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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 Mih1 from Saccharomyces cerevisiae S288c, encoded by MIH1/YMR036C, not a similarly named protein from another organism. The literature consistently identifies it as the sole budding-yeast homolog of Cdc25, the M-phase-inducing phosphatase. This agrees with the supplied UniProt accession P23748, MPI/Cdc25 phosphatase-family assignment, and rhodanese-like phosphatase domain. No conflicting MIH1 identity was used in this report. (kennedy2016redundantregulationof pages 1-2, keaton2008nucleocytoplasmictraffickingof pages 1-2)
The primary molecular function of Mih1 is to activate Cdc28/Cdk1–mitotic cyclin complexes by removing the inhibitory phosphate from Cdc28 Tyr19. The best-supported reaction is:
Cdc28-pTyr19 + H₂O → Cdc28-Tyr19 + inorganic phosphate.
This assignment is supported not merely by homology or genetics: purified Mih1 directly dephosphorylated Swe1-phosphorylated Cdc28/Cdk1–Clb2 complexes in vitro. Mih1 therefore constitutes the phosphatase arm of a reversible switch in which Swe1 phosphorylates and inhibits Cdc28 at Tyr19, whereas Mih1 removes that phosphate to promote mitotic activity. (sia1996cdc28tyrosinephosphorylation pages 1-2, kennedy2016redundantregulationof pages 1-2, kennedy2016redundantregulationof pages 4-6)
| Annotation dimension | Best-supported conclusion | Evidence type / key quantitative result | Confidence | Key source |
|---|---|---|---|---|
| Identity and family | Verified target: Mih1 is the Saccharomyces cerevisiae MIH1/YMR036C product and sole budding-yeast Cdc25 homolog—an M-phase-inducer, dual-specificity protein phosphatase. Its MPI/Cdc25-family classification agrees with the UniProt-supplied rhodanese-like phosphatase domain and catalytic HCX₅R motif; the fold assignment is inferred rather than based on a Mih1 structure. | Organism-specific literature identifies MIH1 as the budding-yeast CDC25 homolog; sequence/domain annotation supports a rhodanese-like PTPase catalytic fold. | High for identity/family; moderate for inferred structure | Kennedy et al., 2016, DOI (kennedy2016redundantregulationof pages 1-2, david2021exploringtheregulation pages 45-59) |
| Catalytic reaction and substrate specificity | Direct evidence: Mih1 hydrolyzes the inhibitory phosphate from Cdc28/Cdk1 phospho-Tyr19: Cdc28-pY19 + H₂O → Cdc28-Y19 + inorganic phosphate, activating mitotic Cdk1–cyclin complexes. Cdc28/Clb2 is the best-established physiological substrate; a broad Mih1 substrate repertoire has not been demonstrated. | Purified Mih1 directly dephosphorylated Swe1-phosphorylated Cdk1/Clb2 in vitro. It did not dephosphorylate a fortuitous background phosphoprotein in the same assay, supporting substrate selectivity. | Very high | Kennedy et al., 2016, DOI (kennedy2016redundantregulationof pages 4-6) |
| Mitotic role and redundancy | Mih1 promotes mitotic entry and anaphase progression by opposing Swe1-mediated Cdc28-Y19 phosphorylation, but it is nonessential because Ptp1 and a PP2A-Rts1-dependent activity provide redundancy. | Direct genetics/biochemistry: mih1Δ cells are viable, display elevated mitotic Cdc28-pY19, and have mild mitotic-entry and anaphase delays. Mitotic Cdk1 activity in mih1Δ and mih1Δ ptp1Δ was about 65% of wild type, versus 50% during LatA- or GAL-SWE1-induced arrest. mih1Δ ptp1Δ rts1Δ blocked detectable Cdk1-Y19 dephosphorylation and was lethal unless SWE1 was deleted. | Very high | Kennedy et al., 2016, DOI (kennedy2016redundantregulationof pages 1-2, kennedy2016redundantregulationof pages 2-4, kennedy2016redundantregulationof pages 4-6) |
