The DOI matches its Crossref record; 157 of the 162 references it cites were found in a registry or an index.
RAS Proteins and Their Regulators in Human Disease
Open accessAbstract
RAS proteins are binary switches, cycling between ON and OFF states during signal transduction. These switches are normally tightly controlled, but in RAS-related diseases, such as cancer, RASopathies, and many psychiatric disorders, mutations in the RAS genes or their regulators render RAS proteins persistently active. The structural basis of the switch and many of the pathways that RAS controls are well known, but the precise mechanisms by which RAS proteins function are less clear. All RAS biology occurs in membranes: a precise understanding of RAS' interaction with membranes is essential to understand RAS action and to intervene in RAS-driven diseases.
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In the citing paper
“In particular, farnesylation at the position 185 cysteine residue results in KRAS anchoring at the plasma membrane, initiating the activation of KRAS and its downstream signaling42.”
From Mechanisms of KRAS inhibitor resistance in KRAS-mutant colorectal cancer harboring Her2 amplification and aberrant KRAS localization (2025) · cites this paper as [42]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Post-translational modification of KRAS plays an important role in KRAS–MAPK pathway activation.”
From Mechanisms of KRAS inhibitor resistance in KRAS-mutant colorectal cancer harboring Her2 amplification and aberrant KRAS localization (2025) · cites this paper as [42]
The cited source says what the claim attributes to it.
In the citing paper
“KRAS is one of the most frequently mutated oncogenes in cancer, yet efforts to directly target KRAS have been mostly unsuccessful because initial analyses of KRAS proteins indicated that they lack a clear pocket to which small molecules can bind with high affinity [1, 2].”
From Anti-tumor efficacy of a potent and selective non-covalent KRASG12D inhibitor (2022) · cites this paper as [2]
The cited source says what the claim attributes to it.
In the citing paper
“Although KRAS mutations are often collectively classified as a single oncogenic entity, distinct KRAS alleles exhibit substantial biochemical and functional heterogeneity [1,4,12].”
From Precision Targeting of KRAS-Mutant Cancers: Beyond G12C Toward G12D and Pan-RAS Therapeutic Strategies (2026) · cites this paper as [4]
In the citing paper
“Mutational activation of KRAS promotes the initiation and progression of cancers, especially in the colorectum, pancreas, lung, and blood plasma, with varying prevalence of specific activating missense mutations.”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
In the citing paper
“However, it is frequently mutated in only a handful of cancers, with the highest frequencies in colorectal adenocarcinoma (COAD), lung adenocarcinoma (LUAD), multiple myeloma (MM), and pancreatic adenocarcinoma (PAAD).”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
In the citing paper
“KRAS is one of the most commonly mutated genes in cancer1,2”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
In the citing paper
“When mutated at one of its four hotspot codons—12, 13, 61, or 146—activated KRAS protein hyperactivates many downstream effector pathways, such as the MAPK and PI3K-AKT signaling pathways1”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
In the citing paper
“As protein tyrosine phosphorylation plays an essential role in multiple intracellular processes, SHP2 is involved in the regulation of multiple signaling pathways, including those involved in cancer cells, such as RAS-MAPK, PI3K-AKT and JAK-STAT pathways.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [261]
In the citing paper
“RAS acts as a molecular switch, transmitting signals of cell growth and differentiation by binding to GTP or GDP and switching between active and inactive states.261”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [261]
In the citing paper
“abnormalities in components of the RAS pathway, including activating RAS mutations, are common across a diverse range of malignancies”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
In the citing paper
“The RAS family GTPases, KRAS, NRAS and HRAS, cycle between GTP-loaded ‘on’ and GDP-loaded ‘off’ states4,6, involving the action of RAS-guanine nucleotide exchange factors (RAS-GEFs) and RAS-GTPase-activating proteins (RAS-GAPs), respectively.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
In the citing paper
“Almost all cancer-associated RAS mutations (~95%) affect codon 12, 13 or 61, and lead to a markedly increased basal RAS-GTP:RAS-GDP ratio and constitutive activation of RAS effectors4,6.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
In the citing paper
“When mutated, oncogenic RAS remains preferentially in the active GTP-bound state, whereas GTP hydrolysis by its GTPase function and enzymes such as GTPase-activating proteins, is compromised1,2.”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [1]
In the citing paper
“KRAS in particular, is among the most frequently mutated oncogenes in cancer and is commonly associated with therapeutic resistance and poor prognosis1,5,6.”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [1]
In the citing paper
“These mutations dramatically shift the equilibrium of Ras protein to exist mostly in the GTP-bound state and effectively uncouple Ras proteins from upstream receptor inputs and drive constitutive signaling to downstream Ras effector pathways (13).”
From KRAS mutation in pancreatic cancer (2021) · cites this paper as [13]
In the citing paper
“On the one hand, the affinity of KRAS and GTP is at the pM level, while the concentration of GTP in cells is up to 0.5 μM.”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [18]
In the citing paper
“It is difficult to achieve effective competition like protein kinase inhibitors [18, 19].”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [18]
In the citing paper
“Oncogenic KRAS can activate various downstream effector pathways, and the best characterized are phosphatidylinositol 3-kinase (PI3K) and mitogen-activated protein kinases (MAPK) (23–25).”
From New Horizons in KRAS-Mutant Lung Cancer: Dawn After Darkness (2019) · cites this paper as [24]
In the citing paper
“we recognize that these elements have a substantial influence on KRAS dynamics [53,54] and signaling [55].”
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Metadata
- Authors
- Simanshu, D. K., Nissley, D. V., & McCormick, F.
- Affiliations
- Frederick National Laboratory for Cancer Research (US)
- University of California, San Francisco (US)
- Corresponding author
- McCormick, Frank
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 170
- Issue
- 1
- Pages
- 17-33
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5555610
- OpenAlex
- W2732767128
- Cited by
- 1,943
- References
- 162
- Citations by year
- 2026: 210 · 2025: 263 · 2024: 276 · 2023: 247 · 2022: 267 · 2021: 247 · 2020: 194 · 2019: 143 · 2018: 82 · 2017: 12
- FWCI
- 11.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute
- NIH (HHSN261200800001E)
- Outstanding Investigator Award (5R35CA197709)
- 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
- Ras proteins, Ras signaling, RASopathies, cancer, mental illness, RAS mutations, signal transduction, membrane binding, Ras activation
- MeSH terms
- Congenital Abnormalities, Animals, Mental Disorders, Cell Membrane, Humans, Mutation, Neoplasms, Phylogeny, Yeasts, Signal Transduction, ras Proteins
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