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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 research target is PHD1 from Saccharomyces cerevisiae (S288c background; systematic locus YKL043W), encoding Phd1, a transcription factor implicated in filamentous differentiation programs (pseudohyphal and invasive growth). Multiple primary studies explicitly name PHD1/Phd1 in S. cerevisiae and characterize it as a filamentation transcription factor that regulates FLO11/MUC1 and other differentiation regulators, matching the UniProt context of a putative transcription factor rather than an enzyme or unrelated “PHD” domain protein. (raithatha2012cdk8regulatesstability pages 1-2, pan2000sok2regulatesyeast pages 1-2)
Saccharomyces cerevisiae can switch from unicellular budding to multicellular, elongated growth forms under nutrient limitation. Two commonly discussed forms are:
- Pseudohyphal growth (classically in diploids), characterized by elongated cells that remain attached and form filaments.
- Invasive growth (classically in haploids), involving agar invasion and adhesion.
Both phenotypes require coordinated control of morphology, polarity, and especially cell-surface adhesion, with FLO11/MUC1 a central effector gene encoding a surface glycoprotein (flocculin). (pan2000sok2regulatesyeast pages 1-2, kumar2021thecomplexgenetic pages 5-7)
Phd1 is a transcription factor positioned as a high-level regulator (“master regulator”) of filamentous differentiation gene expression programs, rather than a catalytic enzyme or transporter. Its biological role is therefore best defined by the transcriptional programs it activates/represses and by how its activity is controlled by upstream signaling and protein stability. (raithatha2012cdk8regulatesstability pages 1-2)
A central experimentally supported role for Phd1 is regulation of cell–cell/cell–surface adhesion and filamentation through FLO11:
- In a transcription-factor cascade context, Pan & Heitman (2000) report that Phd1 and Ash1 regulate expression of the cell surface protein Flo11, and that both factors are largely required for filamentation in a sok2 hyperfilamentous background. (Publication date: 2000-11; URL: https://doi.org/10.1128/MCB.20.22.8364-8372.2000) (pan2000sok2regulatesyeast pages 1-2)
- A later authoritative synthesis (Annual Review of Genetics) places Phd1 in a Sok2→Phd1/Ash1/Swi5 transcription-factor cascade capable of regulating FLO11 “independently of the PKA and MAPK pathways,” framing Phd1 as part of a layered regulatory architecture converging on FLO11. (Publication date: 2021-11; URL: https://doi.org/10.1146/annurev-genet-071719-020249) (kumar2021thecomplexgenetic pages 5-7)
Multiple lines of genetic evidence support Phd1 as a potent differentiation regulator:
- Overexpression of PHD1 strongly promotes pseudohyphal growth even on nitrogen-rich medium; in Pan & Heitman (2000), PHD1 overexpression can suppress pseudohyphal defects of tpk2 and ste12 mutants, indicating Phd1 can drive downstream differentiation programs even when canonical upstream regulators are compromised. (pan2000sok2regulatesyeast pages 1-2)
- Conversely, phd1/phd1 mutants did not show obvious pseudohyphal defects under the conditions emphasized in that study, suggesting background/condition dependence and redundancy among differentiation regulators. (pan2000sok2regulatesyeast pages 1-2)
- Raithatha et al. (2012) also describe Phd1 as a “master regulator” of filamentation and report that PHD1 expression is induced under nitrogen starvation and Phd1 accumulates under differentiating conditions, consistent with a role in initiating/maintaining the program. (Publication date: 2012-02; URL: https://doi.org/10.1128/MCB.05420-11) (raithatha2012cdk8regulatesstability pages 1-2)
Phd1 sits within a broader network in which nutrient sensing feeds into transcriptional regulators controlling FLO11 and morphology:
- The broader differentiation system is described as being regulated by MAPK (Kss1), Ras–cAMP–PKA, and Snf1/AMPK signaling; this context is explicitly discussed alongside PHD1 regulation in Raithatha et al. (2012). (raithatha2012cdk8regulatesstability pages 1-2)
- Pan & Heitman (2000) place Phd1 in relation to the cAMP/PKA and MAPK systems and suggest Phd1 may act distinct from those pathways in some contexts, consistent with multiple partially independent inputs to FLO11 regulation. (pan2000sok2regulatesyeast pages 1-2)
- Kumar (2021) highlights that Sok2 is thought to act downstream of cAMP/PKA but can activate a TF cascade (including Phd1) that regulates FLO11 “independently” of direct PKA/MAPK control, emphasizing network modularity and redundancy. (kumar2021thecomplexgenetic pages 5-7)
A major mechanistic advance in understanding Phd1 is that its activity is controlled not only transcriptionally but also by protein stability:
