메뉴 건너뛰기




Volumn 2, Issue 2, 2008, Pages 125-129

Mechanism of Ca2+-dependent desensitization in TRP channels

Author keywords

Calcium; Desensitization; Phospholipase C; PIP2; TRP channels

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CALCIUM ION; CALMODULIN; CYCLIC NUCLEOTIDE GATED CHANNEL; DIACYLGLYCEROL; LIPID; MEMBRANE LIPID; PHOSPHATASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE; PHOSPHOLIPASE C; PHOSPHOTRANSFERASE; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL C; TRANSIENT RECEPTOR POTENTIAL CHANNEL M; VANILLOID RECEPTOR; VOLTAGE GATED CALCIUM CHANNEL; VOLTAGE GATED POTASSIUM CHANNEL; VOLTAGE GATED SODIUM CHANNEL;

EID: 55549148853     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.2.2.6026     Document Type: Review
Times cited : (49)

References (63)
  • 1
    • 39749115631 scopus 로고    scopus 로고
    • Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels
    • DOI 10.1021/bi702109w
    • Phelps CB, Huang RJ, Lishko PV, Wang RR, Gaudet R. Structural Analyses of the Ankyrin Repeat Domain of TRPV6 and Related TRPV Ion Channels. Biochemistry 2008; 47:2476-2484 (Pubitemid 351304553)
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2476-2484
    • Phelps, C.B.1    Huang, R.J.2    Lishko, P.V.3    Wang, R.R.4    Gaudet, R.5
  • 2
    • 0017335111 scopus 로고
    • Drosophila mutant with a transducer defect
    • Minke B. Drosophila mutant with a transducer defect. Biophys Struct Mech 1977; 3:59-64.
    • (1977) Biophys Struct Mech , vol.3 , pp. 59-64
    • Minke, B.1
  • 3
    • 33947730590 scopus 로고    scopus 로고
    • SnapShot: Mammalian TRP channels
    • Clapham DE. SnapShot: mammalian TRP channels. Cell 2007; 129:220.
    • (2007) Cell , vol.129 , pp. 220
    • Clapham, D.E.1
  • 6
    • 33747624445 scopus 로고    scopus 로고
    • Transient receptor potential channels in cardiovascular function and disease
    • DOI 10.1161/01.RES.0000233356.10630.8a, PII 0000301220060721000005
    • Inoue R, Jensen LJ, Shi J, Morita H, Nishida M, Honda A, Ito Y. Transient receptor potential channels in cardiovascular function and disease. Circ Res 2006; 99:119-131 (Pubitemid 44297035)
    • (2006) Circulation Research , vol.99 , Issue.2 , pp. 119-131
    • Inoue, R.1    Jensen, L.J.2    Shi, J.3    Morita, H.4    Nishida, M.5    Honda, A.6    Ito, Y.7
  • 7
    • 0037040395 scopus 로고    scopus 로고
    • The TRP channels, a remarkably functional family
    • DOI 10.1016/S0092-8674(02)00670-0
    • Montell C, Birnbaumer L, Flockerzi V. The TRP channels, a remarkably functional family. Cell 2002; 108:595-598 (Pubitemid 34241421)
    • (2002) Cell , vol.108 , Issue.5 , pp. 595-598
    • Montell, C.1    Birnbaumer, L.2    Flockerzi, V.3
  • 8
    • 2942544346 scopus 로고    scopus 로고
    • TRP ion channels in the nervous system
    • DOI 10.1016/j.conb.2004.05.003, PII S0959438804000704
    • Moran MM, Xu H, Clapham DE. TRP ion channels in the nervous system. Curr Opin Neurobiol 2004; 14:362-369 (Pubitemid 38759867)
    • (2004) Current Opinion in Neurobiology , vol.14 , Issue.3 , pp. 362-369
    • Moran, M.M.1    Xu, H.2    Clapham, D.E.3
  • 10
    • 0025307123 scopus 로고
    • A superfamily of ion channels
    • Jan LY, Jan YN. A superfamily of ion channels. Nature 1990; 345:672.
