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Volumn 21, Issue 12, 2013, Pages 2119-2130

Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; MONOMER; PHOSPHOLAMBAN; PHOSPHOLAMBAN HOMOPENTAMER; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 84889565097     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.09.008     Document Type: Article
Times cited : (39)

References (93)
  • 1
    • 33750707584 scopus 로고    scopus 로고
    • 13C solid-state NMR spectroscopic study
    • 13C solid-state NMR spectroscopic study Biochemistry 45 2006 13312 13322
    • (2006) Biochemistry , vol.45 , pp. 13312-13322
    • Abu-Baker, S.1    Lorigan, G.A.2
  • 3
    • 84866737640 scopus 로고    scopus 로고
    • Phospholamban phosphorylation increases the passive calcium leak from cardiac sarcoplasmic reticulum
    • R. Aschar-Sobbi, T.L. Emmett, G.J. Kargacin, and M.E. Kargacin Phospholamban phosphorylation increases the passive calcium leak from cardiac sarcoplasmic reticulum Pflugers Arch. 464 2012 295 305
    • (2012) Pflugers Arch. , vol.464 , pp. 295-305
    • Aschar-Sobbi, R.1    Emmett, T.L.2    Kargacin, G.J.3    Kargacin, M.E.4
  • 5
    • 84881536509 scopus 로고    scopus 로고
    • Can proton pumping by SERCA enhance the regulatory role of phospholamban and sarcolipin?
    • L. Becucci, M.L. Foresti, A. Schwan, and R. Guidelli Can proton pumping by SERCA enhance the regulatory role of phospholamban and sarcolipin? Biochim. Biophys. Acta 1828 2013 2682 2690
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2682-2690
    • Becucci, L.1    Foresti, M.L.2    Schwan, A.3    Guidelli, R.4
  • 6
    • 33847079676 scopus 로고    scopus 로고
    • Evaluating protein structures determined by structural genomics consortia
    • A. Bhattacharya, R. Tejero, and G.T. Montelione Evaluating protein structures determined by structural genomics consortia Proteins 66 2007 778 795
    • (2007) Proteins , vol.66 , pp. 778-795
    • Bhattacharya, A.1    Tejero, R.2    Montelione, G.T.3
  • 7
    • 0042069902 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies
    • B. Buck, J. Zamoon, T.L. Kirby, T.M. DeSilva, C. Karim, D. Thomas, and G. Veglia Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies Protein Expr. Purif. 30 2003 253 261
    • (2003) Protein Expr. Purif. , vol.30 , pp. 253-261
    • Buck, B.1    Zamoon, J.2    Kirby, T.L.3    Desilva, T.M.4    Karim, C.5    Thomas, D.6    Veglia, G.7
  • 8
    • 84864535546 scopus 로고    scopus 로고
    • Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A
    • D.K. Ceholski, C.A. Trieber, C.F. Holmes, and H.S. Young Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A J. Biol. Chem. 287 2012 26596 26605
    • (2012) J. Biol. Chem. , vol.287 , pp. 26596-26605
    • Ceholski, D.K.1    Trieber, C.A.2    Holmes, C.F.3    Young, H.S.4
  • 9
    • 39049174776 scopus 로고    scopus 로고
    • Beyond small molecule drugs for heart failure: Prospects for gene therapy
    • discussion 256-259, 272-276
    • K.R. Chien Beyond small molecule drugs for heart failure: prospects for gene therapy Novartis Found. Symp. 274 2006 244 256 discussion 256-259, 272-276
    • (2006) Novartis Found. Symp. , vol.274 , pp. 244-256
    • Chien, K.R.1
  • 11
    • 76749091146 scopus 로고    scopus 로고
    • (15)N solid-state NMR spectroscopic studies on phospholamban at its phosphorylated form at ser-16 in aligned phospholipid bilayers
    • S. Chu, S. Abu-Baker, J. Lu, and G.A. Lorigan (15)N solid-state NMR spectroscopic studies on phospholamban at its phosphorylated form at ser-16 in aligned phospholipid bilayers Biochim. Biophys. Acta 1798 2010 312 317
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 312-317
    • Chu, S.1    Abu-Baker, S.2    Lu, J.3    Lorigan, G.A.4
  • 12
    • 0030978470 scopus 로고    scopus 로고
    • Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers
    • R.L. Cornea, L.R. Jones, J.M. Autry, and D.D. Thomas Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers Biochemistry 36 1997 2960 2967
    • (1997) Biochemistry , vol.36 , pp. 2960-2967
