Evidence map›Paper›PMID 33301748›Full record

ArticleBiophysical journal2021

Modeling of Hidden Structures Using Sparse Chemical Shift Data from NMR Relaxation Dispersion.

R Bryn Fenwick, David Oyen, Henry van den Bedem, H Jane Dyson, Peter E Wright

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023
    Review
  3. Article
  4. 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.

R Bryn FenwickDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, California. Electronic address: bryn.fenwick@gmail.com.
David OyenDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, California.
Henry van den BedemSLAC National Accelerator Laboratory, Stanford University, Menlo Park, California, and Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California.
H Jane DysonDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, California.
Peter E WrightDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, California. Electronic address: wright@scripps.edu.
Scripps Research Institute · USStanford University · US

Funding

Protein Dynamics in Dihydrofolate Reductase CatalysisR01GM075995 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2006 to 2021
$6.1M
Supplement to Resolving ensemble averaged conformations by multi-temperature x-ray crystallography - Equipment 2020R01GM123159 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRASER, JAMES SOLOMON · 2018 to 2021
$2.3M
NIGMS NIH HHS R01 GM075995NIGMS NIH HHS R01 GM123159
6 · The paper itself

Abstract

NMR relaxation dispersion measurements report on conformational changes occurring on the μs-ms timescale. Chemical shift information derived from relaxation dispersion can be used to generate structural models of weakly populated alternative conformational states. Current methods to obtain such models rely on determining the signs of chemical shift changes between the conformational states, which are difficult to obtain in many situations. Here, we use a "sample and select" method to generate relevant structural models of alternative conformations of the C-terminal-associated region of Escherichia coli dihydrofolate reductase (DHFR), using only unsigned chemical shift changes for backbone amides and carbonyls (

Indexed as

Escherichia coliTetrahydrofolate DehydrogenaseMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProtein ConformationTetrahydrofolate Dehydrogenase

Identifiers

PMID33301748
PMCPMC7840400
OpenAlexW3112031948

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.