- Raithatha et al. (2012) provide experimental evidence that Phd1 is intrinsically unstable and that its degradation is initiated via Cdk8-dependent phosphorylation (Cdk8 is a kinase associated with the RNA polymerase II Mediator complex). (raithatha2012cdk8regulatesstability pages 1-2)
- Quantitative stability measurements by cycloheximide-chase show a short half-life (~10–15 min) in rich medium, and strong stabilization in conditions where Cdk8 activity is absent or reduced. (raithatha2012cdk8regulatesstability pages 6-7)
- Under nitrogen limitation, Phd1 becomes progressively stabilized: half-life increases to ~40 min after 2 h in nitrogen-limiting SLAD and to >45 min after 4 h, consistent with a differentiation-triggered stabilization mechanism. (raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability media d01b8851)
- In cdk8Δ, Phd1 is strongly stabilized (>45 min), consistent with Cdk8 acting as a negative regulator through turnover. (raithatha2012cdk8regulatesstability pages 2-3)
- A notable genetics–biochemistry bridge is a natural polymorphism in a differentiating strain background (1278b) that removes a candidate Cdk8 phosphosite (S92F), stabilizing Phd1 and enhancing filamentation, supporting causality between phosphorylation site, stability, and phenotype. (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 6-7)
Visual evidence: cycloheximide-chase panels and the regulatory model were retrieved from Raithatha et al. (2012), including stability curves and a pathway model summarizing how nutrient limitation reduces Cdk8 activity to permit accumulation of Phd1 and other transcription factors. (raithatha2012cdk8regulatesstability media d01b8851, raithatha2012cdk8regulatesstability media c487618b)
Direct experimental localization evidence (e.g., GFP microscopy or cell fractionation explicitly stating nuclear localization) was not found in the retrieved excerpts. However:
- Raithatha et al. (2012) used FLAG-tagged Phd1 for biochemical detection and treat Phd1 as a DNA-binding transcriptional regulator; nuclear function is therefore strongly implied but not directly demonstrated in the retrieved text segments. (raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 3-4)
Accordingly, the most defensible annotation from the retrieved evidence is:
- Cellular compartment (evidence level): nuclear localization is inferred from transcription factor function and Mediator/Cdk8 context, but direct localization assays were not available in the gathered evidence. (raithatha2012cdk8regulatesstability pages 1-2)
Direct 2023–2024 mechanistic papers specifically dissecting Phd1 regulation were not retrieved by the search tools. However, one 2024 primary study provides contemporary functional context:
Cromie et al. (2024) examined gene-expression programs underlying “ruffled/structured” colony morphology and performed deletion tests in a structured-colony background (F13). They report:
- PHD1 (YKL043W) is in a gene-expression cluster whose expression correlates positively with colony structure.
- Yet, phd1Δ had little effect on colony morphology at day 5 (colonies still displayed an outer structured zone and inner smooth zone), whereas flo11Δ or msb2Δ produced fully smooth colonies. (Publication date: 2024-09; URL: https://doi.org/10.1371/journal.pone.0311061) (cromie2024spatiotemporalpatternsof pages 21-23)
Interpretation: This supports the view that PHD1 participates in a broader colony-structure/filamentation-associated transcriptional state, but may be nonessential or redundant in at least some genetic backgrounds and environmental regimes—consistent with older observations that loss of PHD1 alone can show modest phenotypes while overexpression is strongly pro-filamentation. (pan2000sok2regulatesyeast pages 1-2, cromie2024spatiotemporalpatternsof pages 21-23)
A clear real-world implementation of PHD1 knowledge is in synthetic gene regulation:
- Pothoulakis & Ellis (2018) engineered synthetic regulatory systems to control expression of native PHD1 and FLO8, demonstrating that externally controlled induction of these transcription factors can trigger pseudohyphal growth in both diploid and haploid strains, including in rich media. This establishes PHD1 as an actionable “handle” to program multicellular morphology in yeast. (Publication date: 2018-01; URL: https://doi.org/10.1038/s42003-017-0008-0) (pothoulakis2018syntheticgeneregulation pages 1-2)
Application relevance: controllable filamentation can be used as a chassis capability for engineered surface adhesion, structured multicellular assemblies, and programmable colony architectures, leveraging natural differentiation modules. (pothoulakis2018syntheticgeneregulation pages 1-2)
The following table consolidates the supported claims, evidence types, and quantitative data extracted from the retrieved corpus.