    • Cornea, R.L.1    Jones, L.R.2    Autry, J.M.3    Thomas, D.D.4
  • 14
    • 0023815974 scopus 로고
    • Conformation and orientation of gramicidin a in oriented phospholipid bilayers measured by solid state carbon-13 NMR
    • B.A. Cornell, F. Separovic, A.J. Baldassi, and R. Smith Conformation and orientation of gramicidin a in oriented phospholipid bilayers measured by solid state carbon-13 NMR Biophys. J. 53 1988 67 76
    • (1988) Biophys. J. , vol.53 , pp. 67-76
    • Cornell, B.A.1    Separovic, F.2    Baldassi, A.J.3    Smith, R.4
  • 15
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • F.H.C. Crick The packing of α-helices: simple coiled-coils Acta Crystallogr. 6 1953 689 697
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 18
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • M.R. de Planque, and J.A. Killian Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring Mol. Membr. Biol. 20 2003 271 284
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 271-284
    • De Planque, M.R.1    Killian, J.A.2
  • 21
    • 0037109010 scopus 로고    scopus 로고
    • Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy
    • C. Fernández, C. Hilty, G. Wider, and K. Wüthrich Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy Proc. Natl. Acad. Sci. USA 99 2002 13533 13537
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13533-13537
    • Fernández, C.1    Hilty, C.2    Wider, G.3    Wüthrich, K.4
  • 22
    • 0006755498 scopus 로고
    • Calcium in Biological Systems
    • I. Bertini, H.B. Gray, S.J. Lippard, J.S. Valentine, University Science Books Mill Valley, CA
    • S. Forsen, and J. Kordel Calcium in Biological Systems I. Bertini, H.B. Gray, S.J. Lippard, J.S. Valentine, Bioinorganic Chemistry 1994 University Science Books Mill Valley, CA 107 166
    • (1994) Bioinorganic Chemistry , pp. 107-166
    • Forsen, S.1    Kordel, J.2
  • 23
    • 78650889008 scopus 로고    scopus 로고
    • Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump
    • J.P. Glaves, C.A. Trieber, D.K. Ceholski, D.L. Stokes, and H.S. Young Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump J. Mol. Biol. 405 2011 707 723
    • (2011) J. Mol. Biol. , vol.405 , pp. 707-723
    • Glaves, J.P.1    Trieber, C.A.2    Ceholski, D.K.3    Stokes, D.L.4    Young, H.S.5
  • 27
    • 81855192140 scopus 로고    scopus 로고
    • Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy
    • M. Gustavsson, N.J. Traaseth, and G. Veglia Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy Biochim. Biophys. Acta 1818 2012 146 153
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 146-153
    • Gustavsson, M.1    Traaseth, N.J.2    Veglia, G.3
  • 28
    • 84886402422 scopus 로고    scopus 로고
    • Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban
    • 10.1073/pnas.1303006110 Published online October 7, 2013
    • M. Gustavsson, R. Verardi, D.G. Mullen, K.R. Mote, N.J. Traaseth, T. Gopinath, and G. Veglia Allosteric regulation of SERCA by phosphorylation- mediated conformational shift of phospholamban Proc. Natl. Acad. Sci. USA 2013 10.1073/pnas.1303006110 Published online October 7, 2013
    • (2013) Proc. Natl. Acad. Sci. USA
    • Gustavsson, M.1    Verardi, R.2    Mullen, D.G.3    Mote, K.R.4    Traaseth, N.J.5    Gopinath, T.6    Veglia, G.7
  • 33
    • 57649231173 scopus 로고    scopus 로고
    • Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex
    • Z. Hou, E.M. Kelly, and S.L. Robia Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex J. Biol. Chem. 283 2008 28996 29003
    • (2008) J. Biol. Chem. , vol.283 , pp. 28996-29003
    • Hou, Z.1    Kelly, E.M.2    Robia, S.L.3
  • 34
    • 84870655957 scopus 로고    scopus 로고
    • Crystal structure of the calcium release-activated calcium channel Orai
    • X. Hou, L. Pedi, M.M. Diver, and S.B. Long Crystal structure of the calcium release-activated calcium channel Orai Science 338 2012 1308 1313
    • (2012) Science , vol.338 , pp. 1308-1313
    • Hou, X.1    Pedi, L.2    Diver, M.M.3    Long, S.B.4
  • 35
