메뉴 건너뛰기




Volumn , Issue , 2011, Pages 121-151

Single-protein dynamics and the regulation of the plasma-membrane Ca 2+ pump

Author keywords

ATPase; Autoinhibitory domain; Burst measurements; Calmodulin (CaM); FRET; Maximum likelihood; Modulation depth; Oxidative modification; Plasma membrane Ca2+ ATPase (PMCA); Polarization modulation

Indexed keywords


EID: 84867771398     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-90-481-9864-1_6     Document Type: Chapter
Times cited : (1)

References (85)
  • 1
    • 62149088950 scopus 로고    scopus 로고
    • Plasma membrane Ca2+-ATPase: From a housekeeping function to a versatile signaling role
    • Brini M (2009) Plasma membrane Ca2+-ATPase: From a housekeeping function to a versatile signaling role. Pflugers Arch 457:657-664
    • (2009) Pflugers Arch , vol.457 , pp. 657-664
    • Brini, M.1
  • 2
    • 47049102553 scopus 로고    scopus 로고
    • The plasma membrane Ca2+ ATPase of animal cells: Structure, function and regulation
    • Di Leva F, Domi T, Fedrizzi L, Lim D, Carafoli E (2008) The plasma membrane Ca2+ ATPase of animal cells: Structure, function and regulation. Arch Biochem Biophys 476(1):65-74
    • (2008) Arch Biochem Biophys , vol.476 , Issue.1 , pp. 65-74
    • Di Leva, F.1    Domi, T.2    Fedrizzi, L.3    Lim, D.4    Carafoli, E.5
  • 6
    • 2042531806 scopus 로고    scopus 로고
    • How do P-Type ATPases transport ions?
    • Apell HJ (2004) How do P-Type ATPases transport ions?. Bioelectrochemistry 63:149-156
    • (2004) Bioelectrochemistry , vol.63 , pp. 149-156
    • Apell, H.J.1
  • 7
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin D, Means AR (2000) Calmodulin: A prototypical calcium sensor. Trends Cell Biol 10:322-328
    • (2000) Trends Cell Biol , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 9
    • 84943234840 scopus 로고    scopus 로고
    • Calmodulin-mediated signaling
    • Means AR (2004) Calmodulin-mediated signaling. Handbook Cell Signal 2:83-85
    • (2004) Handbook Cell Signal , vol.2 , pp. 83-85
    • Means, A.R.1
  • 10
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich KP, Ikura M (2002) Calmodulin in action: Diversity in target recognition and activation mechanisms. Cell 108:739-742
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 11
    • 0031938735 scopus 로고    scopus 로고
    • An interaction-based analysis of calcium-induced conformational changes in Ca2+ sensor proteins
    • Nelson MR, Chazin WJ (1998) An interaction-based analysis of calcium-induced conformational changes in Ca2+ sensor proteins. Protein Sci 7:270-282
    • (1998) Protein Sci , vol.7 , pp. 270-282
    • Nelson, M.R.1    Chazin, W.J.2
  • 12
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang M, Tanaka T, Ikura M (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat Struct Biol 2:758-767
    • (1995) Nat Struct Biol , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 13
    • 0037022309 scopus 로고    scopus 로고
    • Calcium signaling: A tale for all seasons
    • Carafoli E (2002) Calcium signaling: A tale for all seasons. Proc Natl Acad Sci USA 99:1115-1122
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1115-1122
    • Carafoli, E.1
  • 14
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2 2 A resolution
    • Babu YS, Bugg CE, Cook WJ (1988) Structure of calmodulin refined at 2.2 A resolution. J Mol Biol 204:191-204
    • (1988) J Mol Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 15
    • 0141594755 scopus 로고    scopus 로고