| Morphogenesis checkpoint | Mih1 is the phosphatase arm of the budding-yeast morphogenesis checkpoint. When budding or polarization fails, reduced Mih1 output together with Swe1 activity sustains inhibitory Cdc28-pY19 and delays nuclear division; removing MIH1 strengthens or prolongs this delay. | Direct genetics: in cdc24 cells unable to polarize, deleting SWE1 abolished the mitotic delay, whereas homozygous MIH1 deletion made it effectively permanent; even a twofold gene-dosage change altered timing. Later work found 40% binucleate cdc24-1 alk1Δ cells by 2 h, while additional MIH1 deletion restored normal anaphase kinetics, implicating premature Mih1 activation. | High | Sia et al., 1996, DOI; Galli et al., 2021, DOI (sia1996cdc28tyrosinephosphorylation pages 1-2, sia1996cdc28tyrosinephosphorylation pages 4-5, galli2021haspinmodulatesthe pages 4-6, galli2021haspinmodulatesthe pages 6-7) |
| Cellular localization | Mih1 acts in both cytoplasm and nucleus and undergoes cell-cycle-regulated nucleocytoplasmic shuttling. It is predominantly cytoplasmic through most of the cycle but transiently accumulates in nuclei during late mitosis/telophase. | Direct immunofluorescence: approximately 75% of post-anaphase cells showed nuclear Mih1, whereas nuclear signal was rare in G1. Substitution of Lys31–Lys33 with alanines prevented telophase nuclear accumulation; the cytoplasm-restricted protein remained functional but was less effective, producing larger, elongated cells and delayed nuclear division. | High | Keaton et al., 2008, DOI (keaton2008nucleocytoplasmictraffickingof pages 9-11, keaton2008nucleocytoplasmictraffickingof pages 1-2) |
| Regulation | Mih1 abundance is comparatively constitutive, while activity is regulated chiefly through phosphorylation, localization, and checkpoint context. PP2A-Cdc55/Zds promotes Mih1 dephosphorylation at mitotic entry; casein kinases Yck1/Yck2 and Mck1 contribute to Mih1 phosphorylation. The physiological effects of individual Mih1 phosphosites remain unresolved. | Mixed direct and pathway-level evidence: cdc55Δ causes persistent Mih1 hyperphosphorylation, consistent with Mih1 being a PP2A-Cdc55 substrate; Mih1-myc abundance remained constitutive across the cell cycle. Yck1/Yck2 and Mck1 involvement is supported by phosphorylation-state studies but not a complete site-resolved mechanism. | Moderate–high | Pal et al., 2008, DOI; Keaton et al., 2008, DOI; Yasutis and Kozminski, 2013, DOI (david2021exploringtheregulation pages 75-77, mcqueen2013explorationofthe pages 24-28, keaton2008nucleocytoplasmictraffickingof pages 9-11, yasutis2013cellcyclecheckpoint pages 4-5, yasutis2013cellcyclecheckpoint pages 5-6) |
| 2023–2024 evidence status | No substantive 2023–2024 MIH1-specific mechanistic primary study was found in the targeted search. Current annotation therefore rests on foundational studies, the 2016 direct biochemical analysis, and a 2021 checkpoint extension; a 2023 yeast phosphoproteome resource does not by itself revise Mih1’s established mechanism. | Targeted literature-search result; this is an evidence-gap statement, not proof that no publication exists. | Moderate | Leutert et al., 2023, DOI; latest target-specific mechanistic evidence assessed here: Galli et al., 2021, DOI (galli2021haspinmodulatesthe pages 4-6, galli2021haspinmodulatesthe pages 6-7) |
Table: Compact evidence assessment for S. cerevisiae MIH1/P23748, distinguishing direct experiments from structural or pathway inference. It summarizes identity, catalytic specificity, pathway function, localization, regulation, quantitative findings, and the 2023–2024 evidence gap.
