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Volumn 17, Issue 10, 2006, Pages 1153-1159

Ankyrins and human disease: What the electrophysiologist should know

Author keywords

Ankyrin; Brugada syndrome; Cardiomyocyte; Cellular trafficking; Channelopathy; Cytoskeleton; Ion channel; Long QT syndrome; Sudden cardiac death; Ventricular arrhythmia

Indexed keywords

ADAPTOR PROTEIN; ANKYRIN; ANKYRIN B POLYPEPTIDE; ANKYRIN G POLYPEPTIDE; CARRIER PROTEIN; ION CHANNEL; MEMBRANE PROTEIN; SODIUM CHANNEL; UNCLASSIFIED DRUG;

EID: 33748752499     PISSN: 10453873     EISSN: 15408167     Source Type: Journal    
DOI: 10.1111/j.1540-8167.2006.00540.x     Document Type: Review
Times cited : (35)

References (75)
  • 1
    • 0017853463 scopus 로고
    • Purification of an active proteolytic fragment of the membrane attachment site for human erythrocyte spectrin
    • Bennett V: Purification of an active proteolytic fragment of the membrane attachment site for human erythrocyte spectrin. J Biol Chem 1978;253:2292-2299.
    • (1978) J Biol Chem , vol.253 , pp. 2292-2299
    • Bennett, V.1
  • 3
    • 0027337107 scopus 로고
    • Postmitotic expression of ankyrinR and beta R-spectrin in discrete neuronal populations of the rat brain
    • Lambert S, Bennett V: Postmitotic expression of ankyrinR and beta R-spectrin in discrete neuronal populations of the rat brain. J Neurosci 1993;13:3725-3735.
    • (1993) J Neurosci , vol.13 , pp. 3725-3735
    • Lambert, S.1    Bennett, V.2
  • 4
    • 0025117790 scopus 로고
    • Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins
    • Lux SE, John KM, Bennett V: Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature 1990;344:36-42.
    • (1990) Nature , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 5
    • 0025874185 scopus 로고
    • Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes
    • Otto E, Kunimoto M, McLaughlin T, Bennett V: Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes. J Cell Biol 1991;114:241-253.
    • (1991) J Cell Biol , vol.114 , pp. 241-253
    • Otto, E.1    Kunimoto, M.2    McLaughlin, T.3    Bennett, V.4
  • 6
    • 0033615979 scopus 로고    scopus 로고
    • Ankyrin-B is required for intracellular sorting of structurally diverse Ca2+ homeostasis proteins
    • Tuvia S, Buhusi M, Davis L, Reedy M, Bennett V: Ankyrin-B is required for intracellular sorting of structurally diverse Ca2+ homeostasis proteins. J Cell Biol 1999;147:995-1008.
    • (1999) J Cell Biol , vol.147 , pp. 995-1008
    • Tuvia, S.1    Buhusi, M.2    Davis, L.3    Reedy, M.4    Bennett, V.5
  • 7
    • 0032583202 scopus 로고    scopus 로고
    • Nervous system defects of AnkyrinB (-/-) mice suggest functional overlap between the cell adhesion molecule L1 and 440-kD AnkyrinB in premyelinated axons
    • Scotland P, Zhou D, Benveniste H, Bennett V: Nervous system defects of AnkyrinB (-/-) mice suggest functional overlap between the cell adhesion molecule L1 and 440-kD AnkyrinB in premyelinated axons. J Cell Biol 1998;143:1305-1315.
    • (1998) J Cell Biol , vol.143 , pp. 1305-1315
    • Scotland, P.1    Zhou, D.2    Benveniste, H.3    Bennett, V.4
  • 8
    • 0032508499 scopus 로고    scopus 로고
    • Identification of a novel ankyrin isoform (AnkG190) in kidney and lung that associates with the plasma membrane and binds alpha-Na, K-ATPase
    • Thevananther S, Kolli AH, Devarajan P: Identification of a novel ankyrin isoform (AnkG190) in kidney and lung that associates with the plasma membrane and binds alpha-Na, K-ATPase. J Biol Chem 1998;273:23952-23958.