    • A closed compact structure of native Ca2+-calmodulin
    • Fallon JL, Quiocho FA (2003) A closed compact structure of native Ca2+-calmodulin. Structure 11:1303-1307
    • (2003) Structure , vol.11 , pp. 1303-1307
    • Fallon, J.L.1    Quiocho, F.A.2
  • 17
    • 33845261364 scopus 로고    scopus 로고
    • Calmodulin, conformational states, and calcium signaling A singlemolecule perspective
    • Johnson CK (2006) Calmodulin, conformational states, and calcium signaling. A singlemolecule perspective. Biochemistry 45:14233-14246
    • (2006) Biochemistry , vol.45 , pp. 14233-14246
    • Johnson, C.K.1
  • 18
    • 0017670545 scopus 로고
    • Phosphodiesterase protein activator mimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPase
    • Gopinath RM, Vincenzi FF (1977) Phosphodiesterase protein activator mimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPase. Biochem Biophys Res Commun 77:1203-1209
    • (1977) Biochem Biophys Res Commun , vol.77 , pp. 1203-1209
    • Gopinath, R.M.1    Vincenzi, F.F.2
  • 19
    • 0017622160 scopus 로고
    • Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: Its similarity to the activator of 30:50-cyclic nucleotide phosphodiesterase
    • Jarrett HW, Penniston JT (1977) Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: Its similarity to the activator of 30:50-cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun 77:1210-1216
    • (1977) Biochem Biophys Res Commun , vol.77 , pp. 1210-1216
    • Jarrett, H.W.1    Penniston, J.T.2
  • 20
    • 0023872238 scopus 로고
    • Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes
    • James P, Maeda M, Fischer R, Verma AK, Krebs J, Penniston JT, Carafoli E (1988) Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes. J Biol Chem 263:2905-2910
    • (1988) J Biol Chem , vol.263 , pp. 2905-2910
    • James, P.1    Maeda, M.2    Fischer, R.3    Verma, A.K.4    Krebs, J.5    Penniston, J.T.6    Carafoli, E.7
  • 21
    • 0024361269 scopus 로고
    • The calmodulin binding domain of the plasma membrane Ca2+ pump interacts both with calmodulin and with another part of the pump
    • Enyedi A, Vorherr T, James P, McCormick DJ, Filoteo AG, Carafoli E, Penniston JT (1989) The calmodulin binding domain of the plasma membrane Ca2+ pump interacts both with calmodulin and with another part of the pump. J Biol Chem 264:12313-12321
    • (1989) J Biol Chem , vol.264 , pp. 12313-12321
    • Enyedi, A.1    Vorherr, T.2    James, P.3    McCormick, D.J.4    Filoteo, A.G.5    Carafoli, E.6    Penniston, J.T.7
  • 22
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler EE, Zacharias DA (2001) Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol Rev 81:21-50
    • (2001) Physiol Rev , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 24
    • 36749035512 scopus 로고    scopus 로고
    • Plasma-membrane Ca2+ pumps: Structural diversity as the basis for functional versatility
    • Strehler EE, Filoteo AG, Penniston JT, Caride AJ (2007) Plasma-membrane Ca2+ pumps: Structural diversity as the basis for functional versatility. Biochem Soc Trans 35:919-922
    • (2007) Biochem Soc Trans , vol.35 , pp. 919-922
    • Strehler, E.E.1    Filoteo, A.G.2    Penniston, J.T.3    Caride, A.J.4
  • 25
    • 0034956470 scopus 로고    scopus 로고
    • Delayed activation of the plasma membrane calcium pump by a sudden increase in Ca2+: Fast pumps reside in fast cells
