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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 requested target is unambiguous: human MAP2K5 encodes dual-specificity mitogen-activated protein kinase kinase 5 (MEK5/MKK5; UniProt Q13163). The canonical protein is reported as 448 amino acids and approximately 50.1 kDa, with an N-terminal PB1 interaction domain and a C-terminal STE-family protein-kinase domain. These features agree with the supplied UniProt identity and InterPro domain assignments; literature concerning other genes or organisms was excluded. (fernandez2021resumendetesis. pages 64-68, fernandez2021resumendetesis.a pages 64-68)
MEK5 has an unusually narrow established physiological specificity. Activated principally by MEKK2/MAP3K2 and MEKK3/MAP3K3, it phosphorylates the activation-loop TEY motif of ERK5/MAPK7 at Thr218 and Tyr220. ERK5 remains the only firmly established direct physiological substrate of MEK5. MEK5 therefore functions primarily as the dedicated MAP2K of the MEKK2/3–MEK5–ERK5 signaling module, rather than as a broadly acting kinase. (fernandez2021resumendetesis. pages 68-72, gil2023mapkinaseerk5 pages 50-53, fernandez2021resumendetesis.a pages 68-72)
The strongest physiological interpretation is that MEK5 couples mitogenic and mechanical/stress inputs to ERK5-dependent responses, especially endothelial survival, flow sensing and vascular integrity. Cancer, drug resistance and metabolic associations are important research areas, but most such evidence concerns the entire MEK5–ERK5 axis rather than a uniquely demonstrated action of MAP2K5. Selective research inhibitors exist, but the reviewed evidence did not identify an approved MEK5-directed therapy or a selective MEK5 inhibitor with demonstrated efficacy in a human interventional trial. (drew2012mek5erk5pathwaythe pages 1-2, fernandez2021resumendetesis.a pages 77-80, drew2012mek5erk5pathwaythe pages 11-12)
| Topic | Best-supported conclusion | Key quantitative/detail | Evidence strength/caveat |
|---|---|---|---|
| Identity | MAP2K5 is the human gene encoding dual-specificity MAP kinase kinase 5 (MEK5/MKK5), corresponding to UniProt Q13163; the requested gene and protein are unambiguously matched. | Located at 15q23; canonical protein reported as 448 aa, approximately 50.1 kDa. (fernandez2021resumendetesis. pages 64-68, fernandez2021resumendetesis.a pages 64-68) | Strong database-supported identity. One secondary source reports inconsistent coordinates/length, so the UniProt-linked 448-aa annotation is preferred. (gil2023mapkinaseerk5 pages 50-53) |
| Architecture | MEK5 is a STE-family MAP2K with an N-terminal PB1 interaction domain and a C-terminal dual-specificity protein-kinase domain. | PB1: approximately residues 18–109; kinase domain: approximately 166–409. PB1 residues 18–25 support ERK5 binding, whereas 64–68 support MAP3K2/3 binding. (fernandez2021resumendetesis. pages 64-68, fernandez2021resumendetesis.a pages 64-68) | Strong domain annotation plus interaction evidence; exact interaction boundaries summarized mainly from secondary literature. |
| Upstream activation | MEKK2/MAP3K2 and MEKK3/MAP3K3 bind MEK5 through PB1-domain interactions and activate it by phosphorylation; MEKK2 is generally considered the stronger MEK5-binding activator. | Activating sites are Ser311 and Thr315. PB1-complex disruption inhibits MEK5α activation. (fernandez2021resumendetesis. pages 68-72, fernandez2021resumendetesis.a pages 68-72, drew2012mek5erk5pathwaythe pages 2-4) | Strong biochemical/pathway evidence, although the dominant upstream kinase depends on stimulus and cell type. |
| Catalytic reaction and direct substrate | MEK5 transfers phosphate from ATP to both threonine and tyrosine in the ERK5 activation loop: ATP + ERK5 → ADP + phospho-ERK5. ERK5/MAPK7 is the only firmly established direct physiological substrate. | MEK5 phosphorylates the ERK5 TEY motif at Thr218 and Tyr220; Thr218 is reported to be modified first, and dual phosphorylation is required for full ERK5 activation. (fernandez2021resumendetesis. pages 68-72, gil2023mapkinaseerk5 pages 50-53) | Very strong and specific biochemical evidence. Claims about downstream transcription factors describe ERK5 substrates, not direct MEK5 substrates. |
