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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity is verified. The requested protein is the budding-yeast Ste11 MAP kinase kinase kinase (MAP3K/MEKK) encoded by STE11/YLR362W in Saccharomyces cerevisiae strain S288c, consistent with UniProt P23561. The literature identifies this protein as a shared upstream kinase in three principal MAPK outputs: pheromone-induced mating, filamentous/invasive growth, and the Sho1 branch of the high-osmolarity glycerol (HOG) response. This target must not be confused with the unrelated Schizosaccharomyces pombe protein called Ste11 or with Ste11 homologs from other fungi.
Ste11’s primary biochemical role is to transfer phosphate from ATP to serine/threonine residues in pathway-specific MAPK kinases. Its best-established physiological substrates are Ste7, in mating and filamentous-growth signaling, and Pbs2, in Sho1-dependent HOG signaling. Its decisive biological role is therefore not simply “a stress kinase,” but a shared MAP3K whose localization into distinct scaffolded complexes routes information to different MAPKs and cellular responses. Direct kinetic constants and a comprehensive physiological substrate map remain limited.
| Aspect | Best-supported annotation | Key evidence/qualification |
|---|---|---|
| Identity | Ste11, encoded by STE11/YLR362W in Saccharomyces cerevisiae S288c; UniProt P23561; a MEKK-family serine/threonine MAP kinase kinase kinase (MAP3K). | Identity matches the supplied accession, locus, organism, kinase family, and literature. It must not be confused with the unrelated Schizosaccharomyces pombe transcription factor Ste11 or Ste11 homologs from other fungi. |
| Molecular function/reaction | ATP-dependent protein serine/threonine kinase: ATP + protein-OH → ADP + phosphoprotein. Its primary signaling function is phosphorylation and activation of pathway-specific MAPK kinases. | Catalytic activity resides in the C-terminal protein-kinase domain. Physiological specificity depends strongly on scaffolds, adaptors, recruitment, and stimulus context rather than on an unrestricted set of cellular substrates. |
| Direct canonical substrates | Ste7 is the canonical MAPKK substrate in mating and filamentous/invasive-growth signaling; Pbs2 is the canonical MAPKK substrate in the Sho1 branch of the HOG pathway. | Ste7 activation has biochemical and genetic support; Ste11-to-Pbs2 signaling is supported by pathway reconstitution, epistasis, interaction, and recruitment studies. Ste50 can also be phosphorylated by Ste11, but it is principally an adaptor rather than a canonical MAPKK output. Reported Cmk2 and Ptk2 connections are putative/context-dependent, and Mpk1/Slt2 activation is indirect; these should not be annotated as equally established direct substrates. |
| Upstream activation | Ste11 is activated principally by the Cdc42-associated PAK-family kinase Ste20 after assembly at the plasma membrane; the adaptor Ste50 promotes recruitment and relieves N-terminal autoinhibition. | Cdc42 mainly organizes and activates Ste20 and recruits Ste50-containing complexes; it is not itself a kinase. Ste50–Ste11 association uses their SAM-containing regions, while pathway-specific membrane anchors and scaffolds bring the module to the appropriate cortical site. |
| Mating pathway | Transmits pheromone-receptor signaling through Ste20 → Ste11 → Ste7 → Fus3/Kss1, producing mating-gene expression, cell-cycle arrest, polarized growth, and cell fusion. | The Ste5 scaffold assembles Ste11, Ste7, and Fus3 and recruits the module to Gβγ-associated plasma-membrane sites. Ste5-dependent organization favors the mating output and helps prevent inappropriate signaling through other Ste11-dependent pathways. |
| Filamentous/invasive growth pathway | Functions in the filamentous-growth MAPK cascade, principally Cdc42/Ste20 → Ste11 → Ste7 → Kss1, which promotes invasive growth in haploids and pseudohyphal development in appropriate diploids. | Surface and nutrient inputs converge through proteins including Msb2, Sho1, Cdc42, Ste50, and Ste20. Ste50’s RA domain is important for delivering the Ste11 complex to the plasma membrane. Phenotypic strength is strain- and condition-dependent, so S288c results should not automatically be generalized to strongly filamentous backgrounds. |
| Sho1–HOG pathway | Serves as the MAP3K of the Sho1 branch: osmosensing complexes activate Ste20/Cla4 → Ste11 → Pbs2 → Hog1, enabling adaptation to hyperosmotic stress. | This role is distinct from the parallel Sln1 branch, which uses Ssk2/Ssk22 rather than Ste11. Sho1–Pbs2 and Opy2–Ste50 assemblies position Pbs2 and Ste11 near one another at the plasma membrane, promoting selective Pbs2 phosphorylation. |