    • (1998) J Biol Chem , vol.273 , pp. 23952-23958
    • Thevananther, S.1    Kolli, A.H.2    Devarajan, P.3
  • 9
    • 0029047129 scopus 로고
    • Ank3 (epithelial ankyrin), a widely distributed newmember of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain
    • Peters LL, John KM, Lu FM, Eicher EM, Higgins A, Yialamas M, Turtzo LC, Otsuka AJ, Lux SE: Ank3 (epithelial ankyrin), a widely distributed newmember of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain. J Cell Biol 1995;130:313-330.
    • (1995) J Cell Biol , vol.130 , pp. 313-330
    • Peters, L.L.1    John, K.M.2    Lu, F.M.3    Eicher, E.M.4    Higgins, A.5    Yialamas, M.6    Turtzo, L.C.7    Otsuka, A.J.8    Lux, S.E.9
  • 10
    • 0031711226 scopus 로고    scopus 로고
    • AnkyrinG is associated with the postsynaptic membrane and the sarcoplasmic reticulum in the skeletal muscle fiber
    • Kordeli E, Ludosky MA, Deprette C, Frappier T, Cartaud J: AnkyrinG is associated with the postsynaptic membrane and the sarcoplasmic reticulum in the skeletal muscle fiber. J Cell Sci 1998;111:2197-2207.
    • (1998) J Cell Sci , vol.111 , pp. 2197-2207
    • Kordeli, E.1    Ludosky, M.A.2    Deprette, C.3    Frappier, T.4    Cartaud, J.5
  • 11
    • 0028985712 scopus 로고
    • AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • Kordeli E, Lambert S, Bennett V: AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J Biol Chem 1995;270:2352-2359.
    • (1995) J Biol Chem , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lambert, S.2    Bennett, V.3
  • 12
    • 15744405775 scopus 로고    scopus 로고
    • Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Nav1.5 on the surface of cardiomyocytes
    • Mohler PJ, Rivolta I, Napolitano C, Lemaillet G, Lambert S, Priori SG, Bennett V: Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Nav1.5 on the surface of cardiomyocytes. Proc Natl Acad Sci U S A 2004;101:17533-17538.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17533-17538
    • Mohler, P.J.1    Rivolta, I.2    Napolitano, C.3    Lemaillet, G.4    Lambert, S.5    Priori, S.G.6    Bennett, V.7
  • 14
    • 0027999616 scopus 로고
    • Ankyrin binding activity shared by the neurofascin/L1/NrCAM family of nervous system cell adhesion molecules
    • Davis JQ, Bennett V: Ankyrin binding activity shared by the neurofascin/L1/NrCAM family of nervous system cell adhesion molecules. J Biol Chem 1994;269:27163-27166.
    • (1994) J Biol Chem , vol.269 , pp. 27163-27166
    • Davis, J.Q.1    Bennett, V.2
  • 15
    • 0027532185 scopus 로고
    • Ankyrin-binding proteins related to nervous system cell adhesion molecules: Candidates to provide transmembrane and intercellular connections in adult brain
    • Davis JQ, McLaughlin T, Bennett V: Ankyrin-binding proteins related to nervous system cell adhesion molecules: Candidates to provide transmembrane and intercellular connections in adult brain. J Cell Biol 1993;121:121-133.
    • (1993) J Cell Biol , vol.121 , pp. 121-133
    • Davis, J.Q.1    McLaughlin, T.2    Bennett, V.3
  • 16
    • 0032514147 scopus 로고    scopus 로고
    • Structural requirements for outside-in and inside-out signaling by Drosophila neuroglian, a member of the L1 family of cell adhesion molecules
    • Hortsch M, Homer D, Malhotra JD, Chang S, Frankel J, Jefford G, Dubreuil RR: Structural requirements for outside-in and inside-out signaling by Drosophila neuroglian, a member of the L1 family of cell adhesion molecules. J Cell Biol 1998;142:251-261.
    • (1998) J Cell Biol , vol.142 , pp. 251-261
    • Hortsch, M.1    Homer, D.2    Malhotra, J.D.3    Chang, S.4    Frankel, J.5    Jefford, G.6    Dubreuil, R.R.7
  • 17
    • 0032515171 scopus 로고    scopus 로고
    • Structural requirements for association of neurofascin with ankyrin
    • Zhang X, Davis JQ, Carpenter S, Bennett V: Structural requirements for association of neurofascin with ankyrin. J Biol Chem 1998;273:30785-30794.