    • 33646911358 scopus 로고    scopus 로고
    • Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
    • V.A. Jarymowycz, and M.J. Stone Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences Chem. Rev. 106 2006 1624 1671
    • (2006) Chem. Rev. , vol.106 , pp. 1624-1671
    • Jarymowycz, V.A.1    Stone, M.J.2
  • 36
    • 4143111630 scopus 로고    scopus 로고
    • Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone
    • C.B. Karim, T.L. Kirby, Z. Zhang, Y. Nesmelov, and D.D. Thomas Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone Proc. Natl. Acad. Sci. USA 101 2004 14437 14442
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14437-14442
    • Karim, C.B.1    Kirby, T.L.2    Zhang, Z.3    Nesmelov, Y.4    Thomas, D.D.5
  • 38
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Y. Kimura, K. Kurzydlowski, M. Tada, and D.H. MacLennan Phospholamban inhibitory function is activated by depolymerization J. Biol. Chem. 272 1997 15061 15064
    • (1997) J. Biol. Chem. , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    Maclennan, D.H.4
  • 40
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • D.S. King, C.G. Fields, and G.B. Fields A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis Int. J. Pept. Protein Res. 36 1990 255 266
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 41
    • 0037028988 scopus 로고    scopus 로고
    • An effective method for the discrimination of motional anisotropy and chemical exchange
    • J.M. Kneller, M. Lu, and C. Bracken An effective method for the discrimination of motional anisotropy and chemical exchange J. Am. Chem. Soc. 124 2002 1852 1853
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1852-1853
    • Kneller, J.M.1    Lu, M.2    Bracken, C.3
  • 43
    • 84862286538 scopus 로고    scopus 로고
    • Modulation of cardiac contractility by the phospholamban/SERCA2a regulatome
    • E.G. Kranias, and R.J. Hajjar Modulation of cardiac contractility by the phospholamban/SERCA2a regulatome Circ. Res. 110 2012 1646 1660
    • (2012) Circ. Res. , vol.110 , pp. 1646-1660
    • Kranias, E.G.1    Hajjar, R.J.2
  • 44
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • W.H. Landschulz, P.F. Johnson, and S.L. McKnight The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins Science 240 1988 1759 1764
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 45
    • 0032568588 scopus 로고    scopus 로고
    • Phosphorylation-induced structural change in phospholamban and its mutants, detected by intrinsic fluorescence
    • M. Li, R.L. Cornea, J.M. Autry, L.R. Jones, and D.D. Thomas Phosphorylation-induced structural change in phospholamban and its mutants, detected by intrinsic fluorescence Biochemistry 37 1998 7869 7877
    • (1998) Biochemistry , vol.37 , pp. 7869-7877
    • Li, M.1    Cornea, R.L.2    Autry, J.M.3    Jones, L.R.4    Thomas, D.D.5
  • 46
    • 0041817968 scopus 로고    scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase modulates the structural coupling between the transmembrane and cytosolic domains of phospholamban
    • J. Li, D.J. Bigelow, and T.C. Squier Phosphorylation by cAMP-dependent protein kinase modulates the structural coupling between the transmembrane and cytosolic domains of phospholamban Biochemistry 42 2003 10674 10682
    • (2003) Biochemistry , vol.42 , pp. 10674-10682
    • Li, J.1    Bigelow, D.J.2    Squier, T.C.3
  • 47
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • D.H. MacLennan, and E.G. Kranias Phospholamban: a crucial regulator of cardiac contractility Nat. Rev. Mol. Cell Biol. 4 2003 566 577
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 566-577
    • Maclennan, D.H.1    Kranias, E.G.2
  • 48
    • 0018357165 scopus 로고
    • Cholesterol modulates activity of calcium-dependent ATPase of the sarcoplasmic reticulum
    • T.D. Madden, D. Chapman, and P.J. Quinn Cholesterol modulates activity of calcium-dependent ATPase of the sarcoplasmic reticulum Nature 279 1979 538 541
    • (1979) Nature , vol.279 , pp. 538-541
    • Madden, T.D.1    Chapman, D.2    Quinn, P.J.3
