DOI: 10.1006/jmbi.2000.3885. Use of a New Label, 13C18O, in the Determination of a Structural Model of Phospholamban in a Lipid Bilayer. Spatial Restraints Resolve the Ambiguity Arising from Interpretations of Mutagenesis Data

Use of a New Label, 13C18O, in the Determination of a Structural Model of Phospholamban in a Lipid Bilayer. Spatial Restraints Resolve the Ambiguity Arising from Interpretations of Mutagenesis Data

10.1006/jmbi.2000.3885

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Torres, J., Adams, P. D., & Arkin, I. T. (2000). Use of a New Label, 13Cî»18O, in the Determination of a Structural Model of Phospholamban in a Lipid Bilayer. Spatial Restraints Resolve the Ambiguity Arising from Interpretations of Mutagenesis Data. Journal of Molecular Biology, 300(4), 677â685.

Authors 3

Jaume Torres (first)
Paul D. Adams (additional)
Isaiah T. Arkin (additional)

References 32 Referenced 87

10.1038/nsb0295-154 / Nature Struct. Biol. / Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban by Adams (1995)
10.1002/j.1460-2075.1994.tb06801.x / EMBO J. / Structural organization of the pentameric transmembrane alpha-helices of phospholamban, a cardiac ion chann by Arkin (1994)
10.1146/annurev.biophys.26.1.157 / Annu. Rev. Biophys. Biomol. Struct. / Structural perspectives of phospholamban, a helical transmembrane pentamer by Arkin (1997)
10.1021/ja964253x / J. Am. Chem. Soc. / Site-directed dichroism as a method for obtaining rotational and orientational constraints for oriented polymers by Arkin (1997)
10.1038/nsb0396-240 / Nature Struct. Biol. / Mapping the lipid-exposed surfaces of membrane proteins by Arkin (1996)
10.1006/jmbi.1995.0263 / J. Mol. Biol. / Structural model of the phospholamban ion channel complex in phospholipid membranes by Arkin (1995)
10.1074/jbc.272.25.15872 / J. Biol. Chem. / Functional co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation by Autry (1997)
10.1107/S0907444998003254 / Acta Crystallog. sect. D / Crystallography and NMR system: a new software system for macromolecular structure determination by Brünger (1998)
10.1002/bip.360250307 / Biopolymers / Examination of the secondary structure of proteins by deconvolved FTIR spectra by Byler (1986)
10.1161/01.RES.81.4.485 / Circ Res. / Monomeric phospholamban overexpression in transgenic mouse hearts by Chu (1997)
10.1074/jbc.273.50.33674 / J. Biol. Chem. / Pentameric assembly of phospholamban facilitates inhibition of cardiac function in vivo by Chu (1998)
10.1042/bj2640533 / Biochem. J. / The expression of canine cardiac phospholamban in heterologous systems by Cook (1989)
10.1021/bi961955q / Biochemistry / Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers by Cornea (1997)
10.1016/S0021-9258(18)51579-9 / J. Biol. Chem. / Expression and site-specific mutagenesis of phospholamban. Studies of residues involved in phosphorylation and pentamer formation by Fujii (1989)
{'key': '10.1006/jmbi.2000.3885_RF15', 'series-title': 'Internal Reflection Spectroscopy', 'author': 'Harrick', 'year': '1967'} / Internal Reflection Spectroscopy by Harrick (1967)
10.1016/S0006-3495(98)77835-X / Biophys. J. / Using experimental information to produce a model of the transmembrane domain of the ion channel phospholamban by Herzyk (1998)
10.1021/ja00214a001 / J. Am. Chem. Soc. / The OPLS potential function for proteins, energy minimization for crystals of cyclic peptides and crambin by Jorgensen (1988)
10.1021/bi980642n / Biochemistry / Cysteine reactivity and oligomeric structures of phospholamban and its mutants by Karim (1998)
10.1074/jbc.273.23.14238 / J. Biol. Chem. / Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum by Kimura (1998)
10.1074/jbc.271.36.21726 / J. Biol. Chem. / Phospholamban regulates the Ca2+-ATPase through intramembrane interactions by Kimura (1996)
10.1074/jbc.272.24.15061 / J. Biol. Chem. / Phospholamban inhibitory function is activated by depolymerization by Kimura (1997)
10.1016/S0021-9258(17)33843-7 / J. Biol. Chem. / Effects of adenosine 3′,5′-monophosphate dependent protein kinase on sarcoplasmic reticulum oslated from cardiac and slow and fast contracting skeletal muscles by Kirchberger (1976)
10.1016/S0021-9258(19)81368-6 / J. Biol. Chem. / Phospholamban forms Ca2+-selective channels in lipid bilayers by Kovacs (1988)
10.1006/jmbi.1998.2512 / J. Mol. Biol. / Experimentally based orientational refinement of membrane proteins: A structure for the influenza A M2 H+ channel by Kukol (1999)
10.1152/physrev.1998.78.4.921 / Physiol. Rev. / Phospholamban: protein structure, mechanism of action, and role in cardiac function by Simmerman (1998)
10.1074/jbc.271.10.5941 / J. Biol. Chem. / A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure by Simmerman (1996)
10.1016/0167-4838(89)90203-3 / Biochim. Biophys. Acta / Secondary structure of detergent-solubilized phospholamban, a phosphorylatable, oligomeric protein of cardiac sarcoplasmic reticulum by Simmerman (1989)
10.1021/bi00013a038 / Biochemistry / Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy by Tatulian (1995)
10.1016/S0021-9258(17)42051-5 / J. Biol. Chem. / Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca2+-ATPase of sarcoplasmic reticulum by Toyofuku (1994)
10.1002/pol.1962.1205916712 / J. Polym. Sci. / Infrared dichroism and molecular conformation of α-form poly-γ-benzyl-l-glutamate by Tsuboi (1962)
10.1016/S0021-9258(17)43484-3 / J. Biol. Chem. / Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels. Evidence for a protein structure consisting of multiple identical phosphorylatable subunits by Wegener (1984)
10.1016/S0076-6879(97)89043-X / Methods Enzymol. / Standard FMOC protocols by Wellings (1997)

Dates

Type	When
Created	22 years, 11 months ago (Sept. 18, 2002, 3:24 p.m.)
Deposited	4 years, 4 months ago (May 2, 2021, 11:39 p.m.)
Indexed	1 year ago (Aug. 12, 2024, 7:18 a.m.)
Issued	25 years, 2 months ago (July 1, 2000)
Published	25 years, 2 months ago (July 1, 2000)
Published Print	25 years, 2 months ago (July 1, 2000)

Funders 0

None

BibTeX

@article{Torres_2000, title={Use of a New Label, 13C18O, in the Determination of a Structural Model of Phospholamban in a Lipid Bilayer. Spatial Restraints Resolve the Ambiguity Arising from Interpretations of Mutagenesis Data}, volume={300}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.2000.3885}, DOI={10.1006/jmbi.2000.3885}, number={4}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Torres, Jaume and Adams, Paul D. and Arkin, Isaiah T.}, year={2000}, month=jul, pages={677–685} }

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  "URL": "http://dx.doi.org/10.1006/jmbi.2000.3885",
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  "subject": [],
  "container-title-short": "Journal of Molecular Biology",
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}