The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The target in scope is human RASAL2 (RAS protein activator-like 2; also called nGAP) corresponding to UniProt Q9UJF2. Independent RasGAP-focused reviews describe RASAL2 as a PH–C2–RasGAP domain protein of ~1139 aa, consistent with the UniProt description and with RasGAP-family architecture. (stewart2020pumpingthebrakes pages 2-3)
RAS proteins are small GTPases that toggle between an “on” (GTP-bound) and “off” (GDP-bound) state. RasGAPs accelerate the intrinsic GTP hydrolysis rate of RAS, thereby promoting the conversion of RAS-GTP → RAS-GDP (functional inactivation of RAS signaling). Reviews of Ras negative regulation highlight that the GTPase-stimulating activity resides in the C-terminal GAP domain and that loss of RasGAP function leads to accumulation of GTP-bound RAS with increased downstream signaling. (stewart2020pumpingthebrakes pages 2-3)
Primary molecular function (RASAL2): by definition and domain composition, RASAL2’s canonical biochemical role is to act as a RasGAP that down-regulates RAS signaling by accelerating GTP hydrolysis on RAS. (stewart2020pumpingthebrakes pages 2-3)
A RasGAP review that explicitly lists RASAL2 describes it as a PH domain + C2 domain + C-terminal RasGAP domain protein. (stewart2020pumpingthebrakes pages 2-3)
Functional interpretation (current model): Ras is membrane-associated; therefore, noncatalytic domains (PH/C2) are widely discussed as contributing to membrane targeting and/or protein–protein interactions that position the GAP domain to engage membrane-localized RAS. (stewart2020pumpingthebrakes pages 2-3)
A RasGAP-centered cancer review synthesizes a major theme for RASAL2: it is frequently described as a tumor suppressor in multiple cancers (low expression associated with Ras–ERK activation and worse prognosis), yet it can also behave in some contexts as an oncogenic driver of EMT/metastasis, with reported links to YAP, Wnt/β-catenin, PI3K/AKT, and Rac1 pathway wiring. This is presented as a context-dependent phenomenon and a key interpretive issue in the RASAL2 literature. (bellazzo2020cuttingthebrakes pages 3-5)
By its RasGAP catalytic function, RASAL2 is placed upstream of major RAS effector pathways (e.g., ERK/MAPK, PI3K/AKT) as a negative regulator. The “Ras brakes” reviews emphasize that RasGAP loss increases signaling through RAS-regulated pathways. (stewart2020pumpingthebrakes pages 2-3)
In luminal breast cancer models, combined perturbation of RasGAP tumor suppressors (RASAL2 with DAB2IP) is described as producing strong activation of ERK and AKT outputs, supporting the view that RasGAP co-loss can amplify multiple RAS-pathway branches. (olsen2017lossofrasgap pages 11-11)
A key mechanistic concept from the luminal breast cancer literature is cooperative tumor suppression by two RasGAPs, RASAL2 and DAB2IP. The Cancer Discovery study reports that combined loss promotes invasiveness and EMT, and that reconstitution of both genes suppresses metastasis in vivo. (olsen2017lossofrasgap pages 5-6, olsen2017lossofrasgap pages 7-8)
A later 2024 review focused on DAB2IP frames this cooperation as nonredundant and notes that concomitant loss of both RasGAPs “dramatically increased invasion and metastasis” in ER+ breast cancer models, reinforcing the concept that RasGAP network integrity is important for metastasis control. (fania2024anupdateon pages 1-2)
A 2024 JCI Insight paper also highlights that DAB2IP loss often occurs together with loss of RASAL2 and links this to poor outcome in luminal breast cancer contexts, placing RASAL2 within a clinically relevant RasGAP-loss state. (mukherjee2024dab2iplossin pages 1-2)