    • (1998) J Biol Chem , vol.273 , pp. 30785-30794
    • Zhang, X.1    Davis, J.Q.2    Carpenter, S.3    Bennett, V.4
  • 18
    • 0023945567 scopus 로고
    • Mouse T lymphoma cells contain a transmembrane glycoprotein (GP85) that binds ankyrin
    • Kalomiris EL, Bourguignon LY: Mouse T lymphoma cells contain a transmembrane glycoprotein (GP85) that binds ankyrin. J Cell Biol 1988;106:319-327.
    • (1988) J Cell Biol , vol.106 , pp. 319-327
    • Kalomiris, E.L.1    Bourguignon, L.Y.2
  • 19
    • 0028141591 scopus 로고
    • Ankyrin-binding domain of CD44(GP85) is required for the expression of hyaluronic acid-mediated adhesion function
    • Lokeshwar VB, Fregien N, Bourguignon LY: Ankyrin-binding domain of CD44(GP85) is required for the expression of hyaluronic acid-mediated adhesion function. J Cell Biol 1994;126:1099-1109.
    • (1994) J Cell Biol , vol.126 , pp. 1099-1109
    • Lokeshwar, V.B.1    Fregien, N.2    Bourguignon, L.Y.3
  • 20
    • 0023954085 scopus 로고
    • Colocalization and coprecipitation of ankyrin and Na+,K+-ATPase in kidney epithelial cells
    • Koob R, Zimmermann M, Schoner W, Drenckhahn D: Colocalization and coprecipitation of ankyrin and Na+,K+-ATPase in kidney epithelial cells. Eur J Cell Biol 1988;45:230-237.
    • (1988) Eur J Cell Biol , vol.45 , pp. 230-237
    • Koob, R.1    Zimmermann, M.2    Schoner, W.3    Drenckhahn, D.4
  • 21
    • 0024571516 scopus 로고
    • Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells
    • Morrow JS, Cianci CD, Ardito T, Mann AS, Kashgarian M: Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. J Cell Biol 1989;108:455-465.
    • (1989) J Cell Biol , vol.108 , pp. 455-465
    • Morrow, J.S.1    Cianci, C.D.2    Ardito, T.3    Mann, A.S.4    Kashgarian, M.5
  • 22
    • 0023262074 scopus 로고
    • Ankyrin binding to (Na+ + K+)ATPase and implications for the organization of membrane domains in polarized cells
    • Nelson WJ, Veshnock PJ: Ankyrin binding to (Na+ + K+)ATPase and implications for the organization of membrane domains in polarized cells. Nature 1987;328:533-536.
    • (1987) Nature , vol.328 , pp. 533-536
    • Nelson, W.J.1    Veshnock, P.J.2
  • 23
    • 0027336147 scopus 로고
    • The cardiac Na+-Ca2+ exchanger binds to the cytoskeletal protein ankyrin
    • Li ZP, Burke EP, Frank JS, Bennett V, Philipson KD: The cardiac Na+-Ca2+ exchanger binds to the cytoskeletal protein ankyrin. J Biol Chem 1993;268:11489-11491.
    • (1993) J Biol Chem , vol.268 , pp. 11489-11491
    • Li, Z.P.1    Burke, E.P.2    Frank, J.S.3    Bennett, V.4    Philipson, K.D.5
  • 24
    • 0027323556 scopus 로고
    • Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin
    • Morgans CW, Kopito RR: Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin. J Cell Sci 1993;105:1137-1142.
    • (1993) J Cell Sci , vol.105 , pp. 1137-1142
    • Morgans, C.W.1    Kopito, R.R.2
  • 25
    • 0038458198 scopus 로고    scopus 로고
    • Anion exchanger 2 (AE2) binds to erythrocyte ankyrin and is colocalized with ankyrin along the basolateral plasma membrane of human gastric parietal cells
    • Jons T, Drenckhahn D: Anion exchanger 2 (AE2) binds to erythrocyte ankyrin and is colocalized with ankyrin along the basolateral plasma membrane of human gastric parietal cells. Eur J Cell Biol 1998;75:232-236.
    • (1998) Eur J Cell Biol , vol.75 , pp. 232-236
    • Jons, T.1    Drenckhahn, D.2
  • 26
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes
    • Bennett V, Stenbuck PJ: The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature 1979;280:468-473.
