Evidence map›Paper›PMID 17573437›Full record

ArticleBiophysical journal2007

Rotational dynamics of phospholamban determined by multifrequency electron paramagnetic resonance.

Yuri E Nesmelov, Christine B Karim, Likai Song, Peter G Fajer, David D Thomas

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.8field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  10. Time-resolved FRET reveals the structural mechanism of SERCA-PLB regulation.Biochemical and biophysical research communications · 2014
    Article
  11. Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  12. Article
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  18. Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Yuri E NesmelovDepartment of Biochemistry, University of Minnesota Medical School, Minneapolis, Minnesota, USA. nesme004@umn.edu
Christine B Karim
Likai Song
Peter G Fajer
David D Thomas
University of Minnesota · USFlorida State University · US

Funding

Structural Dynamics of Muscle Calcium ATPase RegulationR01GM027906 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1985 to 2016
$8.6M
Structural Dynamics of Muscle ContractionR01AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1986 to 2018
$8.0M
MOLECULAR DYNAMICS OF MUSCLE CONTRACTIONR37AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID DALE · 1994 to 2003
$2.1M
Enhanced EPR Sensitivity for Biomedical ResearchR03AR048961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI NESMELOV, YURI · 2003 to 2005
$215k
NIAMS NIH HHS AR32961NIAMS NIH HHS AR48961NIAMS NIH HHS R01 AR032961NIAMS NIH HHS R03 AR048961NIAMS NIH HHS R37 AR032961NIGMS NIH HHS GM27906NIGMS NIH HHS R01 GM027906
6 · The paper itself

Abstract

We have used multifrequency electron paramagnetic resonance to define the multistate structural dynamics of an integral membrane protein, phospholamban (PLB), in a lipid bilayer. PLB is a key regulator of cardiac calcium transport, and its function requires transitions between distinct states of intramolecular dynamics. Monomeric PLB was synthesized with the TOAC spin label at positions 11 (in the cytoplasmic domain) and 46 (in the transmembrane domain) and reconstituted into lipid bilayers. Unlike other protein spin labels, TOAC reports directly the motion of the peptide backbone, so quantitative analysis of its dynamics is worthwhile. Electron paramagnetic resonance spectra at 9.4 GHz (X-band) and 94 GHz (W-band) were analyzed in terms of anisotropic rotational diffusion of the two domains. Motion of the transmembrane domain is highly restricted, while the cytoplasmic domain exhibits two distinct conformations, a major one with moderately restricted nanosecond dynamics (T) and another with nearly unrestricted subnanosecond motion (R). The global analysis of spectra at two frequencies yielded values for the rotational correlation times and order parameters that were much more precisely determined than at either frequency alone. Multifrequency EPR is a powerful approach for analysis of complex rotational dynamics of proteins.

Indexed as

Models, ChemicalModels, MolecularCalcium-Binding ProteinsComputer SimulationElectron Spin Resonance SpectroscopyKineticsPhospholambanProtein ConformationRotationCalcium-Binding ProteinsPhospholamban

Identifiers

PMID17573437
PMCPMC1989693
OpenAlexW2115886057

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.