RAS is anchored to membranes; accordingly, RasGAP modular domains are interpreted as contributing to localization. A Ras-regulator review explicitly lists RASAL2’s PH and C2 domains and discusses such domains as mediating membrane targeting and interactions enabling Ras engagement at membranes. (stewart2020pumpingthebrakes pages 2-3)
A RasGAP cancer review specifically notes phosphorylation within the PH domain and underscores that membrane localization is important for RasGAP function/activity. (bellazzo2020cuttingthebrakes pages 3-5)
Evidence limitation: The retrieved corpus contains general RasGAP-domain architecture and membrane-targeting interpretations (PH/C2), but limited direct, RASAL2-specific cell biology (e.g., imaging/localization maps) beyond these review statements; this should be considered when interpreting localization claims as inference from domain architecture rather than a definitive localization atlas. (stewart2020pumpingthebrakes pages 2-3, bellazzo2020cuttingthebrakes pages 3-5)
A mechanistic Autophagy study (Feb 2021) reports a detailed regulatory model connecting RASAL2 to nutrient stress and autophagy:
This work explicitly states that RASAL2 S351 phosphorylation functions as a molecular switch that can convert RASAL2 from an autophagy suppressor into an autophagy activator, and links this to breast tumor growth and poor outcomes (qualitatively described in the excerpt). (bao2021prkaaampkαphosphorylationswitches pages 1-3)
A phosphoproteomics-driven study of LKB1 signaling identifies RASAL2 as an LKB1-dependent phosphoprotein (>2-fold in both attached and detached datasets) and proposes candidate AMPK-related phosphorylation sites: S56, S89, S736, S864, S899. LKB1-dependent phosphorylation increases are reported at S89, S736, and S864, with genetic data implicating MARK kinases and SIK family members (notably SIK1+SIK3) in detachment-associated phosphorylation patterns; AMPK contributes partially in some assays. (kamireddy2020aquantitativephosphoproteomicsa pages 50-55, kamireddy2020aquantitativephosphoproteomicsa pages 55-59)
A RasGAP cancer review notes that RASAL2 can be phosphorylated on Ser237 within the PH domain (review statement), consistent with the broader theme that regulatory phosphorylation can tune RasGAP localization or function. (bellazzo2020cuttingthebrakes pages 3-5)
A 2023 study in cervical cancer (BIOCELL; Jan 2023) reports:
This study uses overexpression/knockdown in HeLa/SiHa cells to show functional suppression of proliferation/migration/invasion and induction of apoptosis with RASAL2 restoration. (chen2023rasal2actsas pages 3-7)
A 2024 review (Cell Death & Differentiation; Jun 2024) highlights that DAB2IP is a RasGAP and adaptor modulating multiple oncogenic pathways (NF-κB, Wnt/β-catenin, PI3K/AKT, MAPK) and explicitly notes functional cooperation with RASAL2 in limiting metastasis in ER+ breast cancer; the review frames restoration/upregulation of DAB2IP as a potential strategy that concurrently dampens multiple oncogenic pathways. (fania2024anupdateon pages 1-2, fania2024anupdateon pages 2-3)
A 2024 JCI Insight paper (Dec 2024) further contextualizes RasGAP loss as clinically meaningful in ER+ breast cancer, noting that DAB2IP loss often co-occurs with RASAL2 loss and that such RasGAP-loss states are associated with poorer outcomes, with an explicit statement that co-loss promotes poorer outcome in ~50% of Luminal B breast cancer. (mukherjee2024dab2iplossin pages 1-2)
The strongest “real-world” implementation supported by the retrieved evidence is risk stratification based on RasGAP expression patterns.