  • 49
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • F.M. Marassi, and S.J. Opella A solid-state NMR index of helical membrane protein structure and topology J. Magn. Reson. 144 2000 150 155
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 50
    • 84873880957 scopus 로고    scopus 로고
    • Calcium cycling proteins and heart failure: Mechanisms and therapeutics
    • A.R. Marks Calcium cycling proteins and heart failure: mechanisms and therapeutics J. Clin. Invest. 123 2013 46 52
    • (2013) J. Clin. Invest. , vol.123 , pp. 46-52
    • Marks, A.R.1
  • 51
    • 0141885396 scopus 로고    scopus 로고
    • Theoretical analysis of residual dipolar coupling patterns in regular secondary structures of proteins
    • A. Mascioni, and G. Veglia Theoretical analysis of residual dipolar coupling patterns in regular secondary structures of proteins J. Am. Chem. Soc. 125 2003 12520 12526
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12520-12526
    • Mascioni, A.1    Veglia, G.2
  • 53
    • 4143073485 scopus 로고    scopus 로고
    • 15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles
    • 15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles Biophys. J. 87 2004 1205 1214
    • (2004) Biophys. J. , vol.87 , pp. 1205-1214
    • Metcalfe, E.E.1    Zamoon, J.2    Thomas, D.D.3    Veglia, G.4
  • 54
    • 15544370248 scopus 로고    scopus 로고
    • Serine 16 phosphorylation induces an order-to-disorder transition in monomeric phospholamban
    • E.E. Metcalfe, N.J. Traaseth, and G. Veglia Serine 16 phosphorylation induces an order-to-disorder transition in monomeric phospholamban Biochemistry 44 2005 4386 4396
    • (2005) Biochemistry , vol.44 , pp. 4386-4396
    • Metcalfe, E.E.1    Traaseth, N.J.2    Veglia, G.3
  • 55
  • 56
    • 0030635055 scopus 로고    scopus 로고
    • Ambiguous distance data in the calculation of NMR structures
    • M. Nilges Ambiguous distance data in the calculation of NMR structures Fold. Des. 2 1997 S53 S57
    • (1997) Fold. Des. , vol.2
    • Nilges, M.1
  • 57
    • 23344441824 scopus 로고    scopus 로고
    • The structure of phospholamban pentamer reveals a channel-like architecture in membranes
    • K. Oxenoid, and J.J. Chou The structure of phospholamban pentamer reveals a channel-like architecture in membranes Proc. Natl. Acad. Sci. USA 102 2005 10870 10875
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.J.2
  • 58
    • 34548442113 scopus 로고    scopus 로고
    • Comparing the structure and dynamics of phospholamban pentamer in its unphosphorylated and pseudo-phosphorylated states
    • K. Oxenoid, A.J. Rice, and J.J. Chou Comparing the structure and dynamics of phospholamban pentamer in its unphosphorylated and pseudo-phosphorylated states Protein Sci. 16 2007 1977 1983
    • (2007) Protein Sci. , vol.16 , pp. 1977-1983
    • Oxenoid, K.1    Rice, A.J.2    Chou, J.J.3
  • 59
    • 35748972048 scopus 로고    scopus 로고
    • MOLE: A Voronoi diagram-based explorer of molecular channels, pores, and tunnels
    • M. Petrek, P. Kosinová, J. Koca, and M. Otyepka MOLE: a Voronoi diagram-based explorer of molecular channels, pores, and tunnels Structure 15 2007 1357 1363
    • (2007) Structure , vol.15 , pp. 1357-1363
    • Petrek, M.1    Kosinová, P.2    Koca, J.3    Otyepka, M.4
  • 60
    • 0036280798 scopus 로고    scopus 로고
    • Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17
    • P. Pollesello, and A. Annila Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17 Biophys. J. 83 2002 484 490
    • (2002) Biophys. J. , vol.83 , pp. 484-490
    • Pollesello, P.1    Annila, A.2
  • 63
    • 33846399142 scopus 로고    scopus 로고
    • E(z), a depth-dependent potential for assessing the energies of insertion of amino acid side-chains into membranes: Derivation and applications to determining the orientation of transmembrane and interfacial helices
    • A. Senes, D.C. Chadi, P.B. Law, R.F. Walters, V. Nanda, and W.F. Degrado E(z), a depth-dependent potential for assessing the energies of insertion of amino acid side-chains into membranes: derivation and applications to determining the orientation of transmembrane and interfacial helices J. Mol. Biol. 366 2007 436 448
