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ProteomicsMapping the Interactome of KRAS and Its G12C/D/V Mutants by Integrating TurboID Proximity Labeling with Quantitative Proteomics
RAS is one of the most frequently mutated proto-oncogenes in human malignancies, with mutation sites and subtypes exhibiting tumor-type dependent distribution. Oncogenic RAS mutations will maintain continuously GTP-bound activation states that leading to dysregulation of downstream signaling, ultima...
ORGANISM(S): Homo sapiens (Human) 
2025-06-09 | PXD062101 | Pride
Kras interactome  kras g12 mutants  turboid proximity-labeling  quantitative proteomics；metabolic reprogramming 
ProteomicsProteomic mapping of the interactome of KRAS mutants identifies new features of RAS signalling networks and the mechanism of action of Sotorasib.
RAS proteins are key regulators of cell signalling and are master regulators of different cell functions including cell proliferation, differentiation and cell death. Point mutations in the genes of this family are common, particularly in the KRAS. These mutations were thought to cause the constativ...
ORGANISM(S): Homo sapiens (Human) 
2023-10-15 | PXD043536 | Pride
Apms Ras Signalling 
ProteomicsOncogenic Mutations of KRAS Modulate Its Turnover by the CUL3/LZTR1 E3 ligase Complex
KRAS is a proto-oncogene encoding a small GTPase. Mutations contribute up to 30% of human solid tumours including lung adenocarcinoma, pancreatic and colorectal carcinomas. Most KRAS activating mutations interfere with GTP hydrolysis, essential for its role as a molecular switch, leading to alterati...
ORGANISM(S): Homo sapiens (Human) 
2024-03-06 | PXD029725 | Pride
G13d Kras G12d 
ProteomicsOmics Analysis of Lung Adenocarcinoma with KRAS G12 Mutations
We conducted a proteomic analysis of LUAD patients with KRAS G12 mutations, and explore the interactome of KRAS G12 proteins. In conclusion, the findings of this study provide a deep understanding of the molecular mechanism of KRAS G12 mutation-driven LUAD.
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD058891 | Pride
Kras luad immune omics 
TranscriptomicsIdentification of LMO2 transcriptome and interactome in diffuse large B-cell lymphoma
LMO2 regulates gene expression facilitating the formation of multipartite DNA-binding complexes. In B cells, LMO2 is specifically up-regulated in the Germinal Center (GC) reaction and is expressed in GC-derived non-Hodgkin’s lymphomas. LMO2 is one of the most powerful prognostic indicators in DLBCL ...
ORGANISM(S): Homo sapiens 
2012-07-12 | E-GEOD-34576 | biostudies-arrayexpress
UnknownProteomic Mapping of the Interactome of KRAS Mutants Identifies New Features of RAS Signalling Networks and the Mechanism of Action of Sotorasib.
Not available
S-EPMC10452836 | biostudies-literature
ProteomicsAnalysis of context-specific KRAS-effectors (sub)complexes in Caco-2 cells
Ras is a key switch controlling cell behavior. In the GTP-bound form, Ras interacts with numerous effectors in a mutually exclusive manner, where individual Ras-effectors are likely part of larger cellular (sub)complexes. The molecular details of these (sub)complexes and their alteration in specific...
ORGANISM(S): Homo sapiens (Human) 
2023-02-23 | PXD035399 | Pride
Kras Affinity purification (ap)-mass spectrometry (ms) Protein-protein interactions 
UnknownMapping the Interactome of KRAS and Its G12C/D/V Mutants by Integrating TurboID Proximity Labeling with Quantitative Proteomics.
Not available
S-EPMC12109396 | biostudies-literature
ProteomicsAnalysis of oncogenic Kras-induced changes in the RNA-bound proteome of PDAC cells
In order to reveal the impact of oncogenic KRAS signaling on the RNA-bound proteome of Pancreatic Ductal Adenocarcinoma (PDAC), we carried out quantitative whole Transcriptome RNA Interactome Capture (RIC) analysis in tumour cells from an inducible mouse model of PDAC (iKras PDAC) (Ying et al., 2012...
ORGANISM(S): Mus musculus (Mouse) 
2023-02-12 | PXD030825 | Pride
Rna interactome capture  ric  oops  kras  rna-binding  rbp  silac 
UnknownComparative Nucleotide-Dependent Interactome Analysis Reveals Shared and Differential Properties of KRas4a and KRas4b.
Not available
S-EPMC5785771 | biostudies-literature
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