| Claim/annotation | Evidence type | Key experimental details (strain/condition/assay) | Quantitative/statistical data | Primary source (authors year journal) | DOI URL |
|---|---|---|---|---|---|
| Phd1 is a transcription factor and a master regulator of filamentous differentiation in S. cerevisiae | Genetics; regulatory analysis | Primary study summarized Phd1 as regulating expression of most other differentiation TFs; overproduction induced filamentation; evidence integrated with nitrogen-starvation differentiation assays (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 2-2) | Overexpression sufficient to induce filamentation; no exact fold reported in gathered evidence (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 2-2) | Raithatha et al. 2012, Molecular and Cellular Biology (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 2-2) | https://doi.org/10.1128/MCB.05420-11 |
| Primary molecular function is transcriptional regulation of pseudohyphal/invasive growth programs rather than enzymatic catalysis | Genetics; phenotype suppression | Overexpression of PHD1 strongly promoted pseudohyphal growth even on nitrogen-rich medium and could suppress pseudohyphal defects of tpk2 and ste12 mutants (pan2000sok2regulatesyeast pages 1-2) | Strong pseudohyphal growth on rich medium upon overexpression; phd1/phd1 mutants alone showed no obvious pseudohyphal defect in that assay (pan2000sok2regulatesyeast pages 1-2) | Pan & Heitman 2000, Molecular and Cellular Biology (pan2000sok2regulatesyeast pages 1-2) | https://doi.org/10.1128/MCB.20.22.8364-8372.2000 |
| Phd1 positively regulates FLO11/MUC1, a key cell-surface flocculin required for filamentation/invasion | Genetics; transcriptional cascade | Genome-array/Northern analyses in sok2/sok2 hyperfilamentous mutants placed PHD1 in a cascade with Ash1 controlling FLO11 expression and cell-cell adhesion (pan2000sok2regulatesyeast pages 1-2); review synthesis places Phd1 in Sok2→Phd1/Ash1/Swi5→FLO11 regulation (kumar2021thecomplexgenetic pages 5-7) | In sok2 background, Phd1 and Ash1 were largely required for filamentation; exact expression fold not given in gathered excerpts (pan2000sok2regulatesyeast pages 1-2, kumar2021thecomplexgenetic pages 5-7) | Pan & Heitman 2000, MCB; Kumar 2021, Annual Review of Genetics (pan2000sok2regulatesyeast pages 1-2, kumar2021thecomplexgenetic pages 5-7) | https://doi.org/10.1128/MCB.20.22.8364-8372.2000; https://doi.org/10.1146/annurev-genet-071719-020249 |
| Phd1 functions in pseudohyphal growth and haploid invasive growth pathways | Genetics; phenotypic analysis | Ste12 and PHD1 were required for haploid invasive growth; PHD1 induction/stabilization tracked with nitrogen starvation, a canonical pseudohyphal trigger (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 1-2) | Nitrogen starvation increased PHD1 mRNA and stabilized protein; invasive-growth requirement shown genetically but without exact percentages in gathered text (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 1-2) | Raithatha et al. 2012, MCB (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 1-2) | https://doi.org/10.1128/MCB.05420-11 |
| Upstream pathway context includes Ras2/cAMP-PKA, MAPK/Kss1, and Snf1; Phd1 acts within or alongside this network | Review synthesis; genetics | Filamentous differentiation broadly regulated by MAPK (Kss1), Ras-cAMP-PKA, and Snf1-AMPK; Sok2 is thought to act downstream of cAMP/PKA, while the Sok2→Phd1/Ash1/Swi5 cascade can regulate FLO11 independently of direct PKA/MAPK control (raithatha2012cdk8regulatesstability pages 1-2, pan2000sok2regulatesyeast pages 1-2, kumar2021thecomplexgenetic pages 5-7) | Pathway placement is qualitative in gathered evidence; no direct kinetic constants reported (raithatha2012cdk8regulatesstability pages 1-2, pan2000sok2regulatesyeast pages 1-2, kumar2021thecomplexgenetic pages 5-7) | Raithatha et al. 2012, MCB; Pan & Heitman 2000, MCB; Kumar 2021, Annu Rev Genet (raithatha2012cdk8regulatesstability pages 1-2, pan2000sok2regulatesyeast pages 1-2, kumar2021thecomplexgenetic pages 5-7) | https://doi.org/10.1128/MCB.05420-11; https://doi.org/10.1128/MCB.20.22.8364-8372.2000; https://doi.org/10.1146/annurev-genet-071719-020249 |