| Localization | Ste11 is primarily a soluble intracellular signaling protein that is transiently recruited to cortical/plasma-membrane complexes where pathway activation occurs; constitutive residence in an organelle is not its defining localization. | In mating, membrane-localized Ste5 positions Ste11 near Ste20. In filamentous growth and Sho1–HOG signaling, Ste50 links Ste11 to Cdc42 or the Opy2-containing membrane complex, while Pbs2 and Sho1 organize the HOG module. Localization is dynamic and pathway dependent. |
| Domain/regulatory architecture | The N terminus is a regulatory and interaction region containing a SAM domain; the C terminus contains the conserved serine/threonine protein-kinase domain and ATP-binding site. | The SAM-containing region binds Ste50. A neighboring N-terminal segment binds Ste5 and participates in inhibitory contacts with the catalytic region. Deletion or activating mutations in the regulatory region can generate constitutive Ste11 activity. The supplied Ras-binding-like annotation should not be interpreted as proving that Ste11 itself is a conventional Ras effector; the best-established RA-domain recruitment function belongs to Ste50. |
| Signaling specificity/crosstalk | One shared MAP3K is routed into different outputs by stimulus-specific complexes: Ste5–Ste7 for mating, Ste7/Kss1 assemblies for filamentation, and Sho1/Pbs2 for HOG. Hog1-dependent feedback and phosphatases further suppress inappropriate cross-activation. | Loss of Hog1 or Pbs2 permits osmotic stress to activate mating-pathway outputs through Sho1, Ste20, Ste50, Ste11, and Ste7. Ste11 has also been linked experimentally to FKS2 and cell-wall-integrity regulation, but Cmk2, Ptk2, and Mpk1/Slt2 effects reflect broader crosstalk and should remain secondary annotations. |
| 2024 update | Concurrent salt and pheromone stimulation revealed that the two HOG branches are not functionally interchangeable: Sho1 sustains Hog1 activation and can promote Kss1-dependent cross-pathway transcription, whereas the Sln1 branch contributes strongly to Hog1 activation amplitude. | The study identified 108 Kss1-responsive genes and strong salt-dependent induction of mating genes under Sho1-dominant conditions, including FUS1, PRM1, and BAR1. It treated Ste11 as shared upstream pathway architecture but did not directly perturb Ste11, so its findings refine the context of Ste11 signaling rather than its catalytic mechanism. |
| Applications/limitations | Ste11-dependent cascades are widely used as model systems for MAPK scaffolding, signal insulation, concurrent-stimulus processing, quantitative signaling, and engineered yeast biosensors; homologous modules also inform fungal stress and virulence research. | Ste11 itself has no established clinical application. Results from engineered constitutively active alleles, other yeast strains, or Ste11 homologs in pathogenic fungi cannot be assigned directly to P23561 without validation. Direct kinetic constants, high-resolution full-length structure, and a comprehensive physiological substrate map remain limited. |
Table: Concise evidence-based annotation of S. cerevisiae S288c Ste11, distinguishing its canonical MAPKK substrates and pathway-specific recruitment from secondary crosstalk. It also summarizes the qualified relevance of recent 2024 signaling results.
The S. cerevisiae literature explicitly identifies STE11/YLR362W as encoding a MEKK-family MAP3K that regulates mating, invasive growth, and osmotic-stress signaling. Its catalytic domain is homologous to mammalian MEKK-family kinases, matching the supplied protein-kinase-superfamily and STE Ser/Thr-family annotation (wang2011ste11pmekksignals pages 1-3).
The experimentally characterized architecture also agrees with the supplied domain annotation. Ste11 has a multifunctional N-terminal regulatory region and a C-terminal kinase domain. Residues 26–129 have SAM-domain similarity and are required for binding the Ste50 adaptor; a neighboring region, approximately residues 133–335, contributes to Ste5 association and negative regulation of catalytic activity. Deletion of this inhibitory region or activating mutations can bypass normal Ste50 dependence (wu1999functionalcharacterizationof pages 12-14, wu1999functionalcharacterizationof pages 10-10). Interaction between the N-terminal regulatory and C-terminal catalytic regions supports an autoinhibitory model, while Ste50 binding can disrupt this interaction and promote Ste11 activation (wu1999functionalcharacterizationof pages 1-2).