The organism-specific identification is:
Primary yeast literature describes Mih1 as the budding-yeast—and in this context sole—Cdc25 homolog. The target is therefore distinct from Cdc25 proteins in fission yeast, animals, or other fungi, although those proteins provide evolutionary context. (keaton2008nucleocytoplasmictraffickingof pages 1-2, kennedy2016redundantregulationof pages 1-2)
The supplied InterPro/Pfam assignments—MPI phosphatase, rhodanese-like domain, and Rhodanese/PF00581—are coherent with the Cdc25 phosphatase family. A secondary source describes Mih1 as containing a rhodanese-like protein-tyrosine-phosphatase domain with the characteristic HCX₅R catalytic-loop motif. This domain conclusion is sequence/family inference; the evidence retrieved here did not include an experimentally solved Mih1 structure. A crystallographic study of another yeast rhodanese-like protein, Ygr203w, must not be treated as a Mih1 structure. (david2021exploringtheregulation pages 45-59, david2021exploringtheregulation pages 75-77)
The strongest biochemical experiment was reported by Kennedy et al. in Genetics (published online December 29, 2015; print March 2016; DOI: https://doi.org/10.1534/genetics.115.182469). Cdc28/Cdk1–Clb2 complexes were first phosphorylated by Swe1 and then incubated with purified phosphatases. Purified Mih1 removed Cdc28 Tyr19 phosphorylation directly. A fortuitous background phosphoprotein in the same preparation was not dephosphorylated by Mih1, providing evidence that the result was not indiscriminate bulk phosphatase activity. (kennedy2016redundantregulationof pages 1-2, kennedy2016redundantregulationof pages 4-6)
Accordingly, the best-established physiological substrate is Cdc28/Cdk1 phosphorylated at Tyr19, particularly mitotic cyclin complexes such as Cdc28–Clb2. The current evidence does not establish a large, broad Mih1 substrate repertoire. Annotation should therefore remain specific rather than labeling Mih1 as a general cellular tyrosine phosphatase. Its classification as a “dual-specificity phosphatase” reflects Cdc25-family catalytic chemistry and potential residue-class capability; the decisive S. cerevisiae physiological reaction documented here is Tyr19 dephosphorylation. (kennedy2016redundantregulationof pages 1-2, kennedy2016redundantregulationof pages 4-6)
Tyr19 phosphorylation inhibits Cdc28–Clb activity. Removing this phosphate increases mitotic Cdk1 activity and thereby facilitates mitotic entry and progression. In synchronized cells, mih1Δ and mih1Δ ptp1Δ Cdk1 complexes retained approximately 65% of wild-type mitotic kinase activity, whereas latrunculin-A treatment or GAL-driven Swe1 overexpression reduced activity to approximately 50%. Conversely, Cdk1 isolated from mitotic swe1Δ cells had about threefold greater activity than synchronized mitotic wild type, illustrating how strongly the Swe1–Mih1 axis can tune the active Cdk1 pool. (kennedy2016redundantregulationof pages 2-4)
Mih1 and Swe1 form an antagonistic control module:
Unlike fission-yeast Cdc25, Mih1 is not essential under standard budding-yeast growth conditions. mih1Δ cells are viable and display elevated mitotic Cdc28-pTyr19, but only mild delays in mitotic entry and anaphase onset; they eventually dephosphorylate Cdc28 as they enter G1. This led to the discovery of redundant control by Ptp1 and a PP2A-Rts1-dependent activity. (kennedy2016redundantregulationof pages 1-2)
Direct biochemical evidence shows that Ptp1, like Mih1, can dephosphorylate Cdc28-pTyr19. Genetic/in-vivo assays further indicate that PP2A-Rts1 either acts on Cdc28-pTyr19 or controls another unidentified phosphatase. In mih1Δ ptp1Δ rts1Δ cells, detectable Cdc28-Y19 dephosphorylation was blocked; this triple-mutant state was lethal, and lethality was rescued by deleting SWE1. Thus, Mih1 is the canonical Cdc25-like enzyme but participates in a robust, partially redundant network rather than acting alone. (kennedy2016redundantregulationof pages 2-4, kennedy2016redundantregulationof pages 4-6)
