Evidence map›Paper›PMID 32113145›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2020

Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy.

Venkatraman Ramanujam, T Reid Alderson, Iva Pritišanac, Jinfa Ying, Ad Bax

Open access · greenAbstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Protein Unfolded State: One, No One and One Hundred Thousand.Journal of the American Chemical Society · 2022
    Review
  7. Article
  8. 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 1 institution in 2 countries.

Venkatraman RamanujamLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, 60438 Frankfurt am Main, Germany.
T Reid AldersonLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, 60438 Frankfurt am Main, Germany.
Iva PritišanacLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, 60438 Frankfurt am Main, Germany.
Jinfa YingLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, 60438 Frankfurt am Main, Germany.
Ad BaxLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, 60438 Frankfurt am Main, Germany. Electronic address: bax@nih.gov.
Goethe University Frankfurt · DE

Funding

Study of protein folding and misfolding by NMR spectroscopyZIADK075141 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, ADRIAAN · 2017 to 2025
$8.6M
Intramural NIH HHS ZIA DK075141
6 · The paper itself

Abstract

Pulsed-field gradient NMR spectroscopy is widely used to measure the translational diffusion and hydrodynamic radius (R

Indexed as

DiffusionHydrogen-Ion ConcentrationHydrostatic PressureIntrinsically Disordered ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein FoldingSynucleinsUbiquitinUreaIntrinsically Disordered ProteinsSynucleinsUbiquitinUreaDioxaneHydration layerIDPPressure-induced unfoldingProtein compactionRadius of hydrationRandom coilSelf-diffusionTranslational diffusionUbiquitinUnfolded chainUreaα-synuclein

Identifiers

PMID32113145
PMCPMC7153785
OpenAlexW3007513860

What OpenQuestion holds

Textmetadata
LicenceTDM
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.