Evidence map›Paper›PMID 40948893›Full record

ArticleBio-protocol2025

Use of a High-Affinity Ubiquitin-Binding Domain to Detect and Purify Ubiquitinated Substrates and Their Interacting Proteins.

Nitu Saha, Mengwen Zhang, Mark Hochstrasser

Abstract read
In one paragraph

Article in Bio-protocol, 2025. 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
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.

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

3 authors.

Nitu SahaDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
Mengwen ZhangDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
Mark HochstrasserDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.

Funding

Mechanisms of Cell Regulation and Manipulation by the Ubiquitin SystemR35GM136325 · NIGMS · YALE UNIVERSITY · PI Mark W Hochstrasser · 2020 to 2026
$6.5M
Degradation of Short Lived Regulatory Protein in YeastR37GM046904 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 2009 to 2018
$3.6M
NIGMS NIH HHS R35 GM136325NIGMS NIH HHS R37 GM046904
6 · The paper itself

Abstract

OtUBD is a high-affinity ubiquitin-binding domain (UBD) derived from a large protein produced by the microorganism

Indexed as

Affinity purificationOrientiaOtUBDProteomicsUbiquitin

Identifiers

PMID40948893
PMCPMC12423275

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.