    • Caride AJ, Filoteo AG, Penheiter AR, Paszty K, Enyedi A, Penniston JT (2001) Delayed activation of the plasma membrane calcium pump by a sudden increase in Ca2+: Fast pumps reside in fast cells. Cell Calcium 30:49-57
    • (2001) Cell Calcium , vol.30 , pp. 49-57
    • Caride, A.J.1    Filoteo, A.G.2    Penheiter, A.R.3    Paszty, K.4    Enyedi, A.5    Penniston, J.T.6
  • 26
    • 0029013891 scopus 로고
    • Tissue distribution of the four gene products of the plasma membrane Ca2+ pump
    • Stauffer TP, Guerini D, Carafoli E (1995) Tissue distribution of the four gene products of the plasma membrane Ca2+ pump. J Biol Chem 270:12184-12190
    • (1995) J Biol Chem , vol.270 , pp. 12184-12190
    • Stauffer, T.P.1    Guerini, D.2    Carafoli, E.3
  • 27
    • 0030610570 scopus 로고    scopus 로고
    • Plasma membrane Ca2+ pump isoforms 2a and 2b are unusually responsive to calmodulin and Ca2+
    • Elwess NL, Filoteo AG, Enyedi A, Penniston JT (1997) Plasma membrane Ca2+ pump isoforms 2a and 2b are unusually responsive to calmodulin and Ca2+. J Biol Chem 272:17981-17986
    • (1997) J Biol Chem , vol.272 , pp. 17981-17986
    • Elwess, N.L.1    Filoteo, A.G.2    Enyedi, A.3    Penniston, J.T.4
  • 29
    • 0033520919 scopus 로고    scopus 로고
    • The rate of activation by calmodulin of isoform 4 of the plasma membrane Ca2+ pump is slow and is changed by alternative splicing
    • Caride AJ, Elwess NL, Verma AK, Filoteo AG, Enyedi A, Bajzer Z, Penniston JT (1999) The rate of activation by calmodulin of isoform 4 of the plasma membrane Ca2+ pump is slow and is changed by alternative splicing. J Biol Chem 274:35227-35232
    • (1999) J Biol Chem , vol.274 , pp. 35227-35232
    • Caride, A.J.1    Elwess, N.L.2    Verma, A.K.3    Filoteo, A.G.4    Enyedi, A.5    Bajzer, Z.6    Penniston, J.T.7
  • 30
    • 0035955671 scopus 로고    scopus 로고
    • The plasma membrane calcium pump displays memory of past calcium spikes. Differences between isoforms 2b and 4b
    • Caride AJ, Penheiter AR, Filoteo AG, Bajzer Z, Enyedi A, Penniston JT (2001) The plasma membrane calcium pump displays memory of past calcium spikes. Differences between isoforms 2b and 4b. J Biol Chem 276:39797-39804
    • (2001) J Biol Chem , vol.276 , pp. 39797-39804
    • Caride, A.J.1    Penheiter, A.R.2    Filoteo, A.G.3    Bajzer, Z.4    Enyedi, A.5    Penniston, J.T.6
  • 31
    • 34347216391 scopus 로고    scopus 로고
    • Partitioning of the plasma membrane Ca2+-ATPase into lipid rafts in primary neurons: Effects of cholesterol depletion
    • Jiang L, Fernandes D, Mehta N, Bean JL, Michaelis ML, Zaidi A (2007) Partitioning of the plasma membrane Ca2+-ATPase into lipid rafts in primary neurons: Effects of cholesterol depletion. J Neurochem 102:378-388
    • (2007) J Neurochem , vol.102 , pp. 378-388
    • Jiang, L.1    Fernandes, D.2    Mehta, N.3    Bean, J.L.4    Michaelis, M.L.5    Zaidi, A.6
  • 32
    • 33644850532 scopus 로고    scopus 로고
    • The plasma membrane Ca2 +-ATPase isoform 4 is localized in lipid rafts of cerebellum synaptic plasma membranes
    • Sepulveda MR, Berrocal-Carrillo M, Gasset M, Mata AM (2006) The plasma membrane Ca2 +-ATPase isoform 4 is localized in lipid rafts of cerebellum synaptic plasma membranes. J Biol Chem 281:447-453
    • (2006) J Biol Chem , vol.281 , pp. 447-453
    • Sepulveda, M.R.1    Berrocal-Carrillo, M.2    Gasset, M.3    Mata, A.M.4
  • 33
    • 47049101464 scopus 로고    scopus 로고
    • Structural aspects of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum
    • Toyoshima C (2008) Structural aspects of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum. Arch Biochem Biophys 476:3-11