    • (1990) Nature , vol.345 , pp. 672
    • Jan, L.Y.1    Jan, Y.N.2
  • 11
    • 0026734109 scopus 로고
    • Tracing the roots of ion channels
    • Jan LY, Jan YN. Tracing the roots of ion channels. Cell 1992; 69:715-718
    • (1992) Cell , vol.69 , pp. 715-718
    • Jan, L.Y.1    Jan, Y.N.2
  • 12
    • 33748748066 scopus 로고    scopus 로고
    • Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel
    • DOI 10.1074/jbc.C600153200
    • Jin X, Touhey J, Gaudet R. Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J Biol Chem 2006; 281:25006-25010 (Pubitemid 44401888)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.35 , pp. 25006-25010
    • Jin, X.1    Touhey, J.2    Gaudet, R.3
  • 13
    • 34250190946 scopus 로고    scopus 로고
    • The Ankyrin Repeats of TRPV1 Bind Multiple Ligands and Modulate Channel Sensitivity
    • DOI 10.1016/j.neuron.2007.05.027, PII S0896627307004060
    • Lishko PV, Procko E, Jin X, Phelps CB, Gaudet R. The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 2007; 54:905-918 (Pubitemid 46907502)
    • (2007) Neuron , vol.54 , Issue.6 , pp. 905-918
    • Lishko, P.V.1    Procko, E.2    Jin, X.3    Phelps, C.B.4    Gaudet, R.5
  • 14
    • 33748138924 scopus 로고    scopus 로고
    • Crystal structure of the human TRPV2 channel ankyrin repeat domain
    • DOI 10.1110/ps.062357206
    • McCleverty CJ, Koesema E, Patapoutian A, Lesley SA, Kreusch A. Crystal structure of the human TRPV2 channel ankyrin repeat domain. Protein Sci 2006; 15:2201-2206 (Pubitemid 44316022)
    • (2006) Protein Science , vol.15 , Issue.9 , pp. 2201-2206
    • Mccleverty, C.J.1    Koesema, E.2    Patapoutian, A.3    Lesley, S.A.4    Kreusch, A.5
  • 15
    • 0035568314 scopus 로고    scopus 로고
    • The TRP channel and phospholipase C-mediated signaling
    • DOI 10.1023/A:1015191702536
    • Minke B. The TRP channel and phospholipase C-mediated signaling. Cell Mol Neurobiol 2001; 21:629-643 (Pubitemid 34538860)
    • (2001) Cellular and Molecular Neurobiology , vol.21 , Issue.6 , pp. 629-643
    • Minke, B.1
  • 16
    • 33645997388 scopus 로고    scopus 로고
    • Insights on TRP channels from in vivo studies in Drosophila
    • Minke B, Parnas M. Insights on TRP channels from in vivo studies in Drosophila. Annu Rev Physiol 2006; 68:649-684
    • (2006) Annu Rev Physiol , vol.68 , pp. 649-684
    • Minke, B.1    Parnas, M.2
  • 17
    • 33845727488 scopus 로고    scopus 로고
    • TRP channels and lipids: From Drosophila to mammalian physiology
    • DOI 10.1113/jphysiol.2006.118372
    • Hardie RC. TRP channels and lipids: from Drosophila to mammalian physiology. J Physiol 2007; 578:9-24. (Pubitemid 44971106)
    • (2007) Journal of Physiology , vol.578 , Issue.1 , pp. 9-24
    • Hardie, R.C.1
  • 18
    • 70049107889 scopus 로고    scopus 로고
    • Complex regulation of the TRPC3, 6 and 7 channel subfamily by diacylglycerol and phosphatidylinositol-4,5-bisphosphate
    • Lemonnier L, Trebak M, Putney JW Jr. Complex regulation of the TRPC3, 6 and 7 channel subfamily by diacylglycerol and phosphatidylinositol-4,5- bisphosphate. Cell Calcium 2007.