| Localization | MEK5 is predominantly cytosolic, where it assembles with upstream MAP3Ks and ERK5. Activated ERK5—not necessarily MEK5—undergoes regulated nuclear translocation. | ERK5 contains its own reported NLS at 505–539 and NES at 771–816; these should not be misattributed to MEK5. (fernandez2021resumendetesis.a pages 64-68, fernandez2021resumendetesis. pages 64-68) | MEK5 localization evidence is less detailed than ERK5 trafficking evidence; many publications discuss the localization of the downstream kinase rather than MEK5 itself. |
| Isoforms | Alternative splicing produces multiple annotated forms; the best-studied are full-length MEK5α and an N-terminally truncated MEK5β. MEK5α efficiently activates ERK5, whereas MEK5β can behave as a dominant-negative competitor. | The shorter form lacks 89 N-terminal residues and is approximately 40 kDa. Both forms can co-immunoprecipitate with ERK5, but MEK5β interferes with MEK5α–ERK5 association. (fernandez2021resumendetesis.a pages 64-68, cameron2004differentialroleof pages 1-1) | Supported by transfection and co-immunoprecipitation experiments. Historical α/β naming is inconsistent across sources and should be mapped carefully to current UniProt isoforms. |
| Physiological pathway | MEK5 is the central MAP2K in the MEKK2/3–MEK5–ERK5 cascade, coupling mitogens and stresses to ERK5-dependent survival, differentiation and transcription. The best-established organismal context is endothelial mechanotransduction and vascular integrity. | Reported inputs include EGF, VEGF, PDGF, FGF-2, cytokines, oxidative/osmotic stress, hypoxia and fluid shear stress. (fernandez2021resumendetesis. pages 68-72, fernandez2021resumendetesis.a pages 68-72, drew2012mek5erk5pathwaythe pages 1-2) | Strong pathway-level evidence, but broad phenotypes are often inferred from ERK5 perturbation and are not always separable from direct MEK5 function. |
| Pharmacology | BIX02188 and BIX02189 are widely used research inhibitors of MEK5 catalytic activity and suppress ERK5 phosphorylation without inhibiting several tested MAPK-family controls. | Reported MEK5 IC50 values: 4.3 nM for BIX02188 and 1.5 nM for BIX02189; CSF1R is a reported off-target. (fernandez2021resumendetesis.a pages 77-80, drew2012mek5erk5pathwaythe pages 11-12) | Useful preclinical probes, not proof of clinical selectivity. Older agents such as U0126 and PD98059 are insufficiently selective; ERK5 inhibitors should not be described as MEK5 inhibitors. |
| Recent 2024 research | Current work mainly examines the broader MEK5–ERK5 pathway rather than discovering a new direct MEK5 reaction. A 2024 breast-cancer systems-pharmacology study prioritized genistein and drug combinations computationally; a major CAD Perturb-seq study recovered endothelial flow programs but did not report a MAP2K5-specific perturbation result. | The CAD study tested genes near GWAS loci in human aortic endothelial cells, achieved an average 40% knockdown, identified 50 programs, and linked 41 genes at 43 CAD signals to endothelial programs. (schnitzler2024convergenceofcoronary pages 9-11, schnitzler2024convergenceofcoronary pages 11-14, schnitzler2024convergenceofcoronary pages 1-4) | Recent findings reinforce pathway relevance but are indirect for MAP2K5. Computational drug prioritization and broader endothelial-flow signatures are hypothesis-generating, not evidence that a MEK5 therapy works in patients. |
| Clinical status | MEK5 remains a research and preclinical therapeutic target; no selective MEK5 inhibitor was identified as approved or as having demonstrated efficacy in a human interventional trial in the reviewed evidence. | Available disease associations include genetics, expression studies and experimental cancer models; Open Targets reports moderate association scores for several traits, approximately 0.31–0.42, but these do not establish causality or therapeutic validation. (OpenTargets Search: -MAP2K5) | Clinical evidence is weak. Cancer-expression associations, pathway inhibition in cells and genetic associations should not be equated with clinical validation, an approved indication or an actionable biomarker. |
Table: Concise evidence map for human MAP2K5/MEK5 (Q13163), separating direct molecular evidence from broader ERK5-axis findings. It highlights quantitative details, evidentiary limitations, and the pathway’s still-preclinical therapeutic status.