    • (2008) Arch Biochem Biophys , vol.476 , pp. 3-11
    • Toyoshima, C.1
  • 35
    • 0023654685 scopus 로고
    • The ATP-binding site of the erythrocyte membrane Ca2+ pump
    • Filoteo AG, Gorski JP, Penniston JT (1987) The ATP-binding site of the erythrocyte membrane Ca2+ pump. J Biol Chem 262:6526-6530
    • (1987) J Biol Chem , vol.262 , pp. 6526-6530
    • Filoteo, A.G.1    Gorski, J.P.2    Penniston, J.T.3
  • 36
    • 0029887537 scopus 로고    scopus 로고
    • The plasma membrane Ca2+ pump mutant lysine591! arginine retains some activity, but is still inactivated by fluorescein isothiocyanate
    • Adamo HP, Filoteo AG, Penniston JT (1996) The plasma membrane Ca2+ pump mutant lysine591! arginine retains some activity, but is still inactivated by fluorescein isothiocyanate. Biochem J 317:41-44
    • (1996) Biochem J , vol.317 , pp. 41-44
    • Adamo, H.P.1    Filoteo, A.G.2    Penniston, J.T.3
  • 37
    • 1642497604 scopus 로고    scopus 로고
    • Fluorescence labeling, purification and immobilization of a double cysteine mutant calmodulin fusion protein for single-molecule experiments
    • Allen MW, Urbauer RJB, Zaidi A, Williams TD, Urbauer JL, Johnson CK (2004) Fluorescence labeling, purification and immobilization of a double cysteine mutant calmodulin fusion protein for single-molecule experiments. Anal Biochem 325:273-284
    • (2004) Anal Biochem , vol.325 , pp. 273-284
    • Allen, M.W.1    Urbauer, R.J.B.2    Zaidi, A.3    Williams, T.D.4    Urbauer, J.L.5    Johnson, C.K.6
  • 38
    • 0141683490 scopus 로고    scopus 로고
    • Maximum likelihood approach to single-molecule polarization modulation analysis
    • Osborn KD, Singh MK, Urbauer RJB, Johnson CK (2003) Maximum likelihood approach to single-molecule polarization modulation analysis. ChemPhysChem 4:1005-1011
    • (2003) ChemPhysChem , vol.4 , pp. 1005-1011
    • Osborn, K.D.1    Singh, M.K.2    Urbauer, R.J.B.3    Johnson, C.K.4
  • 39
    • 4444342810 scopus 로고    scopus 로고
    • Single-molecule dynamics of the calcium-dependent activation of plasma-membrane Ca2+-ATPase by calmodulin
    • Osborn KD, Zaidi A, Mandal A, Urbauer RJB, Johnson CK (2004) Single-molecule dynamics of the calcium-dependent activation of plasma-membrane Ca2+-ATPase by calmodulin. Biophys J 87:1892-1899
    • (2004) Biophys J , vol.87 , pp. 1892-1899
    • Osborn, K.D.1    Zaidi, A.2    Mandal, A.3    Urbauer, R.J.B.4    Johnson, C.K.5
  • 40
    • 0001594854 scopus 로고    scopus 로고
    • Quantitative identification of different single molecules by selective time-resolved confocal fluorescence spectroscopy
    • Fries JR, Brand L, Eggeling C, Kollner M, Seidel CAM (1998) Quantitative identification of different single molecules by selective time-resolved confocal fluorescence spectroscopy. J Phys Chem A 102:6601-6613
    • (1998) J Phys Chem A , vol.102 , pp. 6601-6613
    • Fries, J.R.1    Brand, L.2    Eggeling, C.3    Kollner, M.4    Seidel, C.A.M.5
  • 43
    • 0018654140 scopus 로고
    • Purification of the (Ca2+-Mg2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column
    • Niggli V, Penniston JT, Carafoli E (1979) Purification of the (Ca2+-Mg2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column. J Biol Chem 254:9955-9958
    • (1979) J Biol Chem , vol.254 , pp. 9955-9958
    • Niggli, V.1    Penniston, J.T.2    Carafoli, E.3
  • 46
    • 0019876575 scopus 로고
    • Purified (Ca2+-Mg2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids
    • Niggli V, Adunyah ES, Penniston JT, Carafoli E (1981) Purified (Ca2+-Mg2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids. J Biol Chem 256:395-401
    • (1981) J Biol Chem , vol.256 , pp. 395-401
    • Niggli, V.1    Adunyah, E.S.2    Penniston, J.T.3    Carafoli, E.4
  • 47
    • 0027979136 scopus 로고
    • Regulatory region of plasma membrane Ca2+ pump. 28 residues suffice to bind calmodulin but more are needed for full auto-inhibition of the activity
    • Verma AK, Enyedi A, Filoteo AG, Penniston JT (1994) Regulatory region of plasma membrane Ca2+ pump. 28 residues suffice to bind calmodulin but more are needed for full auto-inhibition of the activity. J Biol Chem 269:1687-1691
    • (1994) J Biol Chem , vol.269 , pp. 1687-1691
    • Verma, A.K.1    Enyedi, A.2    Filoteo, A.G.3    Penniston, J.T.4
  • 48
    • 3042778233 scopus 로고    scopus 로고
    • Single-molecule assays of calmodulin target binding detected with a calmodulin energy-Transfer construct
    • Allen MW, Bieber Urbauer RJ, Johnson CK (2004) Single-molecule assays of calmodulin target binding detected with a calmodulin energy-Transfer construct. Anal Chem 76:3630-3637
    • (2004) Anal Chem , vol.76 , pp. 3630-3637
    • Allen, M.W.1    Bieber Urbauer, R.J.2    Johnson, C.K.3
  • 49
    • 34047224081 scopus 로고    scopus 로고
    • Mechanism of calmodulin recognition of the binding domain of isoform 1b of the plasma membrane Ca2+-ATPase: Kinetic pathway and effects of methionine oxidation
    • Slaughter BD, Urbauer RJ, Urbauer JL, Johnson CK (2007) Mechanism of calmodulin recognition of the binding domain of isoform 1b of the plasma membrane Ca2+-ATPase: Kinetic pathway and effects of methionine oxidation. Biochemistry 46:4045-4054
    • (2007) Biochemistry , vol.46 , pp. 4045-4054
    • Slaughter, B.D.1    Urbauer, R.J.2    Urbauer, J.L.3    Johnson, C.K.4
  • 51
    • 0029809047 scopus 로고    scopus 로고
    • Dynamic structure of the calmodulin-binding domain of the plasma membrane Ca-ATPase in native erythrocyte ghost membranes
    • Yao Y, Gao J, Squier TC (1996) Dynamic structure of the calmodulin-binding domain of the plasma membrane Ca-ATPase in native erythrocyte ghost membranes. Biochemistry 35:12015-12028
    • (1996) Biochemistry , vol.35 , pp. 12015-12028
    • Yao, Y.1    Gao, J.2    Squier, T.C.3
  • 53
    • 0026658959 scopus 로고
    • Binding of calcium by calmodulin: Influence of the calmodulin binding domain of the plasma membrane calcium pump
    • Yazawa M, Vorherr T, James P, Carafoli E, Yagi K (1992) Binding of calcium by calmodulin: Influence of the calmodulin binding domain of the plasma membrane calcium pump. Biochemistry 31:3171-3176
    • (1992) Biochemistry , vol.31 , pp. 3171-3176
    • Yazawa, M.1    Vorherr, T.2    James, P.3    Carafoli, E.4    Yagi, K.5
  • 55
    • 0035116209 scopus 로고    scopus 로고
    • ATP analogues at a glance
    • Bagshaw C (2001) ATP analogues at a glance. J Cell Sci 114:459-460
    • (2001) J Cell Sci , vol.114 , pp. 459-460
    • Bagshaw, C.1
  • 56
    • 0025327915 scopus 로고
    • Magnesium-ions accelerate the formation of the phosphoenzyme of the (Ca2++Mg2+)-Activated ATPase from plasma membranes by acting on the phosphorylation reaction
    • Adamo HP, Rega AF, Garrahan PJ (1990) Magnesium-ions accelerate the formation of the phosphoenzyme of the (Ca2++Mg2+)-Activated ATPase from plasma membranes by acting on the phosphorylation reaction. Biochem Biophys Res Commun 169:700-705