    • (2007) Cell Calcium
    • Lemonnier, L.1    Trebak, M.2    Putney Jr., J.W.3
  • 19
    • 33846935212 scopus 로고    scopus 로고
    • Canonical transient receptor potential 5
    • Beech DJ. Canonical transient receptor potential 5. Handb Exp Pharmacol 2007:109-123
    • (2007) Handb Exp Pharmacol , pp. 109-123
    • Beech, D.J.1
  • 20
    • 33847081630 scopus 로고    scopus 로고
    • Integration of Phosphoinositide- And Calmodulin-Mediated Regulation of TRPC6
    • DOI 10.1016/j.molcel.2007.01.021, PII S1097276507000445
    • Kwon Y, Hofmann T, Montell C. Integration of phosphoinositide- and calmodulin-mediated regulation of TRPC6. Mol Cell 2007; 25:491-503. (Pubitemid 46274446)
    • (2007) Molecular Cell , vol.25 , Issue.4 , pp. 491-503
    • Kwon, Y.1    Hofmann, T.2    Montell, C.3
  • 21
    • 28244499948 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-Bisphosphate rescues TRPM4 channels from desensitization
    • DOI 10.1074/jbc.M506965200
    • Zhang Z, Okawa H, Wang Y, Liman ER. Phosphatidylinositol 4,5-bisphosphate rescues TRPM4 channels from desensitization. J Biol Chem 2005; 280:39185-39192 (Pubitemid 41713870)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39185-39192
    • Zhang, Z.1    Okawa, H.2    Wang, Y.3    Liman, E.R.4
  • 22
    • 32544442208 scopus 로고    scopus 로고
    • 2+-activated cation channel TRPM4 is regulated by phosphatidylinositol 4,5-biphosphate
    • DOI 10.1038/sj.emboj.7600963, PII 7600963
    • Nilius B, Mahieu F, Prenen J, Janssens A, Owsianik G, Vennekens R, Voets T. The Ca2+-activated cation channel TRPM4 is regulated by phosphatidylinositol 4,5-biphosphate. Embo J 2006; 25:467-478 (Pubitemid 43237654)
    • (2006) EMBO Journal , vol.25 , Issue.3 , pp. 467-478
    • Nilius, B.1    Mahieu, F.2    Prenen, J.3    Janssens, A.4    Owsianik, G.5    Vennekens, R.6    Voets, T.7
  • 23
    • 0344149569 scopus 로고    scopus 로고
    • 2 regulate the taste transduction ion channel TRPM5
    • 2 regulate the taste transduction ion channel TRPM5. Proc Natl Acad Sci USA 2003; 100:15160-15165
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15160-15165
    • Liu, D.1    Liman, E.R.2
  • 25
    • 34548658196 scopus 로고    scopus 로고
    • Regulation of transient receptor potential (TRP) channels by phosphoinositides
    • DOI 10.1007/s00424-007-0275-6, Phosphoinositide control of ion channel activity
    • Rohacs T, Nilius B. Regulation of transient receptor potential (TRP) channels by phosphoinositides. Pflugers Arch 2007; 455:157-168 (Pubitemid 47403980)
    • (2007) Pflugers Archiv European Journal of Physiology , vol.455 , Issue.1 , pp. 157-168
    • Rohacs, T.1    Nilius, B.2
  • 29
    • 0037799198 scopus 로고    scopus 로고
    • 2 binding site as a determinant of capsaicin receptor sensitivity
    • 2 binding site as a determinant of capsaicin receptor sensitivity. Science 2003; 300:1284-1288
    • (2003) Science , vol.300 , pp. 1284-1288
    • Prescott, E.D.1    Julius, D.2
  • 30
    • 33750524257 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase binds to TRPV1 and mediates NGF-stimulated TRPV1 trafficking to the plasma membrane
    • DOI 10.1085/jgp.200609576
    • Stein AT, Ufret Vincenty CA, Hua L, Santana LF, Gordon SE. Phosphoinositide 3-kinase binds to TRPV1 and mediates NGF-stimulated TRPV1 trafficking to the plasma membrane. J Gen Physiol 2006; 128:509-522 (Pubitemid 44664629)
    • (2006) Journal of General Physiology , vol.128 , Issue.5 , pp. 509-522
    • Stein, A.T.1    Ufret-Vincenty, C.A.2    Hua, L.3    Santana, L.F.4    Gordon, S.E.5
  • 32
    • 0036023417 scopus 로고    scopus 로고
    • Sorting out MIC, TRP, and CRAC ion channels
    • Clapham DE. Sorting out MIC, TRP, and CRAC ion channels. J Gen Physiol 2002; 120:217-220
    • (2002) J Gen Physiol , vol.120 , pp. 217-220
    • Clapham, D.E.1
  • 33
    • 0035838673 scopus 로고    scopus 로고
    • Physiology, phylogeny, and functions of the TRP superfamily of cation channels
    • Montell C. Physiology, phylogeny, and functions of the TRP superfamily of cation channels. Sci STKE 2001; 2001:1.