Verification result: all required identifiers align.
One retrieved secondary source gave a discordant chromosome band and a 444-residue length; because independent UniProt-linked descriptions agree on 15q23 and 448 residues, those values are preferred. This illustrates why the accession-based identity supplied by the user is more reliable than symbol-only retrieval. (fernandez2021resumendetesis. pages 64-68, fernandez2021resumendetesis.a pages 64-68, gil2023mapkinaseerk5 pages 50-53)
The canonical protein contains an N-terminal PB1 domain, approximately residues 18–109, followed by a kinase domain at approximately residues 166–409. This matches the supplied PB1-like/PB1_MAP2K5, kinase-like and dual-specificity MAPK-kinase annotations. Within the PB1 region, residues 18–25 have been associated with ERK5 binding and residues 64–68 with MAP3K2/3 binding, allowing MEK5 to connect an upstream MAP3K with its downstream MAPK through separable interfaces. Interactions with SQSTM1 and PARD6A have also been reported, although their importance to the core catalytic reaction is less established. (fernandez2021resumendetesis. pages 64-68, fernandez2021resumendetesis.a pages 64-68)
MEK5 is an ATP-dependent dual-specificity protein kinase. Its defining reaction can be summarized as:
ATP + ERK5/MAPK7 → ADP + phosphorylated ERK5/MAPK7
MEK5 phosphorylates both a threonine and a tyrosine in ERK5’s activation-loop Thr-Glu-Tyr (TEY) motif—Thr218 and Tyr220 in human ERK5. Evidence summarized from biochemical work indicates preferential phosphorylation of Thr218 first, followed by Tyr220; phosphorylation of both sites is required for full ERK5 catalytic activation. (fernandez2021resumendetesis. pages 68-72, gil2023mapkinaseerk5 pages 50-53)
The current evidence supports ERK5/MAPK7 as the only firmly recognized direct physiological substrate of MEK5, and MEK5 as the only recognized MAP2K that directly activates ERK5. Accordingly, downstream targets such as MEF2-family transcription factors should be annotated as ERK5 substrates or pathway outputs—not as direct MEK5 substrates. (fernandez2021resumendetesis. pages 68-72, gil2023mapkinaseerk5 pages 50-53, hoang2017oncogenicsignalingof pages 1-5)
This narrow specificity is reinforced structurally by PB1-mediated docking. The PB1 scaffold raises the effective local concentration of MEKK2/3, MEK5 and ERK5 and helps insulate this cascade from canonical ERK1/2, JNK and p38 modules. (drew2012mek5erk5pathwaythe pages 2-4, hoang2017oncogenicsignalingof pages 1-5)
MEK5 occupies the middle tier of a conventional three-kinase MAPK cascade:
stimulus/receptor → MAP3K2/MEKK2 or MAP3K3/MEKK3 → MAP2K5/MEK5 → MAPK7/ERK5 → cytoplasmic and nuclear responses.
MEKK2 and MEKK3 bind the MEK5 PB1 domain and phosphorylate MEK5 at Ser311 and Thr315 within its kinase domain. MEKK2 is generally described as having greater MEK5-binding affinity and as a prominent activator, but upstream usage varies with stimulus and cell type. MEKK1 is not regarded as a corresponding MEK5 activator. (fernandez2021resumendetesis. pages 68-72, fernandez2021resumendetesis.a pages 68-72, drew2012mek5erk5pathwaythe pages 2-4)
Reported inputs include EGF and other growth factors, VEGF, PDGF, FGF-2, neurotrophins, serum, inflammatory cytokines, osmotic and oxidative stress, hypoxia, ischemia and fluid shear stress. WNK1 has been placed further upstream in some EGF-responsive contexts: WNK1 depletion reduced ERK5 activation, whereas WNK1 overexpression increased it in HEK293 cells. This is pathway-level evidence and does not make WNK1 a direct substitute for the established MEKK2/3-to-MEK5 activation step. (fernandez2021resumendetesis. pages 68-72, fernandez2021resumendetesis.a pages 68-72)
MEK5 is reported to be predominantly cytosolic, consistent with its role in assembling upstream MAP3Ks and cytosolic ERK5 into a signaling complex. Its PB1 domain provides the key organizing interfaces in that compartment. (fernandez2021resumendetesis.a pages 64-68)
A critical distinction is that the prominent stimulus-dependent nuclear translocation described in this pathway is chiefly a property of ERK5, not proof that MEK5 itself becomes a nuclear kinase. Inactive ERK5 is retained in a compact cytosolic state; MEK5-dependent activation exposes ERK5 trafficking determinants and promotes ERK5 nuclear entry. Reported ERK5 trafficking regions include an NLS at residues 505–539 and an NES at 771–816. These sequences belong to ERK5 and must not be assigned to MAP2K5. (fernandez2021resumendetesis.a pages 64-68, fernandez2021resumendetesis. pages 64-68, hoang2017oncogenicsignalingof pages 1-5)
Thus, the best-supported compartmental model is: MEK5 executes its primary phosphorylation reaction mainly in the cytosolic signaling complex; activated ERK5 then carries part of the signal into the nucleus.