| PHD1 is directly repressed by Sok2 in rich medium | Genetics; transcriptional regulation | In rich medium, Sok2 acted as a negative regulator of filamentation and directly/indirectly repressed the transcription-factor cascade including PHD1; PHD1 was induced in sok2/sok2 hyperfilamentous mutants (raithatha2012cdk8regulatesstability pages 8-9, pan2000sok2regulatesyeast pages 1-2) | PHD1 induction observed in sok2/sok2 mutants; exact fold change not given in gathered excerpts (raithatha2012cdk8regulatesstability pages 8-9, pan2000sok2regulatesyeast pages 1-2) | Pan & Heitman 2000, MCB; Raithatha et al. 2012, MCB (raithatha2012cdk8regulatesstability pages 8-9, pan2000sok2regulatesyeast pages 1-2) | https://doi.org/10.1128/MCB.20.22.8364-8372.2000; https://doi.org/10.1128/MCB.05420-11 |
| PHD1 expression is partially dependent on Ste12, and Ste12 binds the PHD1 promoter in vitro | Promoter binding; genetics | DNase I footprinting/promoter analysis showed Ste12 binds sites on the PHD1 promoter in vitro; in vivo promoter occupancy also implicated Tec1, Flo8, Sok2, and Phd1 itself (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 2-3) | Qualitative promoter-binding evidence; no occupancy percentages in gathered excerpts (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 2-3) | Raithatha et al. 2012, MCB (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 2-3) | https://doi.org/10.1128/MCB.05420-11 |
| Phd1 positively autoregulates its own expression under nitrogen limitation | Promoter binding; regulatory model | Promoter occupancy and regulatory model indicate Phd1 can bind/activate its own promoter, forming a positive-feedback loop during differentiation (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 6-7) | Positive feedback described qualitatively; no exact fold increase reported in gathered excerpts (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 6-7) | Raithatha et al. 2012, MCB (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 6-7) | https://doi.org/10.1128/MCB.05420-11 |
| Cdk8 negatively regulates Phd1 by phosphorylation-dependent destabilization | Protein stability assay; in vitro kinase/phosphopeptide analysis | Cycloheximide-chase, 32Pi metabolic labeling, immunoprecipitation, in vitro kinase assays, and phosphopeptide analysis showed Cdk8-dependent phosphorylation promotes Phd1 degradation (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 2-2, raithatha2012cdk8regulatesstability pages 2-3) | Phd1 half-life was reported as ~10–15 min in wild type/rich medium and >45 min in cdk8Δ cells (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 2-3) | Raithatha et al. 2012, MCB (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 2-3) | https://doi.org/10.1128/MCB.05420-11 |
| Natural polymorphism at the Cdk8 phosphosite stabilizes Phd1 and enhances filamentation | Protein stability assay; allele comparison | Comparison of PHD1 alleles (S92 versus S92F) showed that the 1278b strain carries S92F, removing a Cdk8 phosphorylation site and stabilizing Phd1 (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 2-2) | Wild-type S92 Phd1 half-life ~15 min in rich medium; stabilized variant and/or cdk8Δ backgrounds showed >45 min stability (raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 2-2) | Raithatha et al. 2012, MCB (raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability pages 2-2) | https://doi.org/10.1128/MCB.05420-11 |
| Nitrogen starvation stabilizes Phd1 protein and increases PHD1 transcript, promoting differentiation | Protein stability assay; transcript analysis | Cells shifted to SLAD/nitrogen-limiting medium showed increased PHD1 mRNA and marked stabilization of Phd1 protein; model proposes loss of Cdk8 activity under these conditions (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability media d01b8851) | Half-life increased from ~15 min in SD to ~40 min after 2 h in SLAD and >45 min after 4 h in SLAD (raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability media d01b8851) | Raithatha et al. 2012, MCB (raithatha2012cdk8regulatesstability pages 8-9, raithatha2012cdk8regulatesstability pages 1-2, raithatha2012cdk8regulatesstability pages 6-7, raithatha2012cdk8regulatesstability media d01b8851) | https://doi.org/10.1128/MCB.05420-11 |