    • (2007) J. Mol. Biol. , vol.366 , pp. 436-448
    • Senes, A.1    Chadi, D.C.2    Law, P.B.3    Walters, R.F.4    Nanda, V.5    Degrado, W.F.6
  • 64
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44 2009 213 223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 65
    • 68349122607 scopus 로고    scopus 로고
    • A refinement protocol to determine structure, topology, and depth of insertion of membrane proteins using hybrid solution and solid-state NMR restraints
    • L. Shi, N.J. Traaseth, R. Verardi, A. Cembran, J. Gao, and G. Veglia A refinement protocol to determine structure, topology, and depth of insertion of membrane proteins using hybrid solution and solid-state NMR restraints J. Biomol. NMR 44 2009 195 205
    • (2009) J. Biomol. NMR , vol.44 , pp. 195-205
    • Shi, L.1    Traaseth, N.J.2    Verardi, R.3    Cembran, A.4    Gao, J.5    Veglia, G.6
  • 66
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • H.K. Simmerman, and L.R. Jones Phospholamban: protein structure, mechanism of action, and role in cardiac function Physiol. Rev. 78 1998 921 947
    • (1998) Physiol. Rev. , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 67
    • 0029862745 scopus 로고    scopus 로고
    • A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure
    • H.K. Simmerman, Y.M. Kobayashi, J.M. Autry, and L.R. Jones A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure J. Biol. Chem. 271 1996 5941 5946
    • (1996) J. Biol. Chem. , vol.271 , pp. 5941-5946
    • Simmerman, H.K.1    Kobayashi, Y.M.2    Autry, J.M.3    Jones, L.R.4
  • 69
    • 84871879382 scopus 로고    scopus 로고
    • Structure-function relation of phospholamban: Modulation of channel activity as a potential regulator of SERCA activity
    • S. Smeazzetto, A. Saponaro, H.S. Young, M.R. Moncelli, and G. Thiel Structure-function relation of phospholamban: modulation of channel activity as a potential regulator of SERCA activity PLoS ONE 8 2013 e52744
    • (2013) PLoS ONE , vol.8 , pp. 52744
    • Smeazzetto, S.1    Saponaro, A.2    Young, H.S.3    Moncelli, M.R.4    Thiel, G.5
  • 70
    • 79958703146 scopus 로고    scopus 로고
    • Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR
    • S.K. Straus, W.R. Scott, C.D. Schwieters, and D.A. Marvin Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR Eur. Biophys. J. 40 2011 221 234
    • (2011) Eur. Biophys. J. , vol.40 , pp. 221-234
    • Straus, S.K.1    Scott, W.R.2    Schwieters, C.D.3    Marvin, D.A.4
  • 72
    • 0016689752 scopus 로고
    • Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase
    • M. Tada, M.A. Kirchberger, and A.M. Katz Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase J. Biol. Chem. 250 1975 2640 2647
    • (1975) J. Biol. Chem. , vol.250 , pp. 2640-2647
    • Tada, M.1    Kirchberger, M.A.2    Katz, A.M.3
  • 73
    • 0000953276 scopus 로고    scopus 로고
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR Chem. Phys. Lett. 344 2001 631 637
    • (2001) Chem. Phys. Lett. , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 75
    • 0026709225 scopus 로고
    • Evidence for a phosphorylation-induced conformational change in phospholamban cytoplasmic domain by CD analysis
    • E. Terzi, L. Poteur, and E. Trifilieff Evidence for a phosphorylation-induced conformational change in phospholamban cytoplasmic domain by CD analysis FEBS Lett. 309 1992 413 416
    • (1992) FEBS Lett. , vol.309 , pp. 413-416
    • Terzi, E.1    Poteur, L.2    Trifilieff, E.3
  • 78
    • 39749193522 scopus 로고    scopus 로고
    • Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy
    • N.J. Traaseth, R. Verardi, and G. Veglia Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy J. Am. Chem. Soc. 130 2008 2400 2401
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2400-2401
    • Traaseth, N.J.1    Verardi, R.2    Veglia, G.3
  • 79
    • 67649865606 scopus 로고    scopus 로고
    • Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach
    • N.J. Traaseth, L. Shi, R. Verardi, D.G. Mullen, G. Barany, and G. Veglia Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach Proc. Natl. Acad. Sci. USA 106 2009 10165 10170
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10165-10170
    • Traaseth, N.J.1    Shi, L.2    Verardi, R.3    Mullen, D.G.4    Barany, G.5    Veglia, G.6
  • 83
    • 79959340086 scopus 로고    scopus 로고
    • Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method
    • R. Verardi, L. Shi, N.J. Traaseth, N. Walsh, and G. Veglia Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method Proc. Natl. Acad. Sci. USA 108 2011 9101 9106
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 9101-9106
    • Verardi, R.1    Shi, L.2    Traaseth, N.J.3    Walsh, N.4    Veglia, G.5
  • 85
    • 84055211729 scopus 로고    scopus 로고
    • 1H solid-state NMR data for determination of transmembrane peptide orientation and dynamics
    • 1H solid-state NMR data for determination of transmembrane peptide orientation and dynamics Biophys. J. 101 2011 2939 2947
    • (2011) Biophys. J. , vol.101 , pp. 2939-2947
    • Vostrikov, V.V.1    Grant, C.V.2    Opella, S.J.3    Koeppe II, R.E.4
  • 86
    • 79958181400 scopus 로고    scopus 로고
    • Gramicidin A backbone and side chain dynamics evaluated by molecular dynamics simulations and nuclear magnetic resonance experiments. II: Nuclear magnetic resonance experiments
    • V.V. Vostrikov, H. Gu, H.I. Ingólfsson, J.F. Hinton, O.S. Andersen, B. Roux, and R.E. Koeppe 2nd Gramicidin A backbone and side chain dynamics evaluated by molecular dynamics simulations and nuclear magnetic resonance experiments. II: nuclear magnetic resonance experiments J. Phys. Chem. B 115 2011 7427 7432
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7427-7432
    • Vostrikov, V.V.1    Gu, H.2    Ingólfsson, H.I.3    Hinton, J.F.4    Andersen, O.S.5    Roux, B.6    Koeppe II, R.E.7
  • 87
    • 0028152571 scopus 로고
    • 2D and 3D NMR study of phenylalanine residues in proteins by reverse isotopic labeling
    • W.V. Vuister, S.-J. Kim, C. Wu, and A. Bax 2D and 3D NMR study of phenylalanine residues in proteins by reverse isotopic labeling J. Am. Chem. Soc. 116 1994 9206 9210
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9206-9210
    • Vuister, W.V.1    Kim, S.-J.2    Wu, C.3    Bax, A.4
  • 88
  • 90
    • 0021350781 scopus 로고
    • Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels. Evidence for a protein structure consisting of multiple identical phosphorylatable subunits
    • A.D. Wegener, and L.R. Jones Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels. Evidence for a protein structure consisting of multiple identical phosphorylatable subunits J. Biol. Chem. 259 1984 1834 1841
    • (1984) J. Biol. Chem. , vol.259 , pp. 1834-1841
    • Wegener, A.D.1    Jones, L.R.2
  • 91
    • 33846595904 scopus 로고
    • High-resolution heteronuclear dipolar solid-state NMR spectroscopy
    • C.H. Wu, A. Ramamoorthy, and S.J. Opella High-resolution heteronuclear dipolar solid-state NMR spectroscopy J. Magn. Reson. A 109 1994 270 272
    • (1994) J. Magn. Reson. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 92
    • 0037093639 scopus 로고    scopus 로고
    • Structural analysis, identification, and design of calcium-binding sites in proteins
    • W. Yang, H.W. Lee, H. Hellinga, and J.J. Yang Structural analysis, identification, and design of calcium-binding sites in proteins Proteins 47 2002 344 356
    • (2002) Proteins , vol.47 , pp. 344-356
    • Yang, W.1    Lee, H.W.2    Hellinga, H.3    Yang, J.J.4
  • 93
    • 0141530952 scopus 로고    scopus 로고
    • NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles
    • J. Zamoon, A. Mascioni, D.D. Thomas, and G. Veglia NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles Biophys. J. 85 2003 2589 2598
    • (2003) Biophys. J. , vol.85 , pp. 2589-2598
    • Zamoon, J.1    Mascioni, A.2    Thomas, D.D.3    Veglia, G.4


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