The supplied Ras-binding-like domain annotation should be interpreted cautiously. The strongest experimental recruitment mechanism involves the RA domain of Ste50, which links the Ste11–Ste50 complex to membrane-associated proteins, rather than establishing Ste11 itself as a conventional Ras effector (sharmeen2020molecularroleofa pages 38-42, michal2011coordinationofmap pages 117-119).
Ste11 is an ATP-dependent protein serine/threonine kinase classified as a MAP3K. Its generic reaction is:
ATP + protein serine/threonine-OH → ADP + phosphorylated protein.
These are the appropriate substrates for a primary functional annotation. Ste50 can also be phosphorylated by Ste11, but its dominant role is as an adaptor and regulator, not as the principal MAPKK output (wu1999functionalcharacterizationof pages 1-2).
A 2011 study connected activated Ste11 to Pbs2, Ste7, Cmk2, Ptk2, and separate stimulation of Mpk1/Slt2 in regulation of the cell-wall gene FKS2. However, Cmk2 and Ptk2 were described as putative/context-dependent targets, while Mpk1 activation was a pathway-level effect. These should not be treated as having the same direct biochemical status as Ste7 and Pbs2 (wang2011ste11pmekksignals pages 1-3, wang2011ste11pmekksignals pages 13-15).
Ste11 is activated principally by Ste20, a p21-activated kinase associated with active Cdc42. In mating, filamentation, and Sho1-HOG signaling, assembly near the plasma membrane brings Ste11 into proximity with Ste20, enabling activating phosphorylation. Cdc42 is therefore an upstream spatial organizer and Ste20 regulator, not a direct phosphodonor to Ste11 (wang2011ste11pmekksignals pages 1-3, sharmeen2020molecularroleofa pages 38-42).
Ste50 binds Ste11 through SAM-containing N-terminal regions. Biochemical experiments found that Ste50 can relieve the inhibitory interaction between Ste11’s regulatory and catalytic portions and modulate Ste11 autophosphorylation. The Ste11–Ste50 interaction appeared constitutive in pull-down experiments and did not detectably change following α-factor or 0.4 M NaCl, suggesting that regulation depends more on localization, conformation, and partner assembly than on simple inducible binding (wu1999functionalcharacterizationof pages 1-2, wu1999functionalcharacterizationof pages 12-14).
Ste50 is essential for normal Sho1-branch signaling but less absolutely required for mating, where the Ste5 scaffold provides another strong recruitment route. Constitutively active Ste11 alleles can bypass Ste50 requirements, supporting a regulatory rather than downstream catalytic role for Ste50 (wu1999functionalcharacterizationof pages 1-2, wu1999functionalcharacterizationof pages 12-14).
The core kinase sequence is Ste20 → Ste11 → Ste7 → Fus3/Kss1. The Ste5 scaffold binds pathway components and recruits the module to Gβγ-associated plasma-membrane sites following pheromone receptor activation. This assembly positions Ste11 near Ste20 and channels its activity toward Ste7, ultimately producing mating-specific transcription, cell-cycle arrest, polarized “shmoo” growth, and cell fusion (wu1999functionalcharacterizationof pages 1-2, shu2024extrabutnot pages 23-28, sharmeen2020molecularroleof pages 38-42).
Ste5 does more than increase reaction efficiency: it contributes to specificity. It preferentially organizes Ste7 and Fus3, whereas Kss1 has different scaffold dependence. This architecture helps a shared Ste11–Ste7 module produce mating rather than filamentation output (shu2024extrabutnot pages 23-28).
Under appropriate nutrient and surface conditions, Ste11 functions in the filamentous-growth pathway, principally Cdc42/Ste20 → Ste11 → Ste7 → Kss1. Kss1-dependent transcription drives polarized growth, adhesion, haploid invasion, or diploid pseudohyphal development, depending on cell type and genetic background. Ste11 and its activators are shared with other pathways; specificity arises from upstream sensors and spatially organized complexes rather than a filamentation-exclusive Ste11 isoform (wang2011ste11pmekksignals pages 1-3, shu2024extrabutnot pages 23-28).