| Forced expression of PHD1 is sufficient to induce pseudohyphal growth synthetically, even in rich media and in haploids | Synthetic induction | Synthetic gene-regulation circuits controlling native PHD1 and FLO8 expression triggered pseudohyphal growth in diploid and haploid cells in rich media; used as an engineered, externally inducible differentiation system (pothoulakis2018syntheticgeneregulation pages 1-2) | Phenotype induction in both diploid and haploid strains under non-starvation conditions; exact percentages not given in gathered excerpt (pothoulakis2018syntheticgeneregulation pages 1-2) | Pothoulakis & Ellis 2018, Communications Biology (pothoulakis2018syntheticgeneregulation pages 1-2) | https://doi.org/10.1038/s42003-017-0008-0 |
| Recent 2024 colony-morphology data support association of PHD1 expression with structured colony regions, but deletion may be background-dependent and nonessential in F13 | RNA-seq/cluster; deletion phenotype | In structured-colony strain F13, PHD1/YKL043W clustered with genes whose expression correlated positively with colony structure (cluster I9); however, phd1Δ retained central smooth plus outer structured zones at day 5, unlike flo11Δ or msb2Δ (cromie2024spatiotemporalpatternsof pages 21-23) | phd1Δ had little effect on F13 morphology, whereas flo11Δ and msb2Δ remained fully smooth at day 5 (cromie2024spatiotemporalpatternsof pages 21-23) | Cromie et al. 2024, PLOS ONE (cromie2024spatiotemporalpatternsof pages 21-23) | https://doi.org/10.1371/journal.pone.0311061 |
| Subcellular localization is expected to be nuclear for a transcription factor, but no direct Phd1 localization evidence was identified in the gathered sources | Evidence gap / inference | Gathered primary and review sources discuss Phd1 as a transcription factor regulating promoters and differentiation programs, but none of the retrieved evidence IDs reported direct GFP/immunolocalization for Phd1 (raithatha2012cdk8regulatesstability pages 8-9, pan2000sok2regulatesyeast pages 1-2) | No direct localization measurement available in gathered evidence (raithatha2012cdk8regulatesstability pages 8-9, pan2000sok2regulatesyeast pages 1-2) | Evidence gap within retrieved literature (raithatha2012cdk8regulatesstability pages 8-9, pan2000sok2regulatesyeast pages 1-2) | N/A |
Table: This table summarizes experimentally supported functional annotations for Saccharomyces cerevisiae PHD1/Phd1 using only the gathered evidence contexts. It highlights molecular function, pathway placement, regulatory inputs, phenotypes, and the current evidence gap for direct localization data.
References
(raithatha2012cdk8regulatesstability pages 1-2): Sheetal Raithatha, Ting-Cheng Su, Pedro Lourenco, Susan Goto, and Ivan Sadowski. Cdk8 regulates stability of the transcription factor phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Molecular and Cellular Biology, 32:664-674, Feb 2012. URL: https://doi.org/10.1128/mcb.05420-11, doi:10.1128/mcb.05420-11. This article has 59 citations and is from a domain leading peer-reviewed journal.
(pan2000sok2regulatesyeast pages 1-2): Xuewen Pan and Joseph Heitman. Sok2 regulates yeast pseudohyphal differentiation via a transcription factor cascade that regulates cell-cell adhesion. Molecular and Cellular Biology, 20:8364-8372, Nov 2000. URL: https://doi.org/10.1128/mcb.20.22.8364-8372.2000, doi:10.1128/mcb.20.22.8364-8372.2000. This article has 164 citations and is from a domain leading peer-reviewed journal.
(kumar2021thecomplexgenetic pages 5-7): Anuj Kumar. The complex genetic basis and multilayered regulatory control of yeast pseudohyphal growth. Nov 2021. URL: https://doi.org/10.1146/annurev-genet-071719-020249, doi:10.1146/annurev-genet-071719-020249. This article has 41 citations and is from a domain leading peer-reviewed journal.