Four alternatively spliced forms have been reported, although historical α/β nomenclature is not completely consistent across publications. The most studied comparison is between a full-length, approximately 50-kDa form and an approximately 40-kDa form lacking 89 N-terminal residues, including important PB1-region information. (fernandez2021resumendetesis. pages 64-68, fernandez2021resumendetesis.a pages 64-68)
In HEK293 transfection and co-immunoprecipitation experiments, both principal forms could associate with ERK5, but only the full-length form efficiently activated ERK5 and induced its nuclear translocation. The shortened form interfered with association of the activating form with ERK5 and behaved as a dominant-negative regulator. Phosphomimetic substitution at MEK5 Ser311/Thr315 activated ERK5 when introduced into the full-length form but not equivalently in the shortened form. These results demonstrate that activation-loop phosphorylation alone is insufficient for productive signaling when the required N-terminal docking architecture is absent. Cameron et al., published 9 January 2004; DOI: https://doi.org/10.1074/jbc.M308755200. (cameron2004differentialroleof pages 1-1)
Activation of ERK5 by MEK5 has been linked to cell survival, proliferation, differentiation, motility, angiogenesis and stress adaptation. These broad phenotypes should be interpreted as outputs of the MEK5–ERK5 module, because many experiments directly perturb ERK5 rather than separately resolving MEK5’s contribution. (gil2023mapkinaseerk5 pages 50-53, drew2012mek5erk5pathwaythe pages 1-2)
The strongest physiological context is vascular endothelium. Laminar shear stress activates an atheroprotective endothelial program in which the MEK5–ERK5 axis contributes to mechanotransduction, survival, barrier integrity and anti-inflammatory transcription. Reviews regard this as a protective stress-response pathway not only in endothelium but also in mechanically challenged bone, cartilage and muscle. This creates an important therapeutic tension: inhibiting the axis may be useful in tumors that exploit it for survival, but systemic inhibition could impair normal vascular or tissue-protective signaling. (drew2012mek5erk5pathwaythe pages 1-2)
The cascade also responds to oxidative and osmotic stress, ischemia and hypoxia. These observations support annotation as a signaling integrator rather than as an enzyme serving a constitutive metabolic pathway. (fernandez2021resumendetesis. pages 68-72, fernandez2021resumendetesis.a pages 68-72)
Cancer literature commonly reports elevated expression or activation of the pathway. Historical quantitative findings include a 22-fold increase in MAP2K5 expression in apoptosis-resistant MCF7 breast-carcinoma cells and approximately 4–5-fold higher MEK5 protein in DU145 prostate-cancer cells than in comparator transformed lines; elevated expression was also observed in MCF7 and T47D cells. These are cellular-expression observations, not proof that MAP2K5 is an oncogenic driver in patients. (cameron2004differentialroleof pages 7-8)
A review reported strong MEK5 expression in more than one-third of prostate tumors and expression in over half of breast tumors in one study, while emphasizing that relationships among abundance, kinase activation, tumor morphology and prognosis remained incompletely established. The same caution applies to associations with metastasis, epithelial-to-mesenchymal transition and treatment resistance. Drew et al., January 2012; DOI: https://doi.org/10.1016/j.bbcan.2011.10.002. (drew2012mek5erk5pathwaythe pages 1-2)
Genetic or pharmacological disruption of upstream MEKK2 inhibited growth of MDA-MB-231 and BT474 xenografts and reduced triple-negative breast-cancer metastasis in experimental models. This supports vulnerability of the broader cascade, but it does not establish that selective inhibition of MEK5 itself will reproduce the result clinically. Hoang et al., January 2017; DOI: https://doi.org/10.1016/j.canlet.2017.01.034. (hoang2017oncogenicsignalingof pages 1-5)
Open Targets links MAP2K5 to smoking behavior, skeletal-system abnormalities, diabetes, type 2 diabetes and metabolic dysfunction-associated steatotic liver disease, with displayed aggregate association scores of approximately 0.31–0.42. These scores integrate heterogeneous evidence and should be treated as prioritization signals rather than proof of direct causation or therapeutic tractability. (OpenTargets Search: -MAP2K5)
Recent literature has expanded the biological setting of the pathway more than it has altered the core biochemical annotation.