    • (2001) Sci STKE , vol.2001 , pp. 1
    • Montell, C.1
  • 34
    • 0032374478 scopus 로고    scopus 로고
    • Calcium Channels Formed by Mammalian Trp Homologues
    • Zhu X, Birnbaumer L. Calcium Channels Formed by Mammalian Trp Homologues. News Physiol Sci 1998; 13:211-217 (Pubitemid 128153558)
    • (1998) News in Physiological Sciences , vol.13 , Issue.MNTH OCT , pp. 211-217
    • Zhu, X.1    Birnbaumer, L.2
  • 36
    • 34250666600 scopus 로고    scopus 로고
    • The transduction channel TRPM5 is gated by intracellular calcium in taste cells
    • DOI 10.1523/JNEUROSCI.4973-06.2007
    • Zhang Z, Zhao Z, Margolskee R, Liman E. The transduction channel TRPM5 is gated by intracellular calcium in taste cells. J Neurosci 2007; 27:5777-5786 (Pubitemid 350021073)
    • (2007) Journal of Neuroscience , vol.27 , Issue.21 , pp. 5777-5786
    • Zhang, Z.1    Zhao, Z.2    Margolskee, R.3    Liman, E.4
  • 37
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham DE. Calcium signaling. Cell 2007; 131:1047-1058
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 38
    • 27744434711 scopus 로고    scopus 로고
    • Melastatin-type transient receptor potential channel 7 is required for intestinal pacemaking activity
    • DOI 10.1053/j.gastro.2005.08.016, PII S0016508505017312
    • Zhu MH, Chae M, Kim HJ, Lee YM, Kim MJ, Jin NG, Yang DK, So I, Kim KW. Desensitization of canonical transient receptor potential channel 5 by protein kinase C. Am J Physiol Cell Physiol 2005; 289:591-600. (Pubitemid 41597392)
    • (2005) Gastroenterology , vol.129 , Issue.5 , pp. 1504-1517
    • Kim, B.J.1    Lim, H.2    Yang, D.K.3    Jun, J.Y.4    Chang, I.Y.5    Park, C.-S.6    So, I.7    Stanfield, P.R.8    Kim, K.W.9
  • 39
    • 0346118925 scopus 로고    scopus 로고
    • Desensitization of Capsaicin-activated Currents in the Vanilloid Receptor TRPV1 Is Decreased by the Cyclic AMP-dependent Protein Kinase Pathway
    • DOI 10.1074/jbc.M306619200
    • Mohapatra DP, Nau C. Desensitization of capsaicin-activated currents in the vanilloid receptor TRPV1 is decreased by the cyclic AMP-dependent protein kinase pathway. J Biol Chem 2003; 278:50080-50090 (Pubitemid 37548845)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50080-50090
    • Mohapatra, D.P.1    Nau, C.2
  • 40
    • 17144397173 scopus 로고    scopus 로고
    • 2+-dependent desensitization in the vanilloid receptor TRPV1 by calcineurin and cAMP-dependent protein kinase
    • 2+-dependent desensitization in the vanilloid receptor TRPV1 by calcineurin and cAMP-dependent protein kinase. J Biol Chem 2005; 280:13424-13432
    • (2005) J Biol Chem , vol.280 , pp. 13424-13432
    • Mohapatra, D.P.1    Nau, C.2
  • 41
    • 33846940717 scopus 로고    scopus 로고
    • Insights into TRPM4 function, regulation and physiological role
    • Vennekens R, Nilius B. Insights into TRPM4 function, regulation and physiological role. Handb Exp Pharmacol 2007:269-285
    • (2007) Handb Exp Pharmacol , pp. 269-285
    • Vennekens, R.1    Nilius, B.2
  • 43
    • 0029965156 scopus 로고    scopus 로고
    • Inhibition of calcineurin inhibits the desensitization of capsaicin-evoked currents in cultured dorsal root ganglion neurones from adult rats