Mih1 has a particularly important role when budding or cell polarization is defective. The morphogenesis checkpoint delays nuclear division until bud formation and polarity are adequate. Foundational experiments using temperature-sensitive cdc24 cells showed that the timing of nuclear division was highly sensitive to both SWE1 and MIH1 dosage. Deleting SWE1 abolished the checkpoint delay, whereas loss of MIH1 greatly strengthened it; in diploids, even a twofold gene-dosage difference produced intermediate timing. These findings established the Cdc28-Tyr19 switch as the checkpoint’s central output. (sia1996cdc28tyrosinephosphorylation pages 1-2, sia1996cdc28tyrosinephosphorylation pages 4-5)
This delay is physiologically consequential rather than a dispensable laboratory phenotype. In polarization-defective cells at 37°C, wild-type checkpoint cells began losing viability at approximately 6 h, whereas swe1 and mih1 mutants began doing so at about 4 h and 5 h, respectively. Both premature and excessively delayed mitosis were therefore detrimental. (sia1996cdc28tyrosinephosphorylation pages 4-5)
A 2021 extension implicated the yeast haspin paralogs Alk1 and Alk2 in maintaining this checkpoint. Loss of Alk1 allowed premature nuclear division after polarity disruption: approximately 40% of cdc24-1 alk1Δ cells were binucleate 2 h after release. Additional deletion of MIH1 restored normal anaphase kinetics, supporting the interpretation that checkpoint failure involved inappropriate Mih1 activity. Loss of Alk1 permitted initial Cdc28-Y19 phosphorylation but prevented its sustained accumulation after roughly 1 h. No Alk1–Mih1 physical interaction was detected by two-hybrid analysis, and obvious Mih1 abundance or mobility changes were not observed, so this regulatory connection is likely indirect. Galli et al., January 2021, DOI: https://doi.org/10.3389/fcell.2020.625717. (galli2021haspinmodulatesthe pages 4-6, galli2021haspinmodulatesthe pages 6-7)
Mih1 is a nucleocytoplasmic protein, not a membrane, secreted, or organelle-resident enzyme. Immunofluorescence of a functional Mih1–12Myc fusion showed signal throughout the cell, with predominantly cytoplasmic localization during most of the vegetative cell cycle. Approximately 75% of post-anaphase cells displayed nuclear Mih1, whereas nuclear Mih1 was rare in G1, indicating transient nuclear accumulation around telophase/mitotic exit. Mih1 protein abundance itself remained relatively constant through the cell cycle. Keaton et al., September 2008, DOI: https://doi.org/10.1091/mbc.e08-03-0286. (keaton2008nucleocytoplasmictraffickingof pages 9-11, keaton2008nucleocytoplasmictraffickingof pages 1-2)
A basic sequence near the N terminus functions as a nuclear-import determinant. Changing Lys31–Lys33 to alanines prevented telophase nuclear accumulation. This cytoplasm-restricted variant remained capable of promoting nuclear division, but it was less effective than wild-type Mih1 in sensitized hsl1 cells, producing larger, more elongated cells and delaying nuclear division. Appending an exogenous SV40 nuclear-localization signal rescued these defects. These experiments show that Mih1 can act from either compartment because Cdc28–Clb2 itself shuttles, but the nuclear Mih1 pool is functionally more efficient. (keaton2008nucleocytoplasmictraffickingof pages 9-11, keaton2008nucleocytoplasmictraffickingof pages 1-2)
The appropriate localization annotation is therefore cytoplasm and nucleus, with cell-cycle-regulated shuttling and transient late-mitotic nuclear enrichment. Mih1 likely encounters mobile Cdc28–cyclin complexes in both compartments rather than acting at one fixed structure. (keaton2008nucleocytoplasmictraffickingof pages 9-11)
Mih1 is extensively regulated at the post-translational level. PP2A containing the Cdc55 regulatory subunit promotes Mih1 dephosphorylation as cells approach mitosis: loss of Cdc55 causes persistent Mih1 hyperphosphorylation. Zds1/Zds2 proteins are required for PP2A-Cdc55-dependent Mih1 dephosphorylation. However, an important unresolved point is whether Mih1 hyperphosphorylation changes its intrinsic catalytic rate, substrate access, or localization; authoritative reviews explicitly note that these alternatives were not resolved. Pal, Paraz and Kellogg, March 2008, DOI: https://doi.org/10.1083/jcb.200711014. (david2021exploringtheregulation pages 75-77, yasutis2013cellcyclecheckpoint pages 4-5, yasutis2013cellcyclecheckpoint pages 5-6)
