomas, T.1    Jordan, K.2    Simek, J.3    Shao, Q.4    Jedeszko, C.5
  • 41
    • 0025924715 scopus 로고
    • Cadmium (Cd2+) disrupts intercellular junctions and actin filaments in LLC-PK1 cells
    • Prozialeck WC, Niewenhuis RJ, (1991) Cadmium (Cd2+) disrupts intercellular junctions and actin filaments in LLC-PK1 cells. Toxicol Appl Pharmacol 107: 81-97.
    • (1991) Toxicol Appl Pharmacol , vol.107 , pp. 81-97
    • Prozialeck, W.C.1    Niewenhuis, R.J.2
  • 42
    • 0027183210 scopus 로고
    • Cadmium in vivo causes disruption of tight junction-associated microfilaments in rat Sertoli cells
    • Hew KW, Heath GL, Jiwa AH, Welsh MJ, (1993) Cadmium in vivo causes disruption of tight junction-associated microfilaments in rat Sertoli cells. Biol Reprod 49: 840-849.
    • (1993) Biol Reprod , vol.49 , pp. 840-849
    • Hew, K.W.1    Heath, G.L.2    Jiwa, A.H.3    Welsh, M.J.4
  • 43
    • 0032522387 scopus 로고    scopus 로고
    • Central role of heterocellular gap junctional communication in endothelium-dependent relaxations of rabbit arteries
    • Chaytor AT, Evans WH, Griffith TM, (1998) Central role of heterocellular gap junctional communication in endothelium-dependent relaxations of rabbit arteries. J Physiol 508 (Pt 2): 561-573.
    • (1998) J Physiol , vol.508 , Issue.Pt 2 , pp. 561-573
    • Chaytor, A.T.1    Evans, W.H.2    Griffith, T.M.3
  • 44
    • 0035082041 scopus 로고    scopus 로고
    • Immunoglobulin and cytokine expression in mixed lymphocyte cultures is reduced by disruption of gap junction intercellular communication
    • Oviedo-Orta E, Gasque P, Evans WH, (2001) Immunoglobulin and cytokine expression in mixed lymphocyte cultures is reduced by disruption of gap junction intercellular communication. FASEB J 15: 768-774.
    • (2001) FASEB J , vol.15 , pp. 768-774
    • Oviedo-Orta, E.1    Gasque, P.2    Evans, W.H.3
  • 45
    • 34249811507 scopus 로고    scopus 로고
    • Functional gap junctions facilitate melanoma antigen transfer and cross-presentation between human dendritic cells
    • Mendoza-Naranjo A, Saez PJ, Johansson CC, Ramirez M, Mandakovic D, et al. (2007) Functional gap junctions facilitate melanoma antigen transfer and cross-presentation between human dendritic cells. J Immunol 178: 6949-6957.
    • (2007) J Immunol , vol.178 , pp. 6949-6957
    • Mendoza-Naranjo, A.1    Saez, P.J.2    Johansson, C.C.3    Ramirez, M.4    Mandakovic, D.5
  • 46
    • 78649894823 scopus 로고    scopus 로고
    • Intramolecular loop/tail interactions are essential for connexin 43-hemichannel activity
    • Ponsaerts R, De Vuyst E, Retamal M, D'Hondt C, Vermeire D, et al. (2010) Intramolecular loop/tail interactions are essential for connexin 43-hemichannel activity. FASEB J 24: 4378-4395.
    • (2010) FASEB J , vol.24 , pp. 4378-4395
    • Ponsaerts, R.1    De Vuyst, E.2    Retamal, M.3    D'Hondt, C.4    Vermeire, D.5
  • 47
    • 84866729771 scopus 로고    scopus 로고
    • Manipulating connexin communication channels: use of peptidomimetics and the translational outputs
    • Evans WH, Bultynck G, Leybaert L, (2012) Manipulating connexin communication channels: use of peptidomimetics and the translational outputs. J Membr Biol 245: 437-449.
    • (2012) J Membr Biol , vol.245 , pp. 437-449
    • Evans, W.H.1    Bultynck, G.2    Leybaert, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.