In luminal B breast cancer, Olsen et al. (Cancer Discovery; Feb 2017) report tumor subsets with low RASAL2 and/or DAB2IP, including 16% low RASAL2, 24% low DAB2IP, and 22% low both. The combined low-expression state stratifies relapse-free survival with a highly significant log-rank P = 3.1×10⁻⁸. (olsen2017lossofrasgap pages 5-6, olsen2017lossofrasgap media 3a556391)
These quantitative patterns are visually supported by the paper’s figures: the low-expression distribution (pie chart) and Kaplan–Meier plot are available as extracted figure crops. (olsen2017lossofrasgap media 3a556391, olsen2017lossofrasgap media 8e13ab1a)
The same study provides preclinical “implementation” in the sense of actionable mechanistic circuitry: reconstitution of both RASAL2 and DAB2IP markedly reduced metastasis versus single-gene reconstitution controls in luminal breast cancer models (reported P values include P=0.043 vs RASAL2 alone, P=0.002 vs DAB2IP alone, and bioluminescence total flux P=0.004). (olsen2017lossofrasgap pages 7-8)
The authors also report clinical associations with stage: tumors lacking both genes were enriched for stage II–IV disease and differed from tumors expressing both genes (P<0.05), consistent with a metastasis/aggressiveness linkage. (olsen2017lossofrasgap pages 6-7)
Using the clinical-trial search tool with “RASAL2” did not yield RASAL2-targeted interventional trials; the retrieved trial appears unrelated to RASAL2 biology, suggesting the term does not map cleanly to trial metadata in this interface. Therefore, current “applications” are better supported as biomarker/prognostic or mechanistic pathway uses rather than direct RASAL2-targeted therapeutics in clinical trials (based on available evidence). (mukherjee2024dab2iplossin pages 1-2)
A consistent expert synthesis across RasGAP-focused reviews is that Ras pathway hyperactivation can arise not only from RAS mutations but also from defects in RAS regulators, including RasGAP loss/inactivation; RasGAPs are modular proteins whose noncatalytic domains contribute to localization and regulatory interactions, meaning “RasGAP loss” can rewire signaling beyond simply increasing Ras-GTP. (stewart2020pumpingthebrakes pages 2-3, bellazzo2020cuttingthebrakes pages 3-5)
The 2024 DAB2IP review explicitly uses the RASAL2/DAB2IP cooperation as an example of nonredundant tumor-suppressive RasGAP circuitry in ER+ breast cancer metastasis and frames this as relevant to therapeutic thinking—particularly strategies that restore RasGAP function to dampen multiple oncogenic pathways simultaneously (in that review, emphasized for DAB2IP). (fania2024anupdateon pages 1-2)
Extracted figure regions from Olsen et al. (Cancer Discovery 2017) provide visual documentation of (i) the distribution of low RASAL2/DAB2IP expression states in luminal B tumors and (ii) the relapse-free survival stratification by combined RasGAP status, plus a schematic model for cooperative regulation of RAS and NF-κB signaling in metastasis. (olsen2017lossofrasgap media 3a556391, olsen2017lossofrasgap media 2deeb97b)
| Claim/Topic | Key finding | Evidence type | Source | Publication date | URL/DOI |
|---|---|---|---|---|---|
| Target identity / core function | Human RASAL2 corresponds to RAS protein activator like 2 / nGAP, a RasGAP-family protein of 1,139 aa; RasGAPs accelerate conversion of RAS-GTP to RAS-GDP, thereby suppressing RAS signaling (stewart2020pumpingthebrakes pages 2-3) | Review / domain summary | Stewart, Journal of Cell Science | Feb 2020 | https://doi.org/10.1242/jcs.238865 |
| Domains | RASAL2 is described as containing PH, C2, and C-terminal RasGAP domains; noncatalytic domains are implicated in membrane targeting/interactions needed to position RasGAPs near membrane-associated RAS (stewart2020pumpingthebrakes pages 2-3) | Review | Stewart, Journal of Cell Science | Feb 2020 | https://doi.org/10.1242/jcs.238865 |