A 2024 study reported that ERK5 supports autocrine mitogenic balance and cell-fate specification in human pluripotent stem cells. The work supports a role for MEK5-dependent ERK5 activation in maintaining signaling and transcriptional programs, but the principal experimentally interrogated molecule was ERK5; it does not establish a new direct MAP2K5 substrate. Song et al., September 2024; DOI: https://doi.org/10.1016/j.stemcr.2024.07.007.
A 2024 systems-pharmacology analysis constructed perturbed protein-interaction networks and prioritized genistein among plant polyphenols, together with candidate combinations involving established breast-cancer drugs. This is a computational prioritization of interventions affecting the MEK5–ERK5 network, not evidence that genistein selectively binds MEK5 or that the combinations are clinically effective. Odongo et al., February 2024; DOI: https://doi.org/10.1186/s13040-024-00357-1.
Schnitzler et al. integrated CAD GWAS, endothelial epigenomics, enhancer-to-gene maps and CRISPRi Perturb-seq in telomerase-immortalized human aortic endothelial cells. The screen targeted expressed genes within 500 kb of CAD signals, achieved an average 40% expression reduction, identified 50 transcriptional programs, and connected 41 genes at 43 CAD signals to endothelial programs. It recovered a flow-response program and endothelial-to-mesenchymal transition, reinforcing the importance of endothelial mechanotransduction; however, the retrieved study sections did not provide a MAP2K5-specific perturbation result. It should therefore be cited as current contextual evidence, not direct validation of MAP2K5 as a CAD gene. Published February 2024; DOI: https://doi.org/10.1038/s41586-024-07022-x. (schnitzler2024convergenceofcoronary pages 9-11, schnitzler2024convergenceofcoronary pages 11-14, schnitzler2024convergenceofcoronary pages 1-4)
The study’s broader quantitative results included strong support for the 41-gene set by PoPS (rank-sum P = 2.5 × 10⁻53). CCM2 knockdown increased GOSR2 by 122% (P = 8.9 × 10⁻7), while GOSR2 knockdown increased an ER-stress program by 94% and reduced a focal-adhesion/JUN program by 23%. These data concern neighboring endothelial programs rather than direct MEK5 biochemistry. (schnitzler2024convergenceofcoronary pages 9-11)
The principal real-world application is as a research target and pathway biomarker, using genetic perturbation, phospho-ERK5 readouts and small-molecule probes to investigate stress signaling, endothelial biology and tumor-cell adaptation.
BIX02188 and BIX02189 are commonly used MEK5 inhibitors. Reported biochemical IC50 values are 4.3 nM and 1.5 nM, respectively. Both suppress ERK5 phosphorylation and MEF2-driven transcription without inhibiting several tested control kinases, including MEK1, MEK2, ERK2 and JNK2; however, CSF1R is a reported off-target, and cellular or organismal selectivity cannot be inferred from a limited kinase panel. (fernandez2021resumendetesis.a pages 77-80, drew2012mek5erk5pathwaythe pages 11-12)
Older reagents require caution. U0126 can inhibit MEK5 dose-dependently, while PD98059 partially inhibits it, so studies using these compounds cannot automatically attribute effects solely to MEK1/2–ERK1/2. Conversely, XMD8-92, ERK5-IN-1, AX15836 and BAY-885 are primarily ERK5-directed compounds and should not be called MEK5 inhibitors. Some ERK5 kinase inhibitors can paradoxically promote ERK5 nuclear localization or transcriptional activity and may fail to phenocopy ERK5 genetic deletion. (fernandez2021resumendetesis.a pages 77-80, drew2012mek5erk5pathwaythe pages 12-14, drew2012mek5erk5pathwaythe pages 11-12)
No selective MEK5 inhibitor was identified as an approved drug or as having demonstrated efficacy in a human interventional trial in the evidence reviewed here. Consequently, therapeutic claims remain preclinical, and no clinically validated MAP2K5 biomarker, companion diagnostic or standard-of-care implementation can presently be assigned.