    • DOI 10.1007/s004240050074
    • Docherty RJ, Yeats JC, Bevan S, Boddeke HW. Inhibition of calcineurin inhibits the desensitization of capsaicin-evoked currents in cultured dorsal root ganglion neurones from adult rats. Pflugers Arch 1996; 431:828-837 (Pubitemid 26134693)
    • (1996) Pflugers Archiv European Journal of Physiology , vol.431 , Issue.6 , pp. 828-837
    • Docherty, R.J.1    Yeats, J.C.2    Bevan, S.3    Boddeke, H.W.G.M.4
  • 44
    • 0038820000 scopus 로고    scopus 로고
    • Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels
    • DOI 10.1074/jbc.R300001200
    • Trudeau MC, Zagotta WN. Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels. J Biol Chem 2003; 278:18705-18708 (Pubitemid 36799249)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.21 , pp. 18705-18708
    • Trudeau, M.C.1    Zagotta, W.N.2
  • 45
    • 0037107123 scopus 로고    scopus 로고
    • Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels
    • Wen H, Levitan IB. Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels. J Neurosci 2002; 22:7991-8001. (Pubitemid 35379104)
    • (2002) Journal of Neuroscience , vol.22 , Issue.18 , pp. 7991-8001
    • Wen, H.1    Levitan, I.B.2
  • 49
    • 24644460439 scopus 로고    scopus 로고
    • 2+-binding proteins in the functional regulation of TRP channels
    • 2+-binding proteins in the functional regulation of TRP channels. Pflugers Arch 2005; 451:105-115
    • (2005) Pflugers Arch , vol.451 , pp. 105-115
    • Zhu, M.X.1
  • 50
    • 0036028768 scopus 로고    scopus 로고
    • 2+ entry activity of TRPC6 in HEK-293 cells
    • 2+ entry activity of TRPC6 in HEK-293 cells. Cell Calcium 2002; 32:201-207
    • (2002) Cell Calcium , vol.32 , pp. 201-207
    • Boulay, G.1
  • 52
    • 34748897412 scopus 로고    scopus 로고
    • Regulation of TRPM2 by extra- And intracellular calcium
    • DOI 10.1085/jgp.200709836
    • Starkus J, Beck A, Fleig A, Penner R. Regulation of TRPM2 by extra- and intracellular calcium. J Gen Physiol 2007; 130:427-440 (Pubitemid 47481605)
    • (2007) Journal of General Physiology , vol.130 , Issue.4 , pp. 427-440
    • Starkus, J.1    Beck, A.2    Fleig, A.3    Penner, R.4
  • 54
    • 18644381102 scopus 로고    scopus 로고
    • Functional recovery from desensitization of vanilloid receptor TRPV1 requires resynthesis of phosphatidylinositol 4,5-bisphosphate
    • DOI 10.1523/JNEUROSCI.1296-05.2005
    • Liu B, Zhang C, Qin F. Functional recovery from desensitization of vanilloid receptor TRPV1 requires resynthesis of phosphatidylinositol 4,5-bisphosphate. J Neurosci 2005; 25:4835-4843 (Pubitemid 40664131)
    • (2005) Journal of Neuroscience , vol.25 , Issue.19 , pp. 4835-4843
    • Liu, B.1    Zhang, C.2    Qin, F.3
  • 55
    • 2342472669 scopus 로고    scopus 로고
    • Biochemistry. Oily barbarians breach ion channel gates
    • Hilgemann DW. Biochemistry. Oily barbarians breach ion channel gates. Science 2004; 304:223-224
    • (2004) Science , vol.304 , pp. 223-224
    • Hilgemann, D.W.1
  • 57
    • 22244449320 scopus 로고    scopus 로고
    • An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family
