Evidence map›Paper›PMID 31199417›Full record

ArticleChemical communications (Cambridge, England)2019

Exact distance measurements for structure and dynamics in solid proteins by fast-magic-angle-spinning NMR.

Kristof Grohe, Evgeny Nimerovsky, Himanshu Singh, Suresh K Vasa, Benedikt Söldner, Beat Vögeli, Chad M Rienstra, Rasmus Linser

Abstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Chemical reviews · 2022
    Review
  6. Review
  7. Article
  8. Article
  9. Transferred-Rotational-Echo Double Resonance.The journal of physical chemistry. A · 2021
    Article
  10. Heteronuclear and homonuclear radio-frequency-driven recoupling.Magnetic resonance (Gottingen, Germany) · 2021
    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

8 authors.

Kristof GroheFaculty for Chemistry and Pharmacy, Ludwig-Maximilians-University Munich, Butenandtstr. 5-13, 81377 Munich, Germany. rasmus.linser@lmu.de and Faculty of Chemistry and Chemical Biology, Technical University Dortmund, Otto-Hahn-Straße 4a, 44227 Dortmund, Germany.ORCID http://orcid.org/0000-0002-3388-4741
Evgeny NimerovskyDepartment of Chemistry, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, USA.ORCID http://orcid.org/0000-0003-3002-0718
Himanshu SinghFaculty for Chemistry and Pharmacy, Ludwig-Maximilians-University Munich, Butenandtstr. 5-13, 81377 Munich, Germany. rasmus.linser@lmu.de and Faculty of Chemistry and Chemical Biology, Technical University Dortmund, Otto-Hahn-Straße 4a, 44227 Dortmund, Germany.ORCID http://orcid.org/0000-0002-2819-6282
Suresh K VasaFaculty for Chemistry and Pharmacy, Ludwig-Maximilians-University Munich, Butenandtstr. 5-13, 81377 Munich, Germany. rasmus.linser@lmu.de and Faculty of Chemistry and Chemical Biology, Technical University Dortmund, Otto-Hahn-Straße 4a, 44227 Dortmund, Germany.ORCID http://orcid.org/0000-0002-8137-9344
Benedikt SöldnerFaculty for Chemistry and Pharmacy, Ludwig-Maximilians-University Munich, Butenandtstr. 5-13, 81377 Munich, Germany. rasmus.linser@lmu.de.
Beat VögeliDepartment of Biochemistry and Molecular Genetics, University of Colorado Denver, 12801 East 17th Avenue, Aurora, CO 80045, USA.ORCID http://orcid.org/0000-0003-1176-3137
Chad M RienstraDepartment of Chemistry, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, USA.ORCID http://orcid.org/0000-0002-9912-5596
Rasmus LinserFaculty for Chemistry and Pharmacy, Ludwig-Maximilians-University Munich, Butenandtstr. 5-13, 81377 Munich, Germany. rasmus.linser@lmu.de and Faculty of Chemistry and Chemical Biology, Technical University Dortmund, Otto-Hahn-Straße 4a, 44227 Dortmund, Germany.ORCID http://orcid.org/0000-0001-8983-2935

Funding

Toolkit for High-Resolution Structure and Dynamics of Functional LipidsR01GM123455 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MORRISSEY, JAMES H., RIENSTRA, CHAD M · 2016 to 2020
$5.0M
Structures of Amphotericin-Sterol ComplexesR01GM112845 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI RIENSTRA, CHAD M · 2015 to 2018
$1.8M
NIGMS NIH HHS R01 GM112845NIGMS NIH HHS R01 GM123455
6 · The paper itself

Abstract

Fast-magic-angle-spinning solid-state NMR is a developing technique for determination of protein structure and dynamics. Proton-proton correlations usually lead to rough distance restraints, a serious hurdle towards high-resolution structures. Analogous to the "eNOE" concept in solution, an integrative approach for more accurate restraints enables improved structural accuracy with minimal analytical effort.

Indexed as

AnimalsCarbonic Anhydrase IIChickensHumansMolecular StructureNuclear Magnetic Resonance, BiomolecularSpectrinsrc Homology DomainsCarbonic Anhydrase IISpectrin

Identifiers

PMID31199417
PMCPMC6658100

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.