    • (1990) Biochem Biophys Res Commun , vol.169 , pp. 700-705
    • Adamo, H.P.1    Rega, A.F.2    Garrahan, P.J.3
  • 57
    • 0029913253 scopus 로고    scopus 로고
    • Pre-steady-state kinetic study of the effects of K+ on the partial reactions of the catalytic cycle of the plasma membrane Ca2+-ATPase
    • Herscher CJ, Rega AF, Adamo HP (1996) Pre-steady-state kinetic study of the effects of K+ on the partial reactions of the catalytic cycle of the plasma membrane Ca2+-ATPase. Biochem J 315:673-677
    • (1996) Biochem J , vol.315 , pp. 673-677
    • Herscher, C.J.1    Rega, A.F.2    Adamo, H.P.3
  • 58
    • 0025922159 scopus 로고
    • The plasma membrane Ca2+ pump contains a site that interacts with its calmodulin-binding domain
    • Falchetto R, Vorherr T, Brunner J, Carafoli E (1991) The plasma membrane Ca2+ pump contains a site that interacts with its calmodulin-binding domain. J Biol Chem 266:2930-2936
    • (1991) J Biol Chem , vol.266 , pp. 2930-2936
    • Falchetto, R.1    Vorherr, T.2    Brunner, J.3    Carafoli, E.4
  • 59
    • 0027069575 scopus 로고
    • The calmodulin-binding site of the plasma membrane Ca2+ pump interacts with the transduction Domain of the enzyme
    • Falchetto R, Vorherr T, Carafoli E (1992) The calmodulin-binding site of the plasma membrane Ca2+ pump interacts with the transduction Domain of the enzyme. Protein Sci 1:1613-1621
    • (1992) Protein Sci , vol.1 , pp. 1613-1621
    • Falchetto, R.1    Vorherr, T.2    Carafoli, E.3
  • 60
    • 10744228658 scopus 로고    scopus 로고
    • Oxidative inactivation of purified plasma membrane Ca2+-ATPase by hydrogen peroxide and protection by calmodulin
    • Zaidi A, Barron L, Sharov VS, Schoneich C, Michaelis EK, Michaelis ML (2003) Oxidative inactivation of purified plasma membrane Ca2+-ATPase by hydrogen peroxide and protection by calmodulin. Biochemistry 42:12001-12010
    • (2003) Biochemistry , vol.42 , pp. 12001-12010
    • Zaidi, A.1    Barron, L.2    Sharov, V.S.3    Schoneich, C.4    Michaelis, E.K.5    Michaelis, M.L.6
  • 61
    • 0035066857 scopus 로고    scopus 로고
    • Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex
    • Gao J, Yao Y, Squier TC (2001) Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex. Biophys J 80:1791-1801
    • (2001) Biophys J , vol.80 , pp. 1791-1801
    • Gao, J.1    Yao, Y.2    Squier, T.C.3
  • 62
    • 12844257477 scopus 로고    scopus 로고
    • Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins
    • Bigelow DJ, Squier TC (2005) Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins. Biochim Biophys Acta 1703:121-134
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 121-134
    • Bigelow, D.J.1    Squier, T.C.2
  • 63
    • 0032830131 scopus 로고    scopus 로고
    • Effects of reactive oxygen species on brain synamptic plasma membrane Ca2+-ATPase
    • Zaidi A, Michaelis ML (1999) Effects of reactive oxygen species on brain synamptic plasma membrane Ca2+-ATPase. Free Radical Biol Med 27:810-821
    • (1999) Free Radical Biol Med , vol.27 , pp. 810-821
    • Zaidi, A.1    Michaelis, M.L.2
  • 64
    • 70350028692 scopus 로고    scopus 로고
    • Effects of paraquat-induced oxidative stress on the neuronal plasma membrane Ca2+-ATPase
    • Zaidi A, Fernandes D, Bean JL, Michaelis ML (2009) Effects of paraquat-induced oxidative stress on the neuronal plasma membrane Ca2+-ATPase. Free Radic Biol Med 47:1507-1514
    • (2009) Free Radic Biol Med , vol.47 , pp. 1507-1514
    • Zaidi, A.1    Fernandes, D.2    Bean, J.L.3    Michaelis, M.L.4