| Family / current understanding | Review classifies RASAL2 among cytoplasmic RasGAPs and notes that loss of RasGAPs can elevate Ras pathway output; RASAL2 has context-dependent tumor-suppressive or oncogenic roles across cancers (bellazzo2020cuttingthebrakes pages 3-5, stewart2020pumpingthebrakes pages 2-3) | Review | Bellazzo, Cancers; Stewart, Journal of Cell Science | Oct 2020; Feb 2020 | https://doi.org/10.3390/cancers12103066 ; https://doi.org/10.1242/jcs.238865 |
| Localization | Review evidence indicates PH and C2 domains promote constitutive plasma membrane association, and RASAL2 associates with membranes at the leading edge; however, detailed RASAL2-specific mechanistic localization data remain limited in gathered evidence (olsen2017lossofrasgap pages 5-6) (olsen2017lossofrasgap pages 5-6) | Review / inferred from family biology | King, Science Signaling | Feb 2013 | https://doi.org/10.1126/scisignal.2003669 |
| Regulation / PTM | Review notes RASAL2 can be phosphorylated on Ser237 within the PH domain and that membrane localization is important for RasGAP activity (bellazzo2020cuttingthebrakes pages 3-5) | Review | Bellazzo, Cancers | Oct 2020 | https://doi.org/10.3390/cancers12103066 |
| Regulation / PTM | AMPK (PRKAA) phosphorylates RASAL2 at S351 under glucose starvation; this promotes dissociation from PPM1B and enables phosphorylated RASAL2 to bind the PIK3C3/VPS34-ATG14-BECN1 complex, increasing PIK3C3 activity and autophagy (bao2021prkaaampkαphosphorylationswitches pages 1-3, bao2021prkaaampkαphosphorylationswitches pages 3-4) | Primary; cell biology / autophagy assays | Bao, Autophagy | Feb 2021 | https://doi.org/10.1080/15548627.2021.1886767 |
| Binding partners / mechanism | Under basal conditions RASAL2 recruits PPM1B/pp2cβ to attenuate AMPK phosphorylation; glucose starvation causes PPM1B dissociation and converts RASAL2 into an autophagy activator via the VPS34 complex (bao2021prkaaampkαphosphorylationswitches pages 1-3, bao2021prkaaampkαphosphorylationswitches pages 3-4) | Primary; interaction and functional assays | Bao, Autophagy | Feb 2021 | https://doi.org/10.1080/15548627.2021.1886767 |
| Functional nuance | RASAL2’s inhibition of basal autophagy is reported to be independent of RasGAP catalytic activity, although the GAP domain is required for this inhibitory role (bao2021prkaaampkαphosphorylationswitches pages 3-4) | Primary; KO/rescue functional assays | Bao, Autophagy | Feb 2021 | https://doi.org/10.1080/15548627.2021.1886767 |
| Regulation / phosphoproteomics | LKB1-dependent phosphoproteomics identified candidate AMPK-related phosphorylation sites on RASAL2: S56, S89, S736, S864, S899; phosphoenriched data showed LKB1-dependent increases at S89, S736, S864 (kamireddy2020aquantitativephosphoproteomicsa pages 50-55, kamireddy2020aquantitativephosphoproteomics pages 50-55) | Primary; phosphoproteomics | Kamireddy, phosphoproteomics study | 2020 | URL not available in gathered evidence |
| Upstream kinases | In detachment settings, SIK1 + SIK3 knockout/knockdown abolished the LKB1-dependent AMPK-motif phospho-signal on RASAL2; AMPK contributed partially; MARKs were also implicated for some sites (kamireddy2020aquantitativephosphoproteomics pages 50-55, kamireddy2020aquantitativephosphoproteomicsa pages 55-59, kamireddy2020aquantitativephosphoproteomics pages 55-59) | Primary; phosphoproteomics / IP / kinase KO | Kamireddy, phosphoproteomics study | 2020 | URL not available in gathered evidence |
| Pathways | In cancer literature, RASAL2 loss is linked to enhanced Ras–ERK/MAPK signaling; context-dependent reports also connect RASAL2 to YAP, Wnt/β-catenin, PI3K/AKT, and Rac1 signaling (bellazzo2020cuttingthebrakes pages 3-5, bao2021prkaaampkαphosphorylationswitches pages 1-3) | Review + primary mechanistic context | Bellazzo, Cancers; Bao, Autophagy | Oct 2020; Feb 2021 | https://doi.org/10.3390/cancers12103066 ; https://doi.org/10.1080/15548627.2021.1886767 |
| Disease / breast cancer cohort | In luminal B breast tumors, 16% showed low RASAL2, 24% low DAB2IP, and 22% low expression of both; combined low expression strongly stratified relapse-free survival (log-rank P = 3.1e-08) (olsen2017lossofrasgap pages 5-6, olsen2017lossofrasgap media 3a556391) | Primary; patient cohort / Kaplan–Meier | Olsen, Cancer Discovery | Feb 2017 | https://doi.org/10.1158/2159-8290.CD-16-0520 |
