Evidence map›Paper›PMID 35107780›Full record

ArticleBiomolecular NMR assignments2022

Backbone NMR resonance assignment of the intrinsically disordered UBact protein from Nitrospira nitrosa.

Steven M Bonn, David Fushman

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecular NMR assignments, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 99% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 1 institution in 1 country.

Steven M BonnDepartment of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD, 20742, USA.ORCID 0000-0002-0710-756X
David FushmanDepartment of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD, 20742, USA. fushman@umd.edu.ORCID 0000-0002-6634-8056
University of Maryland, College Park · US

Funding

Solution structure and dynamics of polyubiquitin chainsR01GM065334 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI DAVID FUSHMAN · 2002 to 2026
$6.2M
NIGMS NIH HHS R01 GM065334
6 · The paper itself

Abstract

Ubiquitin signaling in eukaryotes is responsible for a variety of cellular outcomes, most notably proteasomal degradation. A recent bioinformatic study has revealed the existence of a new proteasomal operon in certain gram-negative bacteria phyla. This operon contains genes similar to those included in the prokaryotic ubiquitin-like protein (Pup) proteasomal operon, but do not themselves contain Pup. Instead, they encode for a protein termed UBact with 30% sequence similarity to Pup. Here, we report the near-complete NMR assignment of the backbone and partial assignment of the side chain chemical shifts of the UBact protein from Nitrospira nitrosa. The

Indexed as

Intrinsically Disordered ProteinsMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProteasome Endopeptidase ComplexProtonsUbiquitinsIntrinsically Disordered ProteinsProteasome Endopeptidase ComplexProtonsUbiquitinsIntrinsically disordered proteinNitrospira nitrosaProteasomeUBact

Identifiers

PMID35107780
PMCPMC9081246
OpenAlexW4210641009

What OpenQuestion holds

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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.