  • 65
    • 0032437456 scopus 로고    scopus 로고
    • Age-related decrease in brain synaptic membrane Ca2+-ATPase in F344/BNF1 rats
    • Zaidi A, Gao J, Squier TC, Michaelis ML (1998) Age-related decrease in brain synaptic membrane Ca2+-ATPase in F344/BNF1 rats. Neurobiol Aging 19:487-495
    • (1998) Neurobiol Aging , vol.19 , pp. 487-495
    • Zaidi, A.1    Gao, J.2    Squier, T.C.3    Michaelis, M.L.4
  • 66
    • 0032538805 scopus 로고    scopus 로고
    • Decrease in Ca-ATPase activity in aged synaptosomal membranes is not associated with changes in fatty acyl chain Dynamics
    • Qin Z, Zaidi A, Gao J, Krainev AG, Michaelis ML, Squier TC, Bigelow DJ (1998) Decrease in Ca-ATPase activity in aged synaptosomal membranes is not associated with changes in fatty acyl chain Dynamics. Mech Ageing Dev 105:291-300
    • (1998) Mech Ageing Dev , vol.105 , pp. 291-300
    • Qin, Z.1    Zaidi, A.2    Gao, J.3    Krainev, A.G.4    Michaelis, M.L.5    Squier, T.C.6    Bigelow, D.J.7
  • 67
    • 21844479556 scopus 로고    scopus 로고
    • Mediating molecular recognition by methionine oxidation: Conformational switching by oxidation of methionine in the carboxyl-Terminal domain of calmodulin
    • Anbanandam A, Bieber Urbauer RJ, Bartlett RK, Smallwood HS, Squier TC, Urbauer JL (2005) Mediating molecular recognition by methionine oxidation: Conformational switching by oxidation of methionine in the carboxyl-Terminal domain of calmodulin. Biochemistry 44:9486-9496
    • (2005) Biochemistry , vol.44 , pp. 9486-9496
    • Anbanandam, A.1    Bieber Urbauer, R.J.2    Bartlett, R.K.3    Smallwood, H.S.4    Squier, T.C.5    Urbauer, J.L.6
  • 68
  • 69
    • 4944253793 scopus 로고    scopus 로고
    • Single-molecule dynamics reveal an altered conformation for the autoinhibitory domain of plasma-membrane Ca2+-ATPase bound to oxidatively modified calmodulin
    • Osborn KD, Bartlett RK, Mandal A, Zaidi A, Urbauer RJB, Urbauer JL, Galeva N, Williams TD, Johnson CK (2004) Single-molecule dynamics reveal an altered conformation for the autoinhibitory domain of plasma-membrane Ca2+-ATPase bound to oxidatively modified calmodulin. Biochemistry 43:12937-12944
    • (2004) Biochemistry , vol.43 , pp. 12937-12944
    • Osborn, K.D.1    Bartlett, R.K.2    Mandal, A.3    Zaidi, A.4    Urbauer, R.J.B.5    Urbauer, J.L.6    Galeva, N.7    Williams, T.D.8    Johnson, C.K.9
  • 70
    • 23944485408 scopus 로고    scopus 로고
    • Single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified plasma-membrane Ca2+-ATPase
    • Osborn KD, Zaidi A, Urbauer RJB, Michaelis ML, Johnson CK (2005) Single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified plasma-membrane Ca2+-ATPase. Biochemistry 44:11074-11081
    • (2005) Biochemistry , vol.44 , pp. 11074-11081
    • Osborn, K.D.1    Zaidi, A.2    Urbauer, R.J.B.3    Michaelis, M.L.4    Johnson, C.K.5
  • 71
    • 57749172724 scopus 로고    scopus 로고
    • Fluorescence polarization assay for calmodulin binding to plasma membrane Ca2+-ATPase: Dependence on enzyme and Ca2+ concentrations
    • Liyanage MR, Zaidi A, Johnson CK (2009) Fluorescence polarization assay for calmodulin binding to plasma membrane Ca2+-ATPase: Dependence on enzyme and Ca2+ concentrations. Anal Biochem 385:1-6
    • (2009) Anal Biochem , vol.385 , pp. 1-6
    • Liyanage, M.R.1    Zaidi, A.2    Johnson, C.K.3
  • 74
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • Selvin PR (1995) Fluorescence resonance energy transfer. Methods Enzymol 246:300-334