| Disease / metastasis mechanism | In luminal breast cancer models, RASAL2 and DAB2IP cooperate to suppress metastasis; reconstitution of both genes reduced metastasis versus single-gene reconstitution or control (P = 0.043 vs RASAL2 alone; P = 0.002 vs DAB2IP alone; total flux P = 0.004) (olsen2017lossofrasgap pages 7-8) | Primary; xenograft / intracardiac metastasis assays | Olsen, Cancer Discovery | Feb 2017 | https://doi.org/10.1158/2159-8290.CD-16-0520 |
| Disease / metastatic phenotypes | In McNeu luminal mouse cancer cells, shRNA codepletion of Rasal2 + Dab2ip significantly increased metastatic lung lesions after tail-vein injection (P = 0.0019) (olsen2017lossofrasgap pages 7-8) | Primary; mouse metastasis assay | Olsen, Cancer Discovery | Feb 2017 | https://doi.org/10.1158/2159-8290.CD-16-0520 |
| Disease / tumor growth | In CAMA1 xenografts, RASAL2 or DAB2IP suppression significantly affected tumor formation/growth (reported P values for individual perturbations include 0.0043, 0.0087 for DAB2IP guides and 0.0016, 0.0022 for RASAL2 shRNAs); combined suppression also reported with P = 0.008, though legend notes no statistically significant increase in tumor volume upon combined suppression (olsen2017lossofrasgap pages 5-6) | Primary; xenograft / CRISPR-shRNA | Olsen, Cancer Discovery | Feb 2017 | https://doi.org/10.1158/2159-8290.CD-16-0520 |
| Clinical relevance / expert view | Reviews emphasize that RASAL2 behaves as a context-dependent RasGAP regulator: often tumor suppressive when expression is lost and Ras signaling rises, but in some settings capable of promoting EMT/metastatic programs through noncanonical pathway wiring (bellazzo2020cuttingthebrakes pages 3-5, bao2021prkaaampkαphosphorylationswitches pages 1-3) | Review / expert synthesis | Bellazzo, Cancers; Bao, Autophagy | Oct 2020; Feb 2021 | https://doi.org/10.3390/cancers12103066 ; https://doi.org/10.1080/15548627.2021.1886767 |
Table: This table compiles the key evidence gathered for human RASAL2, covering molecular function, domains, localization, regulation, pathways, and disease relevance. It highlights residue-level PTMs, pathway interactions, and clinically relevant statistics from breast cancer studies.
References
(stewart2020pumpingthebrakes pages 2-3): Desmond R. Harrell Stewart and Geoffrey J. Clark. Pumping the brakes on ras – negative regulators and death effectors of ras. Journal of Cell Science, Feb 2020. URL: https://doi.org/10.1242/jcs.238865, doi:10.1242/jcs.238865. This article has 35 citations and is from a domain leading peer-reviewed journal.
(bellazzo2020cuttingthebrakes pages 3-5): Arianna Bellazzo and Licio Collavin. Cutting the brakes on ras—cytoplasmic gaps as targets of inactivation in cancer. Cancers, 12:3066, Oct 2020. URL: https://doi.org/10.3390/cancers12103066, doi:10.3390/cancers12103066. This article has 21 citations.
(olsen2017lossofrasgap pages 11-11): Sarah Naomi Olsen, Ania Wronski, Zafira Castaño, Benjamin Dake, Clare Malone, Thomas De Raedt, Miriam Enos, Yoko S. DeRose, Wenhui Zhou, Stephanie Guerra, Massimo Loda, Alana Welm, Ann H. Partridge, Sandra S. McAllister, Charlotte Kuperwasser, and Karen Cichowski. Loss of rasgap tumor suppressors underlies the aggressive nature of luminal b breast cancers. Cancer Discovery, 7(2):202-217, Feb 2017. URL: https://doi.org/10.1158/2159-8290.cd-16-0520, doi:10.1158/2159-8290.cd-16-0520. This article has 72 citations and is from a highest quality peer-reviewed journal.
(olsen2017lossofrasgap pages 5-6): Sarah Naomi Olsen, Ania Wronski, Zafira Castaño, Benjamin Dake, Clare Malone, Thomas De Raedt, Miriam Enos, Yoko S. DeRose, Wenhui Zhou, Stephanie Guerra, Massimo Loda, Alana Welm, Ann H. Partridge, Sandra S. McAllister, Charlotte Kuperwasser, and Karen Cichowski. Loss of rasgap tumor suppressors underlies the aggressive nature of luminal b breast cancers. Cancer Discovery, 7(2):202-217, Feb 2017. URL: https://doi.org/10.1158/2159-8290.cd-16-0520, doi:10.1158/2159-8290.cd-16-0520. This article has 72 citations and is from a highest quality peer-reviewed journal.
