Evidence map›Paper›PMID 34365229›Full record

ReviewCurrent opinion in structural biology2021

Post-translational modification of RAS proteins.

Sharon L Campbell, Mark R Philips

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
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  5. Article
  6. Allostery in Biomolecular Condensates.Journal of molecular biology · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
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  18. Review
  19. Biomarker Landscape in RASopathies.International journal of molecular sciences · 2024
    Review
  20. Article
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.

Sharon L CampbellUniversity of North Carolina School of Medicine, USA. Electronic address: campbesl@med.unc.edu.
Mark R PhilipsPerlmutter Cancer Center, NYU Grossman School of Medicine, USA.
NYU Langone’s Laura and Isaac Perlmutter Cancer Center

Funding

Project 4: The role of codon bias in RAS tumorigenesisP01CA203657 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DER, CHANNING J. · 2016 to 2020
$7.9M
Differential function and tumor vulnerabilities revealed by RAS membrane traffickingR35CA253178 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI MARK Reid PHILIPS · 2020 to 2026
$6.8M
Structure and Mechanism of G-proteins and cell adhesion proteins in regulation of cell growth and motilityR35GM134962 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Sharon L Campbell · 2020 to 2026
$4.2M
Isoprenylcysteine Carboxyl Methyltransferase (ICMT) as a Target in NRAS Driven Melanoma - Resubmission - 1R01CA163489 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 2012 to 2020
$2.8M
Role of nonsense mediated RNA decay in pancreatic cancerR01CA211687 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 2018 to 2022
$2.1M
Structure/Function Analysis of IcmtR01CA118495 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 2006 to 2010
$1.5M
Regulation of KRAS Trafficking and Signaling by GPR31R03TR003358 · NCATS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 2020 to 2020
$170k
NCATS NIH HHS R03 TR003358NCI NIH HHS P01 CA203657NCI NIH HHS R01 CA118495NCI NIH HHS R01 CA163489NCI NIH HHS R01 CA211687NCI NIH HHS R35 CA253178NIGMS NIH HHS R35 GM134962
6 · The paper itself

Abstract

Mutations of RAS genes drive cancer more frequently than any other oncogene. RAS proteins integrate signals from a wide array of receptors and initiate downstream signaling through pathways that control cellular growth. RAS proteins are fundamentally binary molecular switches in which the off/on state is determined by the binding of GDP or GTP, respectively. As such, the intrinsic and regulated nucleotide-binding and hydrolytic properties of the RAS GTPase were historically believed to account for the entirety of the regulation of RAS signaling. However, it is increasingly clear that RAS proteins are also regulated by a vast array of post-translational modifications (PTMs). The current challenge is to understand what are the functional consequences of these modifications and which are physiologically relevant. Because PTMs are catalyzed by enzymes that may offer targets for drug discovery, the study of RAS PTMs has been a high priority for RAS biologists.

Indexed as

Protein Processing, Post-Translationalras ProteinsCarrier ProteinsSignal TransductionCarrier Proteinsras ProteinsCancerGTPasePost-translational modificationRASSignaling

Identifiers

PMID34365229
PMCPMC8649064
OpenAlexW3191565451

What OpenQuestion holds

Textmetadata
LicenceTDM
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.