    • (1995) Methods Enzymol , vol.246 , pp. 300-334
    • Selvin, P.R.1
  • 75
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: Fluorescence resonance energy transfer between a single donor and a single acceptor
    • Ha T, Enderle T, Ogletree DF, Chemla DS, Selvin PR, Weiss S (1996) Probing the interaction between two single molecules: Fluorescence resonance energy transfer between a single donor and a single acceptor. Proc Natl Acad Sci USA 93:6264-6268
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6264-6268
    • Ha, T.1    Enderle, T.2    Ogletree, D.F.3    Chemla, D.S.4    Selvin, P.R.5    Weiss, S.6
  • 76
    • 0033616580 scopus 로고    scopus 로고
    • Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Förster distance dependence and subpopulations
    • Deniz AA, Dahan M, Grunwell JR, Ha T, Faulhaber AE, Chemla DS, Weiss S, Schultz PG (1999) Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Förster distance dependence and subpopulations. Proc Natl Acad Sci USA 96:3670-3675
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3670-3675
    • Deniz, A.A.1    Dahan, M.2    Grunwell, J.R.3    Ha, T.4    Faulhaber, A.E.5    Chemla, D.S.6    Weiss, S.7    Schultz, P.G.8
  • 77
    • 0033813064 scopus 로고    scopus 로고
    • Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy
    • Weiss S (2000) Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy. Nature Struct Biol 7:724-729
    • (2000) Nature Struct Biol , vol.7 , pp. 724-729
    • Weiss, S.1
  • 78
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • Schuler B, Lipman EA, Eaton WA (2002) Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature 419:743-747
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 79
    • 0034807927 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonance energy transfer
    • Ha T (2001) Single-molecule fluorescence resonance energy transfer. Methods 25:78-86
    • (2001) Methods , vol.25 , pp. 78-86
    • Ha, T.1
  • 81
    • 3442896792 scopus 로고    scopus 로고
    • Single-molecule resonance energy transfer and fluorescence correlation spectroscopy of calmodulin in solution
    • Slaughter BD, Allen MW, Unruh JR, Urbauer RJB, Johnson CK (2004) Single-molecule resonance energy transfer and fluorescence correlation spectroscopy of calmodulin in solution. J Phys Chem B 108:10388-10397
    • (2004) J Phys Chem B , vol.108 , pp. 10388-10397
    • Slaughter, B.D.1    Allen, M.W.2    Unruh, J.R.3    Urbauer, R.J.B.4    Johnson, C.K.5
  • 82
  • 84
    • 0037124082 scopus 로고    scopus 로고
    • Tryptophan 1093 is largely responsible for the slow off rate of calmodulin from plasma membrane Ca2+ pump 4b
    • Penheiter AR, Caride AJ, Enyedi A, Penniston JT (2002) Tryptophan 1093 is largely responsible for the slow off rate of calmodulin from plasma membrane Ca2+ pump 4b. J Biol Chem 277:17728-17732
    • (2002) J Biol Chem , vol.277 , pp. 17728-17732
    • Penheiter, A.R.1    Caride, A.J.2    Enyedi, A.3    Penniston, J.T.4
  • 85
    • 39549094442 scopus 로고    scopus 로고
    • Interchange of autoinhibitory domain conformations in plasma-membrane Ca2+-ATPase-calmodulin complexes
    • Mandal A, Liyanage MR, Zaidi A, Johnson CK (2008) Interchange of autoinhibitory domain conformations in plasma-membrane Ca2+-ATPase-calmodulin complexes. Protein Sci 17:555-562
    • (2008) Protein Sci , vol.17 , pp. 555-562
    • Mandal, A.1    Liyanage, M.R.2    Zaidi, A.3    Johnson, C.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.