Ste50’s RA domain is important for delivering Ste11-containing complexes to the plasma membrane during filamentous-growth signaling. This places Ste11 near Cdc42-associated Ste20 and pathway-specific surface inputs (michal2011coordinationofmap pages 117-119). A key qualification is that filamentation is strongly strain- and condition-dependent; S288c phenotypes should not automatically be extrapolated to highly filamentous laboratory backgrounds.
Hyperosmotic stress activates Hog1 through two upstream branches. The Sho1 branch employs a membrane-associated Ste20/Ste11/Pbs2 module, whereas the parallel Sln1 branch uses Ssk1 and the MAP3Ks Ssk2/Ssk22. Both converge on Pbs2 and Hog1 (wu1999functionalcharacterizationof pages 1-2).
In the Sho1 branch, Sho1 and Pbs2 operate as organizing elements, while Opy2–Ste50 recruits Ste11 to the membrane. Juxtaposition of Ste11 with Pbs2 favors selective Pbs2 phosphorylation and subsequent Hog1 activation. This organization explains why Ste11 is essential for Sho1 signaling but dispensable for the Sln1 route when that route remains intact (wu1999functionalcharacterizationof pages 12-14, michal2011coordinationofmap pages 117-119, shu2024extrabutnot pages 23-28).
In backgrounds lacking the parallel two-component branch, Ste11 kinase activity becomes essential for hyperosmotic survival, and deletion of STE50 phenocopies deletion of STE11. Constitutively activated Ste11 bypasses this Ste50 requirement, reinforcing the conclusion that Ste50 recruits and unlocks Ste11 rather than replacing its kinase function (wu1999functionalcharacterizationof pages 12-14).
Ste11 is best viewed as a soluble signaling enzyme that is transiently recruited to plasma-membrane/cortical complexes, rather than as a constitutive membrane or organelle protein.
Thus, the location where Ste11 carries out its primary physiological function is the cytoplasmic face of stimulus-specific plasma-membrane signaling complexes, followed by propagation through cytoplasmic kinase cascades. Nuclear accumulation is characteristic of downstream MAPKs such as Hog1, Fus3, and Kss1, not the defining localization of Ste11.
The central conceptual issue is how one MAP3K can serve several pathways without indiscriminately activating all outputs. The current model combines:
Classic experiments showed that loss of HOG1 or PBS2 allowed osmotic stress—tested with 1 M sorbitol—to activate pheromone-pathway outputs. This crosstalk required Sho1, Ste20, Ste50, Ste11, Ste7, Fus3 or Kss1, and Ste12, but not the pheromone Gβ component Ste4 or the Ste5 scaffold. These findings demonstrate that Ste11 is intrinsically capable of transmitting a Sho1-originating signal toward mating machinery when normal Hog1-dependent insulation is lost (o’rourke1998thehog1mapk pages 1-2).
Broader crosstalk extends to cell-wall regulation. Activated Ste11 stimulated FKS2 expression through contributions from HOG, mating, calcineurin/Crz1, and PKC-associated routes and increased Mpk1/Slt2 signaling independently of the canonical mating output. In a ste7Δ pbs2Δ background, activated Ste11-driven FKS2 expression was approximately threefold lower than in relevant single-mutant comparisons, illustrating redundancy and compensatory routing. These results are informative but secondary to Ste11’s canonical MAP3K annotation (wang2011ste11pmekksignals pages 1-3, wang2011ste11pmekksignals pages 13-15).
The most relevant recent study is Zhang et al., published in Molecular Biology of the Cell in October 2024: doi:10.1091/mbc.e24-06-0270. It examined concurrent salt and pheromone inputs through phospho-MAPK measurements, nuclear translocation, reporters, and transcriptomics. Importantly, the study treated Ste11 as shared upstream pathway architecture but did not directly perturb Ste11, so its results refine the operating context of Ste11 rather than its catalytic mechanism (zhang2024sharedandredundant pages 1-2).
Key findings were:
Expert interpretation is that pathway “redundancy” is only partial: the two HOG inputs converge on Hog1 but shape different dynamics and crosstalk. Since the Sho1 branch uses Ste11 whereas the Sln1 branch does not, these findings strengthen the view that Ste11-containing membrane assemblies are a major locus of signal coordination. They do not, however, show a new Ste11 substrate or a changed catalytic reaction.
No directly relevant 2023–2024 study retrieved here superseded the classic biochemical evidence for Ste11 activation, substrate choice, or localization. For those questions, older focused experiments remain more authoritative than newer broad surveys.