Human MAP2K5/Q13163 is a cytosolic, PB1-containing STE-family MAP2K whose precise function is to activate ERK5/MAPK7 through dual phosphorylation of its TEY activation loop. MEKK2 and MEKK3 activate MEK5 at Ser311/Thr315, while PB1-mediated assembly confers pathway specificity. The protein’s best-supported physiological role is as the central relay of a mitogen- and stress-responsive pathway, particularly in endothelial mechanotransduction and tissue-protective signaling. Cancer and complex-trait associations are biologically plausible and experimentally active areas, but translation remains preclinical. The central annotation should therefore emphasize the highly specific MEKK2/3–MEK5–ERK5 reaction, with broader phenotypes and therapeutic claims recorded as context-dependent pathway consequences rather than intrinsic molecular functions.
References
(fernandez2021resumendetesis. pages 64-68): A Sánchez Fernández. Resumen de tesis. the mek5/erk5 pathway in lung and ovarian cancer. Unknown journal, 2021.
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(fernandez2021resumendetesis. pages 68-72): A Sánchez Fernández. Resumen de tesis. the mek5/erk5 pathway in lung and ovarian cancer. Unknown journal, 2021.
(gil2023mapkinaseerk5 pages 50-53): S Espinosa Gil. Map kinase erk5, by controlling tp53inp2 proteostasis, modulates cancer cell sensitivity to extrinsic apoptosis induced by death-receptor agonists. Unknown journal, 2023.
(fernandez2021resumendetesis.a pages 68-72): A Sánchez Fernández. Resumen de tesis. the mek5/erk5 pathway in lung and ovarian cancer. Unknown journal, 2021.
(drew2012mek5erk5pathwaythe pages 1-2): Barbara A. Drew, Matthew E. Burow, and Barbara S. Beckman. Mek5/erk5 pathway: the first fifteen years. Biochimica et biophysica acta, 1825 1:37-48, Jan 2012. URL: https://doi.org/10.1016/j.bbcan.2011.10.002, doi:10.1016/j.bbcan.2011.10.002. This article has 283 citations.
(fernandez2021resumendetesis.a pages 77-80): A Sánchez Fernández. Resumen de tesis. the mek5/erk5 pathway in lung and ovarian cancer. Unknown journal, 2021.
(drew2012mek5erk5pathwaythe pages 11-12): Barbara A. Drew, Matthew E. Burow, and Barbara S. Beckman. Mek5/erk5 pathway: the first fifteen years. Biochimica et biophysica acta, 1825 1:37-48, Jan 2012. URL: https://doi.org/10.1016/j.bbcan.2011.10.002, doi:10.1016/j.bbcan.2011.10.002. This article has 283 citations.
(drew2012mek5erk5pathwaythe pages 2-4): Barbara A. Drew, Matthew E. Burow, and Barbara S. Beckman. Mek5/erk5 pathway: the first fifteen years. Biochimica et biophysica acta, 1825 1:37-48, Jan 2012. URL: https://doi.org/10.1016/j.bbcan.2011.10.002, doi:10.1016/j.bbcan.2011.10.002. This article has 283 citations.
(cameron2004differentialroleof pages 1-1): Scott J. Cameron, Jun-ichi Abe, Sundeep Malik, Wenyi Che, and Jay Yang. Differential role of mek5α and mek5β in bmk1/erk5 activation. Journal of Biological Chemistry, 279:1506-1512, Jan 2004. URL: https://doi.org/10.1074/jbc.m308755200, doi:10.1074/jbc.m308755200. This article has 63 citations and is from a domain leading peer-reviewed journal.
