Evidence map›Paper›PMID 34218390›Full record

ArticleJournal of biomolecular NMR2021

Toho-1 β-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam.

Varun V Sakhrani, Rittik K Ghosh, Eduardo Hilario, Kevin L Weiss, Leighton Coates, Leonard J Mueller

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2021. 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
–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

6 citing papers in PubMed.

  1. NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam.Proceedings of the National Academy of Sciences of the United States of America · 2026
    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

6 authors.

Varun V SakhraniDepartment of Chemistry, University of California Riverside, Riverside, CA, 92521, USA.
Rittik K GhoshDepartment of Biochemistry, University of California Riverside, Riverside, CA, 92521, USA.
Eduardo HilarioDepartment of Chemistry, University of California Riverside, Riverside, CA, 92521, USA.
Kevin L WeissNeutron Scattering Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN, 37831, USA.
Leighton CoatesSecond Target Station, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN, 37831, USA. coatesl@ornl.gov.ORCID http://orcid.org/0000-0003-2342-049X
Leonard J MuellerDepartment of Chemistry, University of California Riverside, Riverside, CA, 92521, USA. leonard.mueller@ucr.edu.ORCID http://orcid.org/0000-0002-2607-9875

Funding

Chemically-Rich Structure and Dynamics in the Active Site of Tryptophan SynthaseR01GM097569 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI MUELLER, LEONARD J · 2011 to 2020
$2.9M
National Science Foundation 1710671NIGMS NIH HHS R01 GM097569NIH HHS 097569
6 · The paper itself

Abstract

Backbone chemical shift assignments for the Toho-1 β-lactamase (263 amino acids, 28.9 kDa) are reported based on triple resonance solution-state NMR experiments performed on a uniformly

Indexed as

Azabicyclo Compoundsbeta-LactamasesBinding SitesModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationavibactamAzabicyclo Compoundsbeta-Lactamases15N backbone amide relaxationAvibactamBackbone chemical shift assignmentsLigand–protein bindingNon-β-lactam inhibitorsProtein backbone dynamicsProtein NMRβ-lactamase

Identifiers

PMID34218390
PMCPMC9122098

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Registered trials

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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.