Ste11 has no established clinical use and is not itself a validated therapeutic target. Its practical importance is primarily as an experimentally tractable platform for:
These applications rely on the conservation and modularity of the cascade, but results from constitutively active STE11 alleles, other S. cerevisiae backgrounds, or Ste11 homologs in pathogenic fungi cannot be assigned directly to P23561 without species- and strain-specific validation.
Primary annotation: Ste11 is a regulated serine/threonine MAP3K that phosphorylates the MAPKKs Ste7 and Pbs2 after recruitment to plasma-membrane signaling complexes. It transmits pheromone, filamentation, and Sho1-dependent osmotic signals into the Fus3/Kss1 and Hog1 MAPK pathways.
Strong direct evidence: genetic ordering, biochemical activation of Ste7, Ste11–Ste50 binding and regulatory-domain experiments, deletion/constitutive-activation epistasis, and pathway-specific phospho-MAPK and transcriptional readouts (wu1999functionalcharacterizationof pages 1-2, herskowitz1995mapkinasepathways pages 11-11, wu1999functionalcharacterizationof pages 12-14, wu1999functionalcharacterizationof pages 10-10).
Strong pathway-level inference: Opy2/Ste50- and Ste5-dependent cortical recruitment, Pbs2 scaffold routing, and Hog1-mediated insulation (o’rourke1998thehog1mapk pages 1-2, sharmeen2020molecularroleof pages 38-42, michal2011coordinationofmap pages 117-119, shu2024extrabutnot pages 23-28).
Secondary or qualified assignments: Cmk2 and Ptk2 as possible context-dependent targets; Mpk1/Slt2 and FKS2 regulation as crosstalk outputs rather than canonical direct substrate relationships (wang2011ste11pmekksignals pages 1-3, wang2011ste11pmekksignals pages 13-15).
Principal knowledge gaps: quantitative full-length enzyme kinetics, a high-resolution structure of full-length regulated Ste11, stimulus-resolved endogenous Ste11 localization at native abundance, and a definitive proteome-wide catalogue separating direct physiological substrates from indirect pathway effects.
References
(wang2011ste11pmekksignals pages 1-3): Xiaoyan Wang, Mark A Sheff, David M Simpson, and Elaine A Elion. Ste11p mekk signals through hog, mating, calcineurin and pkc pathways to regulate the fks2 gene. BMC Molecular Biology, 12:51-51, Nov 2011. URL: https://doi.org/10.1186/1471-2199-12-51, doi:10.1186/1471-2199-12-51. This article has 17 citations and is from a peer-reviewed journal.
(wu1999functionalcharacterizationof pages 12-14): Cunle Wu, Ekkehard Leberer, David Y. Thomas, and Malcolm Whiteway. Functional characterization of the interaction of ste50p with ste11p mapkkk in saccharomyces cerevisiae. Molecular biology of the cell, 10 7:2425-40, Jul 1999. URL: https://doi.org/10.1091/mbc.10.7.2425, doi:10.1091/mbc.10.7.2425. This article has 114 citations and is from a domain leading peer-reviewed journal.
(wu1999functionalcharacterizationof pages 10-10): Cunle Wu, Ekkehard Leberer, David Y. Thomas, and Malcolm Whiteway. Functional characterization of the interaction of ste50p with ste11p mapkkk in saccharomyces cerevisiae. Molecular biology of the cell, 10 7:2425-40, Jul 1999. URL: https://doi.org/10.1091/mbc.10.7.2425, doi:10.1091/mbc.10.7.2425. This article has 114 citations and is from a domain leading peer-reviewed journal.
(wu1999functionalcharacterizationof pages 1-2): Cunle Wu, Ekkehard Leberer, David Y. Thomas, and Malcolm Whiteway. Functional characterization of the interaction of ste50p with ste11p mapkkk in saccharomyces cerevisiae. Molecular biology of the cell, 10 7:2425-40, Jul 1999. URL: https://doi.org/10.1091/mbc.10.7.2425, doi:10.1091/mbc.10.7.2425. This article has 114 citations and is from a domain leading peer-reviewed journal.
(sharmeen2020molecularroleofa pages 38-42): N Sharmeen. Molecular role of the ste50 adaptor protein in regulating mating-pheromone signaling specificity in «saccharomyces cerevisiae». Unknown journal, 2020.
