Evidence map›Paper›PMID 30018140›Full record

ArticleThe Journal of biological chemistry2018

"Mallostery"-ligand-dependent protein misfolding enables physiological regulation by ERAD.

Margaret A Wangeline, Randolph Y Hampton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Direct binding to sterols accelerates endoplasmic reticulum-associated degradation of HMG CoA reductase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Post-Translational Regulation of HMG CoA Reductase.Cold Spring Harbor perspectives in biology · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. ER-Phagy: A New Regulator of ER Homeostasis.Frontiers in cell and developmental biology · 2021
    Review
  19. Metabolites modulate the functional state of human uridine phosphorylase I.Protein science : a publication of the Protein Society · 2020
    Article
  20. Review
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.

Margaret A WangelineFrom the Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California 92093.
Randolph Y HamptonFrom the Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California 92093 rhampton@ucsd.edu.
University of California, San Diego · US

Funding

GENETIC MECHANISMS AND REGULATIONT32GM007240 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 1985 to 2019
$23.8M
Protein degradation and cholesterol regulationR37DK051996 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 2012 to 2020
$3.2M
NIDDK NIH HHS R37 DK051996NIGMS NIH HHS T32 GM007240
6 · The paper itself

Abstract

HMG-CoA reductase (HMGR) undergoes regulated degradation as part of feedback control of the sterol pathway. In yeast, the stability of the HMGR isozyme Hmg2 is controlled by the 20-carbon isoprenoid geranylgeranyl pyrophosphate (GGPP). Increasing GGPP levels cause more efficient degradation by the HMG-CoA reductase degradation (HRD) pathway, allowing for feedback regulation of HMGR. The HRD pathway is critical for the endoplasmic reticulum (ER)-associated degradation (ERAD) of misfolded ER proteins. Here, we have explored GGPP's role in HRD-dependent Hmg2 degradation. We found that GGPP potently regulates Hmg2 levels

Indexed as

Endoplasmic Reticulum-Associated DegradationProtein FoldingAllosteric RegulationHydroxymethylglutaryl CoA ReductasesLigandsPolyisoprenyl Phosphatesgeranylgeranyl pyrophosphateHydroxymethylglutaryl CoA ReductasesLigandsPolyisoprenyl Phosphatesallosteric regulationchemical chaperonescholesterol regulationendoplasmic-reticulum-associated protein degradationERADHMG-CoA reductaseHRD pathwaymallosteryprotein misfoldingubiquitin

Identifiers

PMID30018140
PMCPMC6153289
OpenAlexW2884497523

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.