(olsen2017lossofrasgap pages 7-8): Sarah Naomi Olsen, Ania Wronski, Zafira Castaño, Benjamin Dake, Clare Malone, Thomas De Raedt, Miriam Enos, Yoko S. DeRose, Wenhui Zhou, Stephanie Guerra, Massimo Loda, Alana Welm, Ann H. Partridge, Sandra S. McAllister, Charlotte Kuperwasser, and Karen Cichowski. Loss of rasgap tumor suppressors underlies the aggressive nature of luminal b breast cancers. Cancer Discovery, 7(2):202-217, Feb 2017. URL: https://doi.org/10.1158/2159-8290.cd-16-0520, doi:10.1158/2159-8290.cd-16-0520. This article has 72 citations and is from a highest quality peer-reviewed journal.
(fania2024anupdateon pages 1-2): Rossella De Florian Fania, Arianna Bellazzo, and Licio Collavin. An update on the tumor-suppressive functions of the rasgap protein dab2ip with focus on therapeutic implications. Cell Death and Differentiation, 31:844-854, Jun 2024. URL: https://doi.org/10.1038/s41418-024-01332-3, doi:10.1038/s41418-024-01332-3. This article has 8 citations and is from a domain leading peer-reviewed journal.
(mukherjee2024dab2iplossin pages 1-2): Angana Mukherjee, Rasha T. Kakati, Sarah Van Alsten, Tyler Laws, Aaron L. Ebbs, Daniel P. Hollern, Philip M. Spanheimer, Katherine A. Hoadley, Melissa A. Troester, Jeremy M. Simon, and Albert S. Baldwin. Dab2ip loss in luminal a breast cancer leads to nf-κb–associated aggressive oncogenic phenotypes. Dec 2024. URL: https://doi.org/10.1172/jci.insight.171705, doi:10.1172/jci.insight.171705. This article has 4 citations and is from a domain leading peer-reviewed journal.
(bao2021prkaaampkαphosphorylationswitches pages 1-3): Yong Bao, Christopher Qian, Meng-Yue Liu, Fei Jiang, Xiaoxiao Jiang, Huijuan Liu, Zhuqing Zhang, Fanghui Sun, Ningwei Fu, Zhaoyuan Hou, Ya Ke, Yan Li, and Zhong-Ming Qian. Prkaa/ampkα phosphorylation switches the role of rasal2 from a suppressor to an activator of autophagy. Feb 2021. URL: https://doi.org/10.1080/15548627.2021.1886767, doi:10.1080/15548627.2021.1886767. This article has 22 citations and is from a domain leading peer-reviewed journal.
(bao2021prkaaampkαphosphorylationswitches pages 3-4): Yong Bao, Christopher Qian, Meng-Yue Liu, Fei Jiang, Xiaoxiao Jiang, Huijuan Liu, Zhuqing Zhang, Fanghui Sun, Ningwei Fu, Zhaoyuan Hou, Ya Ke, Yan Li, and Zhong-Ming Qian. Prkaa/ampkα phosphorylation switches the role of rasal2 from a suppressor to an activator of autophagy. Feb 2021. URL: https://doi.org/10.1080/15548627.2021.1886767, doi:10.1080/15548627.2021.1886767. This article has 22 citations and is from a domain leading peer-reviewed journal.
(kamireddy2020aquantitativephosphoproteomicsa pages 50-55): A Kamireddy. A quantitative phosphoproteomics screen to identify critical targets of the lkb1 tumor suppressor reveals gap proteins for ras superfamily gtpases as novel …. Unknown journal, 2020.
(kamireddy2020aquantitativephosphoproteomicsa pages 55-59): A Kamireddy. A quantitative phosphoproteomics screen to identify critical targets of the lkb1 tumor suppressor reveals gap proteins for ras superfamily gtpases as novel …. Unknown journal, 2020.
(chen2023rasal2actsas pages 1-2): LI CHEN, FANGFANG LI, SHOUYAN CAO, XIA LI, CHAO ZHOU, SAI HAN, and YOUZHONG ZHANG. Rasal2 acts as a tumor suppressor in cervical cancer cells. BIOCELL, 47:1549-1560, Jan 2023. URL: https://doi.org/10.32604/biocell.2023.027308, doi:10.32604/biocell.2023.027308. This article has 0 citations and is from a peer-reviewed journal.
(chen2023rasal2actsas pages 3-7): LI CHEN, FANGFANG LI, SHOUYAN CAO, XIA LI, CHAO ZHOU, SAI HAN, and YOUZHONG ZHANG. Rasal2 acts as a tumor suppressor in cervical cancer cells. BIOCELL, 47:1549-1560, Jan 2023. URL: https://doi.org/10.32604/biocell.2023.027308, doi:10.32604/biocell.2023.027308. This article has 0 citations and is from a peer-reviewed journal.