(michal2011coordinationofmap pages 117-119): Michal Nagiec. Coordination of map kinase signaling during cell fate decisions. Text, 2011. URL: https://doi.org/10.17615/yh1g-7d21, doi:10.17615/yh1g-7d21. This article has 0 citations and is from a peer-reviewed journal.
(herskowitz1995mapkinasepathways pages 11-11): Ira Herskowitz. Map kinase pathways in yeast: for mating and more. Cell, 80:187-197, Jan 1995. URL: https://doi.org/10.1016/0092-8674(95)90402-6, doi:10.1016/0092-8674(95)90402-6. This article has 1386 citations and is from a highest quality peer-reviewed journal.
(wang2011ste11pmekksignals pages 13-15): Xiaoyan Wang, Mark A Sheff, David M Simpson, and Elaine A Elion. Ste11p mekk signals through hog, mating, calcineurin and pkc pathways to regulate the fks2 gene. BMC Molecular Biology, 12:51-51, Nov 2011. URL: https://doi.org/10.1186/1471-2199-12-51, doi:10.1186/1471-2199-12-51. This article has 17 citations and is from a peer-reviewed journal.
(shu2024extrabutnot pages 23-28): Shu Zhang. Extra but not useless: shared and redundant proteins coordinate signal cross-talk between mapk pathways in yeast. Text, 2024. URL: https://doi.org/10.17615/n8vg-ny41, doi:10.17615/n8vg-ny41. This article has 0 citations and is from a peer-reviewed journal.
(sharmeen2020molecularroleof pages 38-42): N Sharmeen. Molecular role of the ste50 adaptor protein in regulating mating-pheromone signaling specificity in «saccharomyces cerevisiae». Unknown journal, 2020.
(sharmeen2020molecularroleofa pages 193-198): N Sharmeen. Molecular role of the ste50 adaptor protein in regulating mating-pheromone signaling specificity in «saccharomyces cerevisiae». Unknown journal, 2020.
(o’rourke1998thehog1mapk pages 1-2): Sean M. O’Rourke and Ira Herskowitz. The hog1 mapk prevents cross talk between the hog and pheromone response mapk pathways in saccharomyces cerevisiae. Genes & development, 12 18:2874-86, Sep 1998. URL: https://doi.org/10.1101/gad.12.18.2874, doi:10.1101/gad.12.18.2874. This article has 505 citations and is from a highest quality peer-reviewed journal.
(zhang2024sharedandredundant pages 1-2): Shu Zhang, Hao Wang, Emily L. Sipko, Shuang Li, Timothy A. Daugird, Wesley R. Legant, and Henrik G. Dohlman. Shared and redundant proteins coordinate signal cross-talk between mapk pathways in yeast. Molecular Biology of the Cell, Oct 2024. URL: https://doi.org/10.1091/mbc.e24-06-0270, doi:10.1091/mbc.e24-06-0270. This article has 6 citations and is from a domain leading peer-reviewed journal.
(shu2024extrabutnot pages 34-37): Shu Zhang. Extra but not useless: shared and redundant proteins coordinate signal cross-talk between mapk pathways in yeast. Text, 2024. URL: https://doi.org/10.17615/n8vg-ny41, doi:10.17615/n8vg-ny41. This article has 0 citations and is from a peer-reviewed journal.
(shu2024extrabutnot pages 37-41): Shu Zhang. Extra but not useless: shared and redundant proteins coordinate signal cross-talk between mapk pathways in yeast. Text, 2024. URL: https://doi.org/10.17615/n8vg-ny41, doi:10.17615/n8vg-ny41. This article has 0 citations and is from a peer-reviewed journal.
(shu2024extrabutnot pages 28-34): Shu Zhang. Extra but not useless: shared and redundant proteins coordinate signal cross-talk between mapk pathways in yeast. Text, 2024. URL: https://doi.org/10.17615/n8vg-ny41, doi:10.17615/n8vg-ny41. This article has 0 citations and is from a peer-reviewed journal.
(shu2024extrabutnot pages 55-58): Shu Zhang. Extra but not useless: shared and redundant proteins coordinate signal cross-talk between mapk pathways in yeast. Text, 2024. URL: https://doi.org/10.17615/n8vg-ny41, doi:10.17615/n8vg-ny41. This article has 0 citations and is from a peer-reviewed journal.