    • (1979) Nature , vol.280 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.J.2
  • 27
    • 0018397366 scopus 로고
    • Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin
    • Bennett V, Stenbuck PJ: Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin. J Biol Chem 1979;254:2533-2541.
    • (1979) J Biol Chem , vol.254 , pp. 2533-2541
    • Bennett, V.1    Stenbuck, P.J.2
  • 28
    • 0034646634 scopus 로고    scopus 로고
    • Sodium channel beta subunits mediate homophilic cell adhesion and recruit ankyrin to points of cell-cell contact
    • Malhotra JD, Kazen-Gillespie K, Hortsch M, Isom LL: Sodium channel beta subunits mediate homophilic cell adhesion and recruit ankyrin to points of cell-cell contact. J Biol Chem 2000;275:11383-11388.
    • (2000) J Biol Chem , vol.275 , pp. 11383-11388
    • Malhotra, J.D.1    Kazen-Gillespie, K.2    Hortsch, M.3    Isom, L.L.4
  • 29
    • 0023948543 scopus 로고
    • Ankyrin and spectrin associate with voltage-dependent sodium channels in brain
    • Srinivasan Y, Elmer L, Davis J, Bennett V, Angelides K: Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. Nature 1988;333:177-180.
    • (1988) Nature , vol.333 , pp. 177-180
    • Srinivasan, Y.1    Elmer, L.2    Davis, J.3    Bennett, V.4    Angelides, K.5
  • 30
    • 20044369520 scopus 로고    scopus 로고
    • The ammonium transporter RhBG: Requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells
    • Lopez C, Metral S, Eladari D, Drevensek S, Gane P, Chambrey R, Bennett V, Cartron J-P, Le Van Kim C, Colin Y: The ammonium transporter RhBG: Requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells. J Biol Chem 2004;280:8221-8228.
    • (2004) J Biol Chem , vol.280 , pp. 8221-8228
    • Lopez, C.1    Metral, S.2    Eladari, D.3    Drevensek, S.4    Gane, P.5    Chambrey, R.6    Bennett, V.7    Cartron, J.-P.8    Le Van Kim, C.9    Colin, Y.10
  • 31
    • 0035896519 scopus 로고    scopus 로고
    • Interaction between the -Nterminal domain of gastric H,K-ATPase and the spectrin binding domain of ankyrin III
    • Festy F, Robert JC, Brasseur R, Thomas A: Interaction between the -Nterminal domain of gastric H,K-ATPase and the spectrin binding domain of ankyrin III. J Biol Chem 2001;276:7721-7726.
    • (2001) J Biol Chem , vol.276 , pp. 7721-7726
    • Festy, F.1    Robert, J.C.2    Brasseur, R.3    Thomas, A.4
  • 33
    • 0027465122 scopus 로고
    • The involvement of ankyrin in the regulation of inositol 1,4,5- trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells
    • Bourguignon LY, Jin H, Iida N, Brandt NR, Zhang SH: The involvement of ankyrin in the regulation of inositol 1,4,5- trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells. J Biol Chem 1993;268:7290-7297.
    • (1993) J Biol Chem , vol.268 , pp. 7290-7297
    • Bourguignon, L.Y.1    Jin, H.2    Iida, N.3    Brandt, N.R.4    Zhang, S.H.5
  • 34
    • 0027469597 scopus 로고
    • Detergent solubility of the inositol trisphosphate receptor in rat brain membranes. Evidence for association of the receptor with ankyrin
    • Joseph SK, Samanta S: Detergent solubility of the inositol trisphosphate receptor in rat brain membranes. Evidence for association of the receptor with ankyrin. J Biol Chem 1993;268:6477-6486.
    • (1993) J Biol Chem , vol.268 , pp. 6477-6486
    • Joseph, S.K.1    Samanta, S.2
  • 35
    • 29144509561 scopus 로고    scopus 로고
    • Ankyrin-B coordinates the Na/K ATPase, Na/Ca exchanger, and InsP(3) receptor in a cardiac T-tubule/SR microdomain
    • Mohler PJ, Davis JQ, Bennett V: Ankyrin-B coordinates the Na/K ATPase, Na/Ca exchanger, and InsP(3) receptor in a cardiac T-tubule/SR microdomain. PLoS Biol 2005;3:2158-2167.
