Evidence map›Paper›PMID 32514875›Full record

ArticleJournal of biomolecular NMR2020

Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy.

Jianping Li, Ampon Sae Her, Nathaniel J Traaseth

Open access · greenAbstract read
PubMed Full text at PMC Publisher
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 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Asymmetric protonation of glutamate residues drives a preferred transport pathway in EmrE.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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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

3 authors at 1 institution in 1 country.

Jianping LiDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY, 10003, USA.
Ampon Sae HerDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY, 10003, USA.
Nathaniel J TraasethDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY, 10003, USA. traaseth@nyu.edu.ORCID http://orcid.org/0000-0002-1185-6088
New York University · US

Funding

Mechanisms of Allostery and Molecular Recognition in the Small Multidrug Resistance FamilyR01AI108889 · NIAID · NEW YORK UNIVERSITY · PI Nathaniel J. Traaseth · 2014 to 2026
$5.4M
Division of Molecular and Cellular Biosciences 1902449National Institute of Allergy and Infectious Diseases AI108889NIAID NIH HHS R01 AI108889
6 · The paper itself

Abstract

NMR spectroscopy is commonly used to infer site-specific acid dissociation constants (pK

Indexed as

AnionsAntiportersAsparagineAspartic AcidCrystallizationEscherichia coli ProteinsGlutamic AcidGlutamineLipid BilayersMembrane ProteinsNuclear Magnetic Resonance, BiomolecularProof of Concept StudyProteinsUbiquitinAnionsAntiportersAsparagineAspartic AcidEmrE protein, E coliEscherichia coli ProteinsGlutamic AcidGlutamineLipid BilayersMembrane ProteinsProteinsUbiquitinAcid dissociation constantsEmrEMagic-angle-spinningMembrane proteinsMicrocrystalline proteinsSolid-state NMR

Identifiers

PMID32514875
PMCPMC7472563
OpenAlexW3034021590

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.