Evidence map›Paper›PMID 29424242›Full record

ReviewCritical reviews in biochemistry and molecular biology2018

Rce1: mechanism and inhibition.

Shahienaz E Hampton, Timothy M Dore, Walter K Schmidt

Open access · bronzeAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 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
2.4field-weighted citation impact, top 10% 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, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Journal of bacteriology · 2024
    Article
  9. Unveiling a CAAX Protease-Like Protein Involved in Didemnin Drug Maturation and Secretion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. RAS-targeted therapies: is the undruggable drugged?Nature reviews. Drug discovery · 2020
    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

3 authors at 2 institutions in 2 countries.

Shahienaz E Hamptona New York University Abu Dhabi , Abu Dhabi , United Arab Emirates.ORCID 0000-0002-6600-9492
Timothy M Dorea New York University Abu Dhabi , Abu Dhabi , United Arab Emirates.ORCID 0000-0002-3876-5012
Walter K Schmidtc Department of Biochemistry & Molecular Biology , University of Georgia , Athens , GA , USA.ORCID 0000-0002-3359-3434
New York University Abu Dhabi · AEUniversity of Georgia · US

Funding

Role of Proteolysis in Regulating CaaX Protein FunctionR01GM117148 · NIGMS · UNIVERSITY OF GEORGIA · PI SCHMIDT, WALTER K · 2016 to 2019
$1.2M
NIGMS NIH HHS R01 GM117148
6 · The paper itself

Abstract

Ras converting enzyme 1 (Rce1) is an integral membrane endoprotease localized to the endoplasmic reticulum that mediates the cleavage of the carboxyl-terminal three amino acids from CaaX proteins, whose members play important roles in cell signaling processes. Examples include the Ras family of small GTPases, the γ-subunit of heterotrimeric GTPases, nuclear lamins, and protein kinases and phosphatases. CaaX proteins, especially Ras, have been implicated in cancer, and understanding the post-translational modifications of CaaX proteins would provide insight into their biological function and regulation. Many proteolytic mechanisms have been proposed for Rce1, but sequence alignment, mutational studies, topology, and recent crystallographic data point to a novel mechanism involving a glutamate-activated water and an oxyanion hole. Studies using in vivo and in vitro reporters of Rce1 activity have revealed that the enzyme cleaves only prenylated substrates and the identity of the a

Indexed as

EndopeptidasesEndoplasmic ReticulumNeoplasm ProteinsNeoplasmsOxyquinolineProteolysisAnimalsHumansProtease Inhibitorsras ProteinsStructure-Activity RelationshipSubstrate SpecificityEndopeptidasesNeoplasm ProteinsOxyquinolineProtease Inhibitorsras ProteinsRCE1 protein, humanCaaX proteinscancerproteasesRasRas converting enzyme

Identifiers

PMID29424242
PMCPMC5874806
OpenAlexW2791694385

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.