(schnitzler2024convergenceofcoronary pages 9-11): Gavin R. Schnitzler, Helen Kang, Shi Fang, Ramcharan S. Angom, Vivian S. Lee-Kim, X. Rosa Ma, Ronghao Zhou, Tony Zeng, Katherine Guo, Martin S. Taylor, Shamsudheen K. Vellarikkal, Aurelie E. Barry, Oscar Sias-Garcia, Alex Bloemendal, Glen Munson, Philine Guckelberger, Tung H. Nguyen, Drew T. Bergman, Stephen Hinshaw, Nathan Cheng, Brian Cleary, Krishna Aragam, Eric S. Lander, Hilary K. Finucane, Debabrata Mukhopadhyay, Rajat M. Gupta, and Jesse M. Engreitz. Convergence of coronary artery disease genes onto endothelial cell programs. Nature, 626:799-807, Feb 2024. URL: https://doi.org/10.1038/s41586-024-07022-x, doi:10.1038/s41586-024-07022-x. This article has 123 citations and is from a highest quality peer-reviewed journal.
(schnitzler2024convergenceofcoronary pages 11-14): Gavin R. Schnitzler, Helen Kang, Shi Fang, Ramcharan S. Angom, Vivian S. Lee-Kim, X. Rosa Ma, Ronghao Zhou, Tony Zeng, Katherine Guo, Martin S. Taylor, Shamsudheen K. Vellarikkal, Aurelie E. Barry, Oscar Sias-Garcia, Alex Bloemendal, Glen Munson, Philine Guckelberger, Tung H. Nguyen, Drew T. Bergman, Stephen Hinshaw, Nathan Cheng, Brian Cleary, Krishna Aragam, Eric S. Lander, Hilary K. Finucane, Debabrata Mukhopadhyay, Rajat M. Gupta, and Jesse M. Engreitz. Convergence of coronary artery disease genes onto endothelial cell programs. Nature, 626:799-807, Feb 2024. URL: https://doi.org/10.1038/s41586-024-07022-x, doi:10.1038/s41586-024-07022-x. This article has 123 citations and is from a highest quality peer-reviewed journal.
(schnitzler2024convergenceofcoronary pages 1-4): Gavin R. Schnitzler, Helen Kang, Shi Fang, Ramcharan S. Angom, Vivian S. Lee-Kim, X. Rosa Ma, Ronghao Zhou, Tony Zeng, Katherine Guo, Martin S. Taylor, Shamsudheen K. Vellarikkal, Aurelie E. Barry, Oscar Sias-Garcia, Alex Bloemendal, Glen Munson, Philine Guckelberger, Tung H. Nguyen, Drew T. Bergman, Stephen Hinshaw, Nathan Cheng, Brian Cleary, Krishna Aragam, Eric S. Lander, Hilary K. Finucane, Debabrata Mukhopadhyay, Rajat M. Gupta, and Jesse M. Engreitz. Convergence of coronary artery disease genes onto endothelial cell programs. Nature, 626:799-807, Feb 2024. URL: https://doi.org/10.1038/s41586-024-07022-x, doi:10.1038/s41586-024-07022-x. This article has 123 citations and is from a highest quality peer-reviewed journal.
(OpenTargets Search: -MAP2K5): Open Targets Query (-MAP2K5, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(hoang2017oncogenicsignalingof pages 1-5): Van T. Hoang, Thomas J. Yan, J. Cavanaugh, P. Flaherty, B. Beckman, and M. Burow. Mek5-erk5 signaling in cancer: implications for targeted therapy. Cancer letters, 392:51-59, Jan 2017. URL: https://doi.org/10.1016/j.canlet.2017.01.034, doi:10.1016/j.canlet.2017.01.034. This article has 92 citations and is from a peer-reviewed journal.
(cameron2004differentialroleof pages 7-8): Scott J. Cameron, Jun-ichi Abe, Sundeep Malik, Wenyi Che, and Jay Yang. Differential role of mek5α and mek5β in bmk1/erk5 activation. Journal of Biological Chemistry, 279:1506-1512, Jan 2004. URL: https://doi.org/10.1074/jbc.m308755200, doi:10.1074/jbc.m308755200. This article has 63 citations and is from a domain leading peer-reviewed journal.
(drew2012mek5erk5pathwaythe pages 12-14): Barbara A. Drew, Matthew E. Burow, and Barbara S. Beckman. Mek5/erk5 pathway: the first fifteen years. Biochimica et biophysica acta, 1825 1:37-48, Jan 2012. URL: https://doi.org/10.1016/j.bbcan.2011.10.002, doi:10.1016/j.bbcan.2011.10.002. This article has 283 citations.