Evidence map›Paper›PMID 34771091›Full record

ReviewMolecules (Basel, Switzerland)2021

Structural Diversity of Ubiquitin E3 Ligase.

Sachiko Toma-Fukai, Toshiyuki Shimizu

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing 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

106 citing papers in PubMed.

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46 more citing papers are in PubMed but not listed here.

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.

Sachiko Toma-FukaiGraduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma 630-0192, Japan.
Toshiyuki ShimizuGraduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure of PCAF_N, a newly categorized E3 ligase, was reported. We present a review of the recent progress toward the structural understanding of E3 ligases.

Indexed as

Models, MolecularProtein ConformationAmino Acid MotifsAmino Acid SequenceCrystallography, X-RayHumansMultigene FamilyProtein BindingProtein Interaction Domains and MotifsProtein IsoformsProtein Processing, Post-TranslationalStructure-Activity RelationshipUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesProtein IsoformsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligasespost-translational modificationstructural biologyubiquitin E3 ligaseX-ray crystallography

Identifiers

PMID34771091
PMCPMC8586995

What OpenQuestion holds

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LicenceCC BY
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.