(raithatha2012cdk8regulatesstability pages 6-7): Sheetal Raithatha, Ting-Cheng Su, Pedro Lourenco, Susan Goto, and Ivan Sadowski. Cdk8 regulates stability of the transcription factor phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Molecular and Cellular Biology, 32:664-674, Feb 2012. URL: https://doi.org/10.1128/mcb.05420-11, doi:10.1128/mcb.05420-11. This article has 59 citations and is from a domain leading peer-reviewed journal.
(raithatha2012cdk8regulatesstability media d01b8851): Sheetal Raithatha, Ting-Cheng Su, Pedro Lourenco, Susan Goto, and Ivan Sadowski. Cdk8 regulates stability of the transcription factor phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Molecular and Cellular Biology, 32:664-674, Feb 2012. URL: https://doi.org/10.1128/mcb.05420-11, doi:10.1128/mcb.05420-11. This article has 59 citations and is from a domain leading peer-reviewed journal.
(raithatha2012cdk8regulatesstability pages 2-3): Sheetal Raithatha, Ting-Cheng Su, Pedro Lourenco, Susan Goto, and Ivan Sadowski. Cdk8 regulates stability of the transcription factor phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Molecular and Cellular Biology, 32:664-674, Feb 2012. URL: https://doi.org/10.1128/mcb.05420-11, doi:10.1128/mcb.05420-11. This article has 59 citations and is from a domain leading peer-reviewed journal.
(raithatha2012cdk8regulatesstability media c487618b): Sheetal Raithatha, Ting-Cheng Su, Pedro Lourenco, Susan Goto, and Ivan Sadowski. Cdk8 regulates stability of the transcription factor phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Molecular and Cellular Biology, 32:664-674, Feb 2012. URL: https://doi.org/10.1128/mcb.05420-11, doi:10.1128/mcb.05420-11. This article has 59 citations and is from a domain leading peer-reviewed journal.
(raithatha2012cdk8regulatesstability pages 3-4): Sheetal Raithatha, Ting-Cheng Su, Pedro Lourenco, Susan Goto, and Ivan Sadowski. Cdk8 regulates stability of the transcription factor phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Molecular and Cellular Biology, 32:664-674, Feb 2012. URL: https://doi.org/10.1128/mcb.05420-11, doi:10.1128/mcb.05420-11. This article has 59 citations and is from a domain leading peer-reviewed journal.
(cromie2024spatiotemporalpatternsof pages 21-23): Gareth A. Cromie, Zhihao Tan, Michelle Hays, Amy Sirr, and Aimée M. Dudley. Spatiotemporal patterns of gene expression during development of a complex colony morphology. PLOS ONE, Sep 2024. URL: https://doi.org/10.1371/journal.pone.0311061, doi:10.1371/journal.pone.0311061. This article has 3 citations and is from a peer-reviewed journal.
(pothoulakis2018syntheticgeneregulation pages 1-2): Georgios Pothoulakis and Tom Ellis. Synthetic gene regulation for independent external induction of the saccharomyces cerevisiae pseudohyphal growth phenotype. Communications Biology, Jan 2018. URL: https://doi.org/10.1038/s42003-017-0008-0, doi:10.1038/s42003-017-0008-0. This article has 19 citations and is from a peer-reviewed journal.
(raithatha2012cdk8regulatesstability pages 8-9): Sheetal Raithatha, Ting-Cheng Su, Pedro Lourenco, Susan Goto, and Ivan Sadowski. Cdk8 regulates stability of the transcription factor phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Molecular and Cellular Biology, 32:664-674, Feb 2012. URL: https://doi.org/10.1128/mcb.05420-11, doi:10.1128/mcb.05420-11. This article has 59 citations and is from a domain leading peer-reviewed journal.
(raithatha2012cdk8regulatesstability pages 2-2): Sheetal Raithatha, Ting-Cheng Su, Pedro Lourenco, Susan Goto, and Ivan Sadowski. Cdk8 regulates stability of the transcription factor phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Molecular and Cellular Biology, 32:664-674, Feb 2012. URL: https://doi.org/10.1128/mcb.05420-11, doi:10.1128/mcb.05420-11. This article has 59 citations and is from a domain leading peer-reviewed journal.