Casein kinases Yck1/Yck2 and the kinase Mck1 have also been implicated in generating the Mih1 phosphorylation pattern under unstressed conditions. The evidence retrieved supports their contribution to Mih1 mobility/phosphorylation state, but it does not provide a complete site-resolved regulatory mechanism. Claims that a particular Mih1 phosphosite directly activates or inhibits catalysis should therefore be treated cautiously. (mcqueen2013explorationofthe pages 24-28)
The broader regulatory architecture links growth and membrane trafficking to mitotic entry. Exocytosis and Rho1/Pkc1/Zds signaling feed into PP2A-Cdc55 and Mih1, coupling successful polarized growth and cell-wall-related processes to Cdc28 activation. Yet PP2A-Cdc55 has complex effects on both Mih1 and Swe1, and some genetic results have supported apparently opposing roles. Expert reviews consequently describe this branch as spatially and mechanistically more complicated than a simple linear activation pathway. (yasutis2013cellcyclecheckpoint pages 4-5, yasutis2013cellcyclecheckpoint pages 5-6)
Available microscopy and immunoblotting indicate that Mih1 abundance is comparatively constitutive. Regulation is therefore dominated by phosphorylation state, access to Cdc28 complexes, subcellular trafficking, and the balance with Swe1 and redundant phosphatases rather than large periodic changes in protein concentration. (keaton2008nucleocytoplasmictraffickingof pages 9-11)
A targeted search of 2023–2024 literature did not identify a substantive new Mih1-specific mechanistic primary study. A 2023 yeast phosphoproteome resource is relevant to the general phosphorylation landscape but did not, in the retrieved evidence, revise the established Mih1 mechanism. Consequently, the most reliable annotation still rests on the foundational morphogenesis-checkpoint study from 1996, localization and phosphoregulation work from 2008, direct biochemical/redundancy analysis from 2016, and the Alk1/Alk2 checkpoint extension from 2021. This is a literature-gap statement rather than proof that no relevant report exists.
The current consensus is therefore stable: Mih1 is the canonical Cdc25-like Cdc28-pTyr19 phosphatase, but its biological output is embedded in a redundant and spatially regulated network. The major conceptual advance after the early checkpoint model was recognition that Mih1 is not the only route to Cdc28-Y19 dephosphorylation. (kennedy2016redundantregulationof pages 1-2, kennedy2016redundantregulationof pages 4-6)
Mih1 is principally a basic-research model, not a clinical or industrially deployed target. Its practical applications are:
The translational relevance is architectural rather than target-specific. Human Cdc25 phosphatases and Wee1 are oncology targets, but Mih1 itself is a yeast protein and there is no evidence in the retrieved literature for a Mih1-directed therapy or commercial bioprocess. Reviews emphasize that conserved pathway organization can be informative even where individual upstream components differ between yeast and vertebrates. (yasutis2013cellcyclecheckpoint pages 1-2, yasutis2013cellcyclecheckpoint pages 5-6)
A defensible concise annotation is:
Mih1 is the nucleocytoplasmic Cdc25-family M-phase-inducer phosphatase of budding yeast. It directly hydrolyzes the inhibitory Tyr19 phosphate on Cdc28/Cdk1–mitotic cyclin complexes, opposing Swe1 to promote mitotic Cdk activity. Mih1 contributes to normal mitotic timing and is a central effector of the morphogenesis checkpoint, particularly when bud formation or polarity is defective. Its activity is controlled by phosphorylation and nucleocytoplasmic trafficking, including PP2A-Cdc55/Zds-dependent dephosphorylation, while Ptp1 and a PP2A-Rts1-dependent mechanism provide functional redundancy.