    • (2005) PLoS Biol , vol.3 , pp. 2158-2167
    • Mohler, P.J.1    Davis, J.Q.2    Bennett, V.3
  • 36
    • 0029052797 scopus 로고
    • Ryanodine receptor-ankyrin interaction regulates internal Ca2+ release in mouse T-lymphoma cells
    • Bourguignon LY, Chu A, Jin H, Brandt NR: Ryanodine receptor-ankyrin interaction regulates internal Ca2+ release in mouse T-lymphoma cells. J Biol Chem 1995;270:17917-17922.
    • (1995) J Biol Chem , vol.270 , pp. 17917-17922
    • Bourguignon, L.Y.1    Chu, A.2    Jin, H.3    Brandt, N.R.4
  • 37
    • 0029150191 scopus 로고
    • The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger
    • Michaely P, Bennett V: The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger. J Biol Chem 1995;270:22050-22057.
    • (1995) J Biol Chem , vol.270 , pp. 22050-22057
    • Michaely, P.1    Bennett, V.2
  • 38
    • 0029567019 scopus 로고
    • Mechanism for binding site diversity on ankyrin. Comparison of binding sites on ankyrin for neurofascin and the Cl-/HCO3- anion exchanger
    • Michaely P, Bennett V: Mechanism for binding site diversity on ankyrin. Comparison of binding sites on ankyrin for neurofascin and the Cl-/HCO3- anion exchanger. J Biol Chem 1995;270:31298-31302.
    • (1995) J Biol Chem , vol.270 , pp. 31298-31302
    • Michaely, P.1    Bennett, V.2
  • 39
    • 33646830169 scopus 로고    scopus 로고
    • Isoform specificity of ankyrin-B: A site in the divergent C-terminal domain is required for intramolecular association
    • Abdi KM, Mohler PJ, Davis JQ, Bennett V: Isoform specificity of ankyrin-B: A site in the divergent C-terminal domain is required for intramolecular association. J Biol Chem 2006;281:5741-5749.
    • (2006) J Biol Chem , vol.281 , pp. 5741-5749
    • Abdi, K.M.1    Mohler, P.J.2    Davis, J.Q.3    Bennett, V.4
  • 40
    • 0021355325 scopus 로고
    • Brain ankyrin. Purification of a 72,000 Mr spectrin-binding domain
    • Davis JQ, Bennett V: Brain ankyrin. Purification of a 72,000 Mr spectrin-binding domain. J Biol Chem 1984;259:1874-1881.
    • (1984) J Biol Chem , vol.259 , pp. 1874-1881
    • Davis, J.Q.1    Bennett, V.2
  • 41
    • 4544252325 scopus 로고    scopus 로고
    • Ankyrin-B targets {beta}2-spectrin to an intracellular compartment in neonatal cardiomyocytes
    • Mohler PJ, Yoon W, Bennett V: Ankyrin-B targets {beta}2-spectrin to an intracellular compartment in neonatal cardiomyocytes. J Biol Chem 2004;279:40185-40193.
    • (2004) J Biol Chem , vol.279 , pp. 40185-40193
    • Mohler, P.J.1    Yoon, W.2    Bennett, V.3
  • 42
    • 0347364671 scopus 로고    scopus 로고
    • The death domain of kidney ankyrin interacts with Fas and promotes Fas-mediated cell death in renal epithelia
    • Del Rio M, Imam A, DeLeon M, Gomez G, Mishra J, Ma Q, Parikh S, Devarajan P: The death domain of kidney ankyrin interacts with Fas and promotes Fas-mediated cell death in renal epithelia. J Am Soc Nephrol 2004;15:41-51.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 41-51
    • Del Rio, M.1    Imam, A.2    DeLeon, M.3    Gomez, G.4    Mishra, J.5    Ma, Q.6    Parikh, S.7    Devarajan, P.8
  • 43
    • 0033601077 scopus 로고    scopus 로고
    • Three-dimensional structure of a complex between the death domains of Pelle and Tube
    • Xiao T, Towb P, Wasserman SA, Sprang SR: Three-dimensional structure of a complex between the death domains of Pelle and Tube. Cell 1999;99:545-555.
    • (1999) Cell , vol.99 , pp. 545-555
    • Xiao, T.1    Towb, P.2    Wasserman, S.A.3    Sprang, S.R.4
  • 44
    • 0026722207 scopus 로고
    • Ankyrin regulation: An alternatively spliced segment of the regulatory domain functions as an intramolecular modulator
    • Davis LH, Davis JQ, Bennett V: Ankyrin regulation: An alternatively spliced segment of the regulatory domain functions as an intramolecular modulator. J Biol Chem 1992;267:18966-18972.
