Evidence map›Paper›PMID 27042198›Full record

ReviewCell division2016

Cul3-KLHL20 ubiquitin ligase: physiological functions, stress responses, and disease implications.

Hsin-Yi Chen, Chin-Chih Liu, Ruey-Hwa Chen

Open access · goldAbstract readReview
In one paragraph

Review in Cell division, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

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  11. Targeted protein degradation: expanding the toolbox.Nature reviews. Drug discovery · 2019
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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

3 authors at 2 institutions in 1 country.

Hsin-Yi ChenGraduate Institute of Cancer Biology and Drug Discovery, College of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan.
Chin-Chih LiuInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan ; Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan.
Ruey-Hwa ChenInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan ; Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan.
Institute of Biological Chemistry, Academia Sinica · TWTaipei Medical University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cullin-RING ubiquitin ligases are the largest Ubiquitin ligase family in eukaryotes and are multi-protein complexes. In these complexes, the Cullin protein serves as a scaffold to connect two functional modules of the ligases, the catalytic subunit and substrate-binding subunit. KLHL20 is a substrate-binding subunit of Cullin3 (Cul3) ubiquitin ligase. Recent studies have identified a number of substrates of KLHL20-based ubiquitin ligase. Through ubiquitination of these substrates, KLHL20 elicits diverse cellular functions, some of which are associated with human diseases. Furthermore, the functions, subcellular localizations, and expression of KLHL20 are regulated by several physiological and stressed signals, which allow KLHL20 to preferentially act on certain substrates to response to these signals. Here, we provide a summary of the functions and regulations of KLHL20 in several physiological processes and stress responses and its disease implications.

Indexed as

Actin cytoskeletonAngiogenesisAutophagyCancerCul3 ubiquitin ligasesHypoxiaKLHL20Ubiquitination

Identifiers

PMID27042198
PMCPMC4818519
OpenAlexW2313431370

What OpenQuestion holds

Textmetadata
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.