Confidence is very high for the Cdc28-pTyr19 reaction and Swe1-opposing pathway, high for nucleocytoplasmic localization and morphogenesis-checkpoint function, and moderate for the detailed causal effects of individual Mih1 phosphorylation states.
References
(kennedy2016redundantregulationof pages 1-2): Erin K Kennedy, Michael Dysart, Noel Lianga, Elizabeth C Williams, Sophie Pilon, Carole Doré, Jean-Sebastien Deneault, and Adam D Rudner. Redundant regulation of cdk1 tyrosine dephosphorylation in saccharomyces cerevisiae. Genetics, 202:903-910, Dec 2016. URL: https://doi.org/10.1534/genetics.115.182469, doi:10.1534/genetics.115.182469. This article has 20 citations and is from a domain leading peer-reviewed journal.
(keaton2008nucleocytoplasmictraffickingof pages 1-2): Mignon A. Keaton, Lee Szkotnicki, Aron R. Marquitz, Jake Harrison, Trevin R. Zyla, and Daniel J. Lew. Nucleocytoplasmic trafficking of g2/m regulators in yeast. Molecular biology of the cell, 19 9:4006-18, Sep 2008. URL: https://doi.org/10.1091/mbc.e08-03-0286, doi:10.1091/mbc.e08-03-0286. This article has 43 citations and is from a domain leading peer-reviewed journal.
(sia1996cdc28tyrosinephosphorylation pages 1-2): R. A. Sia, Heather A. Herald, and D. Lew. Cdc28 tyrosine phosphorylation and the morphogenesis checkpoint in budding yeast. Molecular biology of the cell, 7 11:1657-66, Nov 1996. URL: https://doi.org/10.1091/mbc.7.11.1657, doi:10.1091/mbc.7.11.1657. This article has 236 citations and is from a domain leading peer-reviewed journal.
(kennedy2016redundantregulationof pages 4-6): Erin K Kennedy, Michael Dysart, Noel Lianga, Elizabeth C Williams, Sophie Pilon, Carole Doré, Jean-Sebastien Deneault, and Adam D Rudner. Redundant regulation of cdk1 tyrosine dephosphorylation in saccharomyces cerevisiae. Genetics, 202:903-910, Dec 2016. URL: https://doi.org/10.1534/genetics.115.182469, doi:10.1534/genetics.115.182469. This article has 20 citations and is from a domain leading peer-reviewed journal.
(david2021exploringtheregulation pages 45-59): Alain David. Exploring the regulation of mitotic pp2a-rts1 activity in saccharomyces cerevisiae. ArXiv, Jul 2021. URL: https://doi.org/10.20381/ruor-26657, doi:10.20381/ruor-26657. This article has 0 citations.
(kennedy2016redundantregulationof pages 2-4): Erin K Kennedy, Michael Dysart, Noel Lianga, Elizabeth C Williams, Sophie Pilon, Carole Doré, Jean-Sebastien Deneault, and Adam D Rudner. Redundant regulation of cdk1 tyrosine dephosphorylation in saccharomyces cerevisiae. Genetics, 202:903-910, Dec 2016. URL: https://doi.org/10.1534/genetics.115.182469, doi:10.1534/genetics.115.182469. This article has 20 citations and is from a domain leading peer-reviewed journal.