    • (1992) J Biol Chem , vol.267 , pp. 18966-18972
    • Davis, L.H.1    Davis, J.Q.2    Bennett, V.3
  • 45
    • 0023196746 scopus 로고
    • Regulatory domains of erythrocyte ankyrin
    • Hall TG, Bennett V: Regulatory domains of erythrocyte ankyrin. J Biol Chem 1987;262:10537-10545.
    • (1987) J Biol Chem , vol.262 , pp. 10537-10545
    • Hall, T.G.1    Bennett, V.2
  • 46
    • 0037155903 scopus 로고    scopus 로고
    • The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras in rescue of abnormal inositol 1,4,5-trisphosphate and ryanodine receptor distribution in ankyrin-B (-/-) neonatal cardiomyocytes
    • Mohler PJ, Gramolini AO, Bennett V: The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras in rescue of abnormal inositol 1,4,5-trisphosphate and ryanodine receptor distribution in ankyrin-B (-/-) neonatal cardiomyocytes. J Biol Chem 2002;277:10599-10607.
    • (2002) J Biol Chem , vol.277 , pp. 10599-10607
    • Mohler, P.J.1    Gramolini, A.O.2    Bennett, V.3
  • 48
    • 0037455559 scopus 로고    scopus 로고
    • Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles
    • Bagnato P, Barone V, Giacomello E, Rossi D, Sorrentino V: Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles. J Cell Biol 2003;160:245-253.
    • (2003) J Cell Biol , vol.160 , pp. 245-253
    • Bagnato, P.1    Barone, V.2    Giacomello, E.3    Rossi, D.4    Sorrentino, V.5
  • 49
    • 2942533956 scopus 로고    scopus 로고
    • Isoform specificity among ankyrins: An amphipathic alpha-helix in the divergent regulatory domain of ankyrin-B interacts with the molecular co-chaperone Hdj1/Hsp40
    • Mohler PJ, Hoffman JA, Davis JQ, Abdi KM, Kim CR, Jones SK, Davis LH, Roberts KF, Bennett V: Isoform specificity among ankyrins: An amphipathic alpha-helix in the divergent regulatory domain of ankyrin-B interacts with the molecular co-chaperone Hdj1/Hsp40. J Biol Chem 2004;279:25798-25804.
    • (2004) J Biol Chem , vol.279 , pp. 25798-25804
    • Mohler, P.J.1    Hoffman, J.A.2    Davis, J.Q.3    Abdi, K.M.4    Kim, C.R.5    Jones, S.K.6    Davis, L.H.7    Roberts, K.F.8    Bennett, V.9
  • 50
    • 0025260754 scopus 로고
    • Ankyrin and the hemolytic anemia mutation, nb, map to mouse chromosome 8: Presence of the nb allele is associated with a truncated erythrocyte ankyrin
    • White RA, Birkenmeier CS, Lux SE, Barker JE: Ankyrin and the hemolytic anemia mutation, nb, map to mouse chromosome 8: Presence of the nb allele is associated with a truncated erythrocyte ankyrin. Proc Natl Acad Sci USA 1990;87:3117-3121.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3117-3121
    • White, R.A.1    Birkenmeier, C.S.2    Lux, S.E.3    Barker, J.E.4
  • 52
    • 0036432768 scopus 로고    scopus 로고
    • Molecular basis of red cell membrane disorders
    • Delaunay J: Molecular basis of red cell membrane disorders. Acta Haematol 2002;108:210-218.
    • (2002) Acta Haematol , vol.108 , pp. 210-218
    • Delaunay, J.1
  • 53
    • 0030443956 scopus 로고    scopus 로고
    • Molecular composition of the node of Ranvier: Identification of ankyrin- binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments
    • Davis JQ, Lambert S, Bennett V: Molecular composition of the node of Ranvier: Identification of ankyrin- binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments. J Cell Biol 1996;135:1355-1367.