    • DOI 10.1085/jgp.200509274
    • McLaughlin S, Smith SO, Hayman MJ, Murray D. An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. J Gen Physiol 2005; 126:41-53. (Pubitemid 40994107)
    • (2005) Journal of General Physiology , vol.126 , Issue.1 , pp. 41-53
    • McLaughlin, S.1    Smith, S.O.2    Hayman, M.J.3    Murray, D.4
  • 58
    • 0035895882 scopus 로고    scopus 로고
    • The Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Binds Strongly to Phosphatidylinositol 4,5-Bisphosphate
    • DOI 10.1074/jbc.M008355200
    • Wang J, Arbuzova A, Hangyas Mihalyne G, McLaughlin S. The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. J Biol Chem 2001; 276:5012-5019 (Pubitemid 37371393)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.7 , pp. 5012-5019
    • Wang, J.1    Arbuzova, A.2    Hangyas-Mihalyne, G.3    McLaughlin, S.4
  • 59
    • 0034702838 scopus 로고    scopus 로고
    • Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS
    • Arbuzova A, Wang L, Wang J, Hangyas-Mihalyne G, Murray D, Honig B, McLaughlin S. Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS. Biochemistry 2000; 39:10330-10339
    • (2000) Biochemistry , vol.39 , pp. 10330-10339
    • Arbuzova, A.1    Wang, L.2    Wang, J.3    Hangyas-Mihalyne, G.4    Murray, D.5    Honig, B.6    McLaughlin, S.7
  • 60
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • DOI 10.1038/nature04398
    • McLaughlin S, Murray D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 2005; 438:605-611 (Pubitemid 41740564)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 61
    • 15544377112 scopus 로고    scopus 로고
    • Reversible - Through calmodulin - Electrostatic interactions between basic residues on proteins and acidic lipids in the plasma membrane
    • McLaughlin S, Hangyas Mihalyne G, Zaitseva I, Golebiewska U. Reversible - through calmodulin - electrostatic interactions between basic residues on proteins and acidic lipids in the plasma membrane. Biochem Soc Symp 2005:189-198 (Pubitemid 46126852)
    • (2005) Biochemical Society Symposium , vol.72 , pp. 189-198
    • McLaughlin, S.1    Hangyas-Mihalyne, G.2    Zaitseva, I.3    Golebiewska, U.4
  • 62
    • 0030869425 scopus 로고    scopus 로고
    • Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin
    • DOI 10.1074/jbc.272.43.27167
    • Arbuzova A, Wang J, Murray D, Jacob J, Cafiso DS, McLaughlin S. Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin. J Biol Chem 1997; 272:27167-27177 (Pubitemid 27452675)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 27167-27177
    • Arbuzova, A.1    Wang, J.2    Murray, D.3    Jacob, J.4    Cafiso, D.S.5    McLaughlin, S.6
  • 63
    • 0028028022 scopus 로고
    • Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles
    • Kim J, Shishido T, Jiang X, Aderem A, McLaughlin S. Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles. J Biol Chem 1994; 269:28214-28219 (Pubitemid 24354559)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.45 , pp. 28214-28219
    • Kim, J.1    Shishido, T.2    Jiang, X.3    Aderem, A.4    McLaughlin, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.