The DOI matches its Crossref record; 234 of the 234 references it cites were found in a registry or an index.
Ras oncogenes: split personalities
Open accessAbstract
Extensive research on the Ras proteins and their functions in cell physiology over the past 30 years has led to numerous insights that have revealed the involvement of Ras not only in tumorigenesis but also in many developmental disorders. Despite great strides in our understanding of the molecular and cellular mechanisms of action of the Ras proteins, the expanding roster of their downstream effectors and the complexity of the signalling cascades that they regulate indicate that much remains to be learnt.
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“PDEδ has a large hydrophobic pocket that can bind farnesyl proteins, especially the lipid portion of KRAS protein, thereby preventing the farnesyl modification of KRAS protein from binding to cell membrane and inhibiting tumor cell proliferation and growth.339,340”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [339]
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Cites
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Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
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Self-citationCreation of human tumour cells with defined genetic elements
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Self-citationPhosphatidylinositol-3-OH kinase direct target of Ras
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Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274
Panitumumab–FOLFOX4 Treatment and RAS Mutations in Colorectal Cancer
Douillard, J.-Y., Oliner, K. S., Siena, S., Tabernero, J., Burkes, R., Barugel, M., Humblet, Y., Bodoky, G., Cunningham, D., Jassem, J., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1305275 · Cited by 2,263
RAS oncogenes: weaving a tumorigenic web
Pylayeva-Gupta, Y., Grabocka, E., & Bar-Sagi, D. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3106 · Cited by 1,789
Oncogene ablation-resistant pancreatic cancer cells depend on mitochondrial function
Viale, A., Pettazzoni, P., Lyssiotis, C. A., Ying, H., Sánchez, N., Marchesini, M., Carugo, A., Green, T., Seth, S., Giuliani, V., et al. (2014) · Nature · doi:10.1038/nature13611 · Cited by 1,259
Regulation of Small GTPases by GEFs, GAPs, and GDIs
Cherfils, J., & Zeghouf, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00003.2012 · Cited by 1,245
Metadata
- Authors
- Karnoub, A. E., & Weinberg, R. A.
- Affiliations
- Whitehead Institute for Biomedical Research (US)
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2008-07
- Volume
- 9
- Issue
- 7
- Pages
- 517-531
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC3915522
- OpenAlex
- W2004774286
- Cited by
- 1,467
- References
- 234
- Citations by year
- 2026: 28 · 2025: 48 · 2024: 58 · 2023: 60 · 2022: 67 · 2021: 89 · 2020: 74 · 2019: 87 · 2018: 93 · 2017: 95 · 2016: 103 · 2015: 118 · 2014: 100 · 2013: 108 · 2012: 94
- FWCI
- 6.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (P01 CA08111, U54 CA12515, P01CA080111, P50CA089393)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- oncogenic Ras, carcinogenesis, developmental disorders, downstream effectors, cell physiology, Ras proteins
- MeSH terms
- Amino Acid Sequence, Animals, Cell Transformation, Neoplastic, DNA-Binding Proteins, Enzyme Activation, Gene Expression Regulation, Humans, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Protein Processing, Post-Translational, Genes, ras, Transcription Factors, Signal Transduction, Sequence Alignment, ras Proteins, Phosphatidylinositol 3-Kinases, GTPase-Activating Proteins, Mitogen-Activated Protein Kinases
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