Evidence map›Paper›PMID 39025071›Full record

ReviewMolecular cell2024

Functional and structural insights into RAS effector proteins.

Alessandro M Mozzarelli, Dhirendra K Simanshu, Pau Castel

Erratum issuedAbstract readReview
In one paragraph

Review in Molecular cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Mutational Landscape of Acute Myeloid Leukemia and Its Impact.International journal of molecular sciences · 2026
    Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Literature review of advances and challenges inTranslational lung cancer research · 2025
    Review
  15. Review
  16. Article
  17. Review
  18. M-Ras distinct activation scenarios: A mechanistic outlook and targeting.Computational and structural biotechnology journal · 2025
    Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Alessandro M MozzarelliDepartment of Biochemistry and Molecular Pharmacology, NYU Grossman School of Medicine, New York, NY, USA; Laura and Isaac Perlmutter NYU Cancer Center, NYU Langone Health, New York, NY, USA.
Dhirendra K SimanshuNCI RAS Initiative, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA. Electronic address: dhirendra.simanshu@nih.gov.
Pau CastelDepartment of Biochemistry and Molecular Pharmacology, NYU Grossman School of Medicine, New York, NY, USA; Laura and Isaac Perlmutter NYU Cancer Center, NYU Langone Health, New York, NY, USA. Electronic address: pau.castel@nyulangone.org.

Funding

WORK ORDER 126643 B539 EXPAND IC SUITE75N91019D00024 · NIAID · LEIDOS BIOMEDICAL RESEARCH, INC. · PI BRISCOE, LYNN · 2019 to 2025
$3932.6M
Regulation and tumorigenesis of non-classical RAS oncoproteins - ResubmissionR01CA279171 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Pau Castel · 2024 to 2026
$1.7M
The role of Sin1 in Kras-driven cancerR00CA245122 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI CASTEL, PAU · 2021 to 2023
$633k
NCI NIH HHS 75N91019D00024NCI NIH HHS R00 CA245122NCI NIH HHS R01 CA279171
6 · The paper itself

Abstract

RAS proteins are conserved guanosine triphosphate (GTP) hydrolases (GTPases) that act as molecular binary switches and play vital roles in numerous cellular processes. Upon GTP binding, RAS GTPases adopt an active conformation and interact with specific proteins termed RAS effectors that contain a conserved ubiquitin-like domain, thereby facilitating downstream signaling. Over 50 effector proteins have been identified in the human proteome, and many have been studied as potential mediators of RAS-dependent signaling pathways. Biochemical and structural analyses have provided mechanistic insights into these effectors, and studies using model organisms have complemented our understanding of their role in physiology and disease. Yet, many critical aspects regarding the dynamics and biological function of RAS-effector complexes remain to be elucidated. In this review, we discuss the mechanisms and functions of known RAS effector proteins, provide structural perspectives on RAS-effector interactions, evaluate their significance in RAS-mediated signaling, and explore their potential as therapeutic targets.

Indexed as

ras ProteinsSignal TransductionAnimalsGuanosine TriphosphateHumansModels, MolecularProtein BindingProtein ConformationStructure-Activity RelationshipGuanosine Triphosphateras ProteinseffectorGTPaseRASRAS-binding domainRBD

Identifiers

PMID39025071
PMCPMC11316660

What Socratic 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 Socratic graph.