Evidence map›Paper›PMID 32236785›Full record

ArticleJournal of biomolecular NMR2020

Pinpoint analysis of a protein in slow exchange using F

Mayu Nishizawa, Erik Walinda, Daichi Morimoto, Kenji Sugase

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Fast Ultra-SelectiveAngewandte Chemie (International ed. in English) · 2026
    Article
  2. Article
  3. 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

4 authors.

Mayu NishizawaDepartment of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto, 615-8510, Japan.ORCID http://orcid.org/0000-0002-4039-6738
Erik WalindaDepartment of Molecular and Cellular Physiology, Graduate School of Medicine, Kyoto University, Sakyo-ku Yoshida Konoe-cho, Kyoto, 606-8501, Japan.
Daichi MorimotoDepartment of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto, 615-8510, Japan.
Kenji SugaseDepartment of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto, 615-8510, Japan. sugase@moleng.kyoto-u.ac.jp.ORCID http://orcid.org/0000-0001-8623-7743

Funding

Japan Society for the Promotion of Science 19J13259Japan Society for the Promotion of Science JP 16K18503Japan Society for the Promotion of Science JP 18H04551Japan Society for the Promotion of Science JP 18K14665
6 · The paper itself

Abstract

ZZ-exchange spectroscopy is widely used to study slow exchange processes in biomolecules, especially determination of exchange rates and assignment of minor peaks. However, if the exchange cross peaks overlap or the populations are skewed, kinetic analysis is hindered. In order to analyze slow exchange protein dynamics under such conditions, here we have developed a new method by combining ZZ-exchange and F

Indexed as

DimerizationHumansKineticsMagnetic Resonance ImagingNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein DomainsRecombinant Fusion ProteinsSequestosome-1 ProteinUbiquitinRecombinant Fusion ProteinsSequestosome-1 ProteinSQSTM1 protein, humanUbiquitinAssignmentChemical exchangeF1F2-selective NMR spectroscopyMinor peakZZ-exchange

Identifiers

PMID32236785

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.