Evidence map›Paper›PMID 42132878›Full record

ArticleChemical communications (Cambridge, England)2026

Temperature and lipid composition differentially regulate KRAS assemblies on membranes.

Ji Kang, Elena Scott, Sangho D Yun, Virginia K James, Jing-Yuan Chang, Hanieh Bahramimoghaddam, James Downing, Kacie Evans, David H Russell, Arthur Laganowsky

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical communications (Cambridge, England), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Ji KangDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.
Elena ScottDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.
Sangho D YunDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.ORCID http://orcid.org/0000-0003-2456-4575
Virginia K JamesDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.
Jing-Yuan ChangDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.
Hanieh BahramimoghaddamDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.
James DowningDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.
Kacie EvansDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.
David H RussellDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.ORCID http://orcid.org/0000-0003-0830-3914
Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.ORCID http://orcid.org/0000-0001-5012-5547

Funding

Understanding the role of lipids in structure and function of membrane proteinsRM1GM145416 · NIGMS · TEXAS A&M UNIVERSITY · PI Erin S Baker, Arthur D Laganowsky · 2022 to 2026
$7.4M
Native Mass Spectrometry Guided Structural Biology CenterRM1GM149374 · NIGMS · OHIO STATE UNIVERSITY · PI Vicki H. Wysocki · 2023 to 2026
$5.0M
Innovative Native Ion Mobility Approaches for Transformational Measurements in Structural BiologyR01GM138863 · NIGMS · TEXAS A&M UNIVERSITY · PI CLOWERS, BRIAN, LAGANOWSKY, ARTHUR D · 2020 to 2023
$1.2M
Developing new tools to probe membrane protein-lipid interactions for biomedical applicationsR01GM139876 · NIGMS · TEXAS A&M UNIVERSITY · PI LAGANOWSKY, ARTHUR D · 2021 to 2024
$1.2M
NIGMS NIH HHS R01 GM138863NIGMS NIH HHS R01 GM139876NIGMS NIH HHS RM1 GM145416NIGMS NIH HHS RM1 GM149374
6 · The paper itself

Abstract

RAS GTPases oligomerize on membranes to regulate signaling, but factors governing this process remain unclear. Using variable-temperature native mass spectrometry and NanoBiT assays, we show KRAS dimerization is lipid- and temperature-dependent, increasing at higher temperatures, whereas NRAS is unaffected. These results indicate entropy-driven KRAS assembly and reveal isoform-specific mechanisms of membrane organization.

Indexed as

Cell MembraneLipidsProto-Oncogene Proteins p21(ras)TemperatureGTP PhosphohydrolasesHumansProtein MultimerizationGTP PhosphohydrolasesKRAS protein, humanLipidsProto-Oncogene Proteins p21(ras)

Identifiers

PMID42132878
PMCPMC13170742

What Socratic holds

Textmetadata
LicenceCC BY
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.