Evidence map›Paper›PMID 31128784›Full record

ArticleMethods in enzymology2019

Cysteine-ethylation of tissue-extracted membrane proteins as a tool to detect conformational states by solid-state NMR spectroscopy.

Daniel K Weber, Taysir Bader, Erik K Larsen, Songlin Wang, Tata Gopinath, Mark Distefano, Gianluigi Veglia

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

7 authors.

Daniel K WeberDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Taysir BaderDepartment of Chemistry, University of Minnesota, Minneapolis, MN, United States.
Erik K LarsenDepartment of Chemistry, University of Minnesota, Minneapolis, MN, United States.
Songlin WangDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Tata GopinathDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Mark DistefanoDepartment of Chemistry, University of Minnesota, Minneapolis, MN, United States.
Gianluigi VegliaDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, United States; Department of Chemistry, University of Minnesota, Minneapolis, MN, United States. Electronic address: vegli001@umn.edu.

Funding

NMR Structural Analysis of Calcium Regulation in MuscleR01GM064742 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI VEGLIA, GIANLUIGI · 2002 to 2019
$7.1M
Structural Basis of Dilated CardiomyopathyR01HL144130 · NHLBI · UNIVERSITY OF MINNESOTA · PI VEGLIA, GIANLUIGI · 2018 to 2021
$1.5M
NHLBI NIH HHS R01 HL144130NIGMS NIH HHS R01 GM064742
6 · The paper itself

Abstract

Solid-state NMR (ssNMR) is an ideal tool to study structure and dynamics of membrane proteins in their native lipid environment. In principle, ssNMR has no size limitations. However, this feature is rarely exploited as large membrane proteins display severe resonance overlap. In addition, dismal yields from recombinant bacterial expression systems limit severely spectroscopic characterization of membrane proteins. For very large mammalian membrane proteins, extraction from the original organism remains the most viable approach. In this case, NMR-observable nuclei must be introduced post-translationally, but the approaches developed so far are rather scarce. Here, we detail the synthesis and engineering of a reactive

Indexed as

AnimalsCalcium-Binding ProteinsCysteineHumansIsotope LabelingMembrane ProteinsModels, MolecularMuscle ProteinsNuclear Magnetic Resonance, BiomolecularPhospholambanProtein ConformationProteolipidsSarcoplasmic Reticulum Calcium-Transporting ATPasesCalcium-Binding ProteinsCysteineMembrane ProteinsMuscle ProteinsPhospholambanProteolipidssarcolipinSarcoplasmic Reticulum Calcium-Transporting ATPasesConformational statesCysteine ethylationIsotopic labelingMammalian proteinsPhospholambanSarcolipinSERCASolid-state NMR

Identifiers

PMID31128784
PMCPMC7418180

What OpenQuestion holds

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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.