(fania2024anupdateon pages 2-3): Rossella De Florian Fania, Arianna Bellazzo, and Licio Collavin. An update on the tumor-suppressive functions of the rasgap protein dab2ip with focus on therapeutic implications. Cell Death and Differentiation, 31:844-854, Jun 2024. URL: https://doi.org/10.1038/s41418-024-01332-3, doi:10.1038/s41418-024-01332-3. This article has 8 citations and is from a domain leading peer-reviewed journal.
(olsen2017lossofrasgap media 3a556391): Sarah Naomi Olsen, Ania Wronski, Zafira Castaño, Benjamin Dake, Clare Malone, Thomas De Raedt, Miriam Enos, Yoko S. DeRose, Wenhui Zhou, Stephanie Guerra, Massimo Loda, Alana Welm, Ann H. Partridge, Sandra S. McAllister, Charlotte Kuperwasser, and Karen Cichowski. Loss of rasgap tumor suppressors underlies the aggressive nature of luminal b breast cancers. Cancer Discovery, 7(2):202-217, Feb 2017. URL: https://doi.org/10.1158/2159-8290.cd-16-0520, doi:10.1158/2159-8290.cd-16-0520. This article has 72 citations and is from a highest quality peer-reviewed journal.
(olsen2017lossofrasgap media 8e13ab1a): Sarah Naomi Olsen, Ania Wronski, Zafira Castaño, Benjamin Dake, Clare Malone, Thomas De Raedt, Miriam Enos, Yoko S. DeRose, Wenhui Zhou, Stephanie Guerra, Massimo Loda, Alana Welm, Ann H. Partridge, Sandra S. McAllister, Charlotte Kuperwasser, and Karen Cichowski. Loss of rasgap tumor suppressors underlies the aggressive nature of luminal b breast cancers. Cancer Discovery, 7(2):202-217, Feb 2017. URL: https://doi.org/10.1158/2159-8290.cd-16-0520, doi:10.1158/2159-8290.cd-16-0520. This article has 72 citations and is from a highest quality peer-reviewed journal.
(olsen2017lossofrasgap pages 6-7): Sarah Naomi Olsen, Ania Wronski, Zafira Castaño, Benjamin Dake, Clare Malone, Thomas De Raedt, Miriam Enos, Yoko S. DeRose, Wenhui Zhou, Stephanie Guerra, Massimo Loda, Alana Welm, Ann H. Partridge, Sandra S. McAllister, Charlotte Kuperwasser, and Karen Cichowski. Loss of rasgap tumor suppressors underlies the aggressive nature of luminal b breast cancers. Cancer Discovery, 7(2):202-217, Feb 2017. URL: https://doi.org/10.1158/2159-8290.cd-16-0520, doi:10.1158/2159-8290.cd-16-0520. This article has 72 citations and is from a highest quality peer-reviewed journal.
(olsen2017lossofrasgap media 2deeb97b): Sarah Naomi Olsen, Ania Wronski, Zafira Castaño, Benjamin Dake, Clare Malone, Thomas De Raedt, Miriam Enos, Yoko S. DeRose, Wenhui Zhou, Stephanie Guerra, Massimo Loda, Alana Welm, Ann H. Partridge, Sandra S. McAllister, Charlotte Kuperwasser, and Karen Cichowski. Loss of rasgap tumor suppressors underlies the aggressive nature of luminal b breast cancers. Cancer Discovery, 7(2):202-217, Feb 2017. URL: https://doi.org/10.1158/2159-8290.cd-16-0520, doi:10.1158/2159-8290.cd-16-0520. This article has 72 citations and is from a highest quality peer-reviewed journal.
(kamireddy2020aquantitativephosphoproteomics pages 50-55): A Kamireddy. A quantitative phosphoproteomics screen to identify critical targets of the lkb1 tumor suppressor reveals gap proteins for ras superfamily gtpases as novel …. Unknown journal, 2020.
(kamireddy2020aquantitativephosphoproteomics pages 55-59): A Kamireddy. A quantitative phosphoproteomics screen to identify critical targets of the lkb1 tumor suppressor reveals gap proteins for ras superfamily gtpases as novel …. Unknown journal, 2020.