    • (1996) J Cell Biol , vol.135 , pp. 1355-1367
    • Davis, J.Q.1    Lambert, S.2    Bennett, V.3
  • 54
    • 0024708031 scopus 로고
    • Distribution of Na+ channels and ankyrin in neuromuscular junctions is complementary to that of acetylcholine receptors and the 43 kd protein
    • Flucher BE, Daniels MP: Distribution of Na+ channels and ankyrin in neuromuscular junctions is complementary to that of acetylcholine receptors and the 43 kd protein. Neuron 1989;3:163-175.
    • (1989) Neuron , vol.3 , pp. 163-175
    • Flucher, B.E.1    Daniels, M.P.2
  • 55
    • 0032498588 scopus 로고    scopus 로고
    • Beta-Spectrin is colocalized with both voltage-gated sodium channels and ankyrinG at the adult rat neuromuscular junction
    • Wood SJ, Slater CR: beta-Spectrin is colocalized with both voltage-gated sodium channels and ankyrinG at the adult rat neuromuscular junction. J Cell Biol 1998;140:675-684.
    • (1998) J Cell Biol , vol.140 , pp. 675-684
    • Wood, S.J.1    Slater, C.R.2
  • 56
    • 0032582909 scopus 로고    scopus 로고
    • AnkyrinG is required for clustering of voltage-gated Na channels at axon initial segments and for normal action potential firing
    • Zhou D, Lambert S, Malen PL, Carpenter S, Boland LM, Bennett V: AnkyrinG is required for clustering of voltage-gated Na channels at axon initial segments and for normal action potential firing. J Cell Biol 1998;143:1295-1304.
    • (1998) J Cell Biol , vol.143 , pp. 1295-1304
    • Zhou, D.1    Lambert, S.2    Malen, P.L.3    Carpenter, S.4    Boland, L.M.5    Bennett, V.6
  • 57
    • 0035956420 scopus 로고    scopus 로고
    • Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments
    • Jenkins SM, Bennett V: Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments. J Cell Biol 2001;155:739-746.
    • (2001) J Cell Biol , vol.155 , pp. 739-746
    • Jenkins, S.M.1    Bennett, V.2
  • 58
    • 5444260773 scopus 로고    scopus 로고
    • Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje axon initial segment
    • Ango F, di Cristo G, Higashiyama H, Bennett V, Wu P, Huang ZJ: Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje axon initial segment. Cell 2004;119:257-272.
    • (2004) Cell , vol.119 , pp. 257-272
    • Ango, F.1    Di Cristo, G.2    Higashiyama, H.3    Bennett, V.4    Wu, P.5    Huang, Z.J.6
  • 59
    • 0041345748 scopus 로고    scopus 로고
    • Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits
    • Lemaillet G, Walker B, Lambert S: Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits. J Biol Chem 2003;278:27333-27339.
    • (2003) J Biol Chem , vol.278 , pp. 27333-27339
    • Lemaillet, G.1    Walker, B.2    Lambert, S.3
  • 63
    • 0026466921 scopus 로고
    • Right bundle branch block, persistent ST segment elevation and sudden cardiac death: A distinct clinical and electrocardiographic syndrome. A multicenter report
    • Brugada P, Brugada J: Right bundle branch block, persistent ST segment elevation and sudden cardiac death: A distinct clinical and electrocardiographic syndrome. A multicenter report. J Am Coll Cardiol 1992;20:1391-1396.
    • (1992) J Am Coll Cardiol , vol.20 , pp. 1391-1396
    • Brugada, P.1    Brugada, J.2
  • 66
    • 0029002969 scopus 로고
    • A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel
    • Sanguinetti MC, Jiang C, Curran ME, Keating MT: A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel. Cell 1995;81:299-307.
    • (1995) Cell , vol.81 , pp. 299-307
    • Sanguinetti, M.C.1    Jiang, C.2    Curran, M.E.3    Keating, M.T.4
  • 74
    • 27744480028 scopus 로고    scopus 로고
    • Targeted mutational analysis of ankyrin-B in 541 consecutive, unrelated patients referred for long QT syndrome genetic testing and 200 healthy subjects
    • Sherman J, Tester DJ, Ackerman MJ: Targeted mutational analysis of ankyrin-B in 541 consecutive, unrelated patients referred for long QT syndrome genetic testing and 200 healthy subjects. Heart Rhythm 2005;2:1218-1223.
    • (2005) Heart Rhythm , vol.2 , pp. 1218-1223
    • Sherman, J.1    Tester, D.J.2    Ackerman, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.