Evidence map›Paper›PMID 33453997›Full record

ReviewThe Journal of biological chemistry2020

Post-translational control of the long and winding road to cholesterol.

Laura J Sharpe, Hudson W Coates, Andrew J Brown

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  3. Review
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  7. Reducing LDL-Cholesterol to Very Low Levels: Sailing Between Established Benefits and Potential Risks.High blood pressure & cardiovascular prevention : the official journal of the Italian Society of Hypertension · 2025
    Review
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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 1 institution in 1 country.

Laura J SharpeSchool of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales, Australia.
Hudson W CoatesSchool of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales, Australia.
Andrew J BrownSchool of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales, Australia. Electronic address: aj.brown@unsw.edu.au.
UNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synthesis of cholesterol requires more than 20 enzymes, many of which are intricately regulated. Post-translational control of these enzymes provides a rapid means for modifying flux through the pathway. So far, several enzymes have been shown to be rapidly degraded through the ubiquitin-proteasome pathway in response to cholesterol and other sterol intermediates. Additionally, several enzymes have their activity altered through phosphorylation mechanisms. Most work has focused on the two rate-limiting enzymes: 3-hydroxy-3-methylglutaryl CoA reductase and squalene monooxygenase. Here, we review current literature in the area to define some common themes in the regulation of the entire cholesterol synthesis pathway. We highlight the rich variety of inputs controlling each enzyme, discuss the interplay that exists between regulatory mechanisms, and summarize findings that reveal an intricately coordinated network of regulation along the cholesterol synthesis pathway. We provide a roadmap for future research into the post-translational control of cholesterol synthesis, and no doubt the road ahead will reveal further twists and turns for this fascinating pathway crucial for human health and disease.

Indexed as

CholesterolHumansHydroxymethylglutaryl CoA ReductasesOxidoreductases Acting on CH-CH Group DonorsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalSqualene MonooxygenaseUbiquitinUbiquitin-Protein LigasesCholesterolHydroxymethylglutaryl CoA ReductasesOxidoreductases Acting on CH-CH Group DonorsProteasome Endopeptidase ComplexSqualene MonooxygenaseUbiquitinUbiquitin-Protein Ligasesacetylationcholesterolcholesterol metabolismcholesterol regulationcholesterol synthesisE3 ubiquitin ligaseHMGCRphosphorylationpost-translational modificationpost-translational modification (PTM)post-translational regulationproteasomeprotein degradationSMubiquitinationubiquitin ligaseubiquitylation (ubiquitination)

Identifiers

PMID33453997
PMCPMC7762936
OpenAlexW3092030571

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.