(sia1996cdc28tyrosinephosphorylation pages 4-5): R. A. Sia, Heather A. Herald, and D. Lew. Cdc28 tyrosine phosphorylation and the morphogenesis checkpoint in budding yeast. Molecular biology of the cell, 7 11:1657-66, Nov 1996. URL: https://doi.org/10.1091/mbc.7.11.1657, doi:10.1091/mbc.7.11.1657. This article has 236 citations and is from a domain leading peer-reviewed journal.
(galli2021haspinmodulatesthe pages 4-6): Martina Galli, Laura Diani, Roberto Quadri, Alessandro Nespoli, Elena Galati, Davide Panigada, Paolo Plevani, and Marco Muzi-Falconi. Haspin modulates the g2/m transition delay in response to polarization failures in budding yeast. Frontiers in Cell and Developmental Biology, Jan 2021. URL: https://doi.org/10.3389/fcell.2020.625717, doi:10.3389/fcell.2020.625717. This article has 6 citations.
(galli2021haspinmodulatesthe pages 6-7): Martina Galli, Laura Diani, Roberto Quadri, Alessandro Nespoli, Elena Galati, Davide Panigada, Paolo Plevani, and Marco Muzi-Falconi. Haspin modulates the g2/m transition delay in response to polarization failures in budding yeast. Frontiers in Cell and Developmental Biology, Jan 2021. URL: https://doi.org/10.3389/fcell.2020.625717, doi:10.3389/fcell.2020.625717. This article has 6 citations.
(keaton2008nucleocytoplasmictraffickingof pages 9-11): Mignon A. Keaton, Lee Szkotnicki, Aron R. Marquitz, Jake Harrison, Trevin R. Zyla, and Daniel J. Lew. Nucleocytoplasmic trafficking of g2/m regulators in yeast. Molecular biology of the cell, 19 9:4006-18, Sep 2008. URL: https://doi.org/10.1091/mbc.e08-03-0286, doi:10.1091/mbc.e08-03-0286. This article has 43 citations and is from a domain leading peer-reviewed journal.
(david2021exploringtheregulation pages 75-77): Alain David. Exploring the regulation of mitotic pp2a-rts1 activity in saccharomyces cerevisiae. ArXiv, Jul 2021. URL: https://doi.org/10.20381/ruor-26657, doi:10.20381/ruor-26657. This article has 0 citations.
(mcqueen2013explorationofthe pages 24-28): Jennifer McQueen. Exploration of the budding yeast kinase mck1 in cell cycle regulation. ArXiv, Jan 2013. URL: https://doi.org/10.14288/1.0072986, doi:10.14288/1.0072986. This article has 0 citations.
(yasutis2013cellcyclecheckpoint pages 4-5): Kimberly Yasutis and Keith Kozminski. Cell cycle checkpoint regulators reach a zillion. Cell Cycle, 12:1501-1509, May 2013. URL: https://doi.org/10.4161/cc.24637, doi:10.4161/cc.24637. This article has 83 citations and is from a peer-reviewed journal.
(yasutis2013cellcyclecheckpoint pages 5-6): Kimberly Yasutis and Keith Kozminski. Cell cycle checkpoint regulators reach a zillion. Cell Cycle, 12:1501-1509, May 2013. URL: https://doi.org/10.4161/cc.24637, doi:10.4161/cc.24637. This article has 83 citations and is from a peer-reviewed journal.
(yasutis2013cellcyclecheckpoint pages 1-2): Kimberly Yasutis and Keith Kozminski. Cell cycle checkpoint regulators reach a zillion. Cell Cycle, 12:1501-1509, May 2013. URL: https://doi.org/10.4161/cc.24637, doi:10.4161/cc.24637. This article has 83 citations and is from a peer-reviewed journal.