Evidence map›Paper›PMID 36122228›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.

David Ranava, Christopher M Scheidler, Martin Pfanzelt, Michaela Fiedler, Stephan A Sieber, Sabine Schneider, Mee-Ngan F Yap

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. 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
0.7field-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, 8 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

David RanavaDepartment of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.ORCID 0000-0002-5841-7699
Christopher M ScheidlerDepartment of Chemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Martin PfanzeltDepartment of Chemistry, Chair of Organic Chemistry III, Center for Functional Protein Assemblies (CPA), Technische Universität München, 80333 Garching, Germany.
Michaela FiedlerDepartment of Chemistry, Chair of Organic Chemistry III, Center for Functional Protein Assemblies (CPA), Technische Universität München, 80333 Garching, Germany.ORCID 0000-0001-9407-7356
Stephan A SieberDepartment of Chemistry, Chair of Organic Chemistry III, Center for Functional Protein Assemblies (CPA), Technische Universität München, 80333 Garching, Germany.
Sabine SchneiderDepartment of Chemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.ORCID 0000-0003-1054-8689
Mee-Ngan F YapDepartment of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.ORCID 0000-0003-4213-4050
Center for Integrated Protein Science Munich · DELudwig-Maximilians-Universität München · DENorthwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Devalingam Mahalingam · 1993 to 2026
$153.9M
TR&D 7: Cell Specific ProteomicsP41GM108569 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2015 to 2024
$13.6M
Regulation and function of bacterial hibernating 100S ribosomeR01GM121359 · NIGMS · SAINT LOUIS UNIVERSITY · PI YAP, M.-N. FRANCES · 2017 to 2025
$3.2M
Evolution and consequences of multidrug resistant ribosomeR01AI150986 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI YAP, M.-N. FRANCES · 2020 to 2024
$2.3M
NCI NIH HHS P30 CA060553NIAID NIH HHS R01 AI150986NIGMS NIH HHS P41 GM108569NIGMS NIH HHS R01 GM121359
6 · The paper itself

Abstract

Bacterial hibernating 100S ribosomes (the 70S dimers) are excluded from translation and are protected from ribonucleolytic degradation, thereby promoting long-term viability and increased regrowth. No extraribosomal target of any hibernation factor has been reported. Here, we discovered a previously unrecognized binding partner (YwlG) of hibernation-promoting factor (HPF) in the human pathogen

Indexed as

HibernationRibosomal ProteinsBacteriaGlucoseGlutamic AcidHumansNADOxidoreductasesStaphylococcus aureusVirulence FactorsGlucoseGlutamic AcidNADOxidoreductasesRibosomal ProteinsVirulence Factorsglutamate dehydrogenasehibernationmoonlighting proteinribosomeStaphylococcus aureus

Identifiers

PMID36122228
PMCPMC9522360
OpenAlexW4296297569

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.