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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 protein is correctly identified as Sid2, encoded by sid2 (systematic ORF SPAC24B11.11c) in Schizosaccharomyces pombe strain 972. The supplied UniProt accession Q09898, serine/threonine-protein-kinase annotation (EC 2.7.11.1), and protein-kinase/AGC-family domains agree with the literature: Sid2 is an essential NDR/LATS-family AGC serine/threonine kinase, functions with the coactivator Mob1, and is the terminal kinase of the fission-yeast septation initiation network (SIN). The retrieved primary literature independently confirms the organism, symbol, kinase class, Mob1 relationship, and SIN function, although accession Q09898 and ORF SPAC24B11.11c were not printed in the retrieved article excerpts and therefore remain accession-level identifiers supplied by UniProt rather than independently re-established here. No similarly named protein from another organism was substituted. (feoktistova2012thefissionyeast pages 1-2, ozdemir2022metabolicregulationofa pages 29-31, willet2019ndrkinasesid2 pages 1-3)
Sid2 converts a mitotic signal assembled at spindle-pole bodies (SPBs) into spatially organized phosphorylation at the SPBs and medial contractile ring. Its principal biological output is timely actomyosin-ring maintenance and constriction, septum formation, and resetting of division-site machinery after cytokinesis. It also feeds back on the SIN scaffold Cdc11 to stabilize maximal, asymmetric anaphase signaling. (feoktistova2012thefissionyeast pages 1-2, willet2019ndrkinasesid2 pages 1-3)
Sid2 is a protein kinase rather than a transporter or structural protein. Its generic reaction is:
ATP + protein serine/threonine → ADP + phosphoprotein serine/threonine.
Its kinase-like, protein-kinase ATP-binding, catalytic protein-kinase, protein-kinase C-terminal, and AGC-kinase C-terminal domains are fully consistent with an NDR/LATS-family AGC kinase. NDR/LATS kinases use a conserved N-terminal regulatory region to bind a Mob-family cofactor; structural work on this kinase class supports a model in which Mob organizes the regulatory region and hydrophobic-motif activation segment to stimulate the kinase domain. In S. pombe, Sid2 partners specifically with Mob1, and Mob1 is required for normal Sid2 localization. (ozdemir2022metabolicregulationofa pages 29-31)
The experimentally used minimal Sid2 substrate consensus is RXXS, with serine as the best-established phosphoacceptor; the broader NDR/LATS family can also recognize related RXXS/T sequences. This motif is informative but not sufficient by itself to establish a physiological substrate—localization, cell-cycle timing, docking, biochemical phosphorylation, and phosphosite-mutant phenotypes provide the stronger evidence. (feoktistova2012thefissionyeast pages 1-2, feoktistova2012thefissionyeast pages 3-4, willet2019ndrkinasesid2 pages 1-3)
The SIN is a GTPase-regulated kinase cascade assembled on the Cdc11–Sid4 scaffold at SPBs. The conventional sequence is Spg1-GTP → Cdc7 → Sid1–Cdc14 → Sid2–Mob1, followed by Sid2 action at SPBs and the division site. Genetic epistasis, localization, and kinase-activity experiments strongly support this ordering, although authoritative syntheses caution that every activation step has not been reconstructed biochemically; the pathway should therefore not be interpreted as a completely proven chain of direct kinase-to-kinase reactions. (ozdemir2022metabolicregulationofa pages 29-31, feoktistova2012thefissionyeast pages 1-2)
Sid2 is not merely a terminal passive output. It phosphorylates Cdc11 and thereby creates positive feedback that promotes Cdc7 association with SPBs, maximal SIN activity during anaphase, and appropriate asymmetric signaling between the two SPBs. Counteracting phosphatase activity is thought to help remove Cdc11 phosphorylation at the old SPB. This feedback architecture explains how a scaffolded kinase cascade can become both strongly activated and spatially asymmetric. (feoktistova2012thefissionyeast pages 1-2, feoktistova2012thefissionyeast pages 6-7)
Sid2 is an intracellular, dynamically localized kinase. It first associates with SPBs, where it participates in scaffolded SIN signaling. Its SPB localization is reported to be independent of Spg1, distinguishing physical recruitment from complete catalytic activation. Sid2–Mob1 subsequently appears at the medial contractile actomyosin ring/division site; this medial localization depends on upstream SIN components and coincides with the transition to ring constriction and septation. (feoktistova2012thefissionyeast pages 1-2)
At the division site, Sid2 is positioned to phosphorylate ring-associated and cortical substrates. Live imaging measured Sid2-GFP residence there for 28.75 ± 1.1 min in wild type. Residence fell to 22.75 ± 0.6 min in the nonphosphorylatable cdc11-S5A background and was 30.50 ± 0.9 min in phosphomimetic cdc11-S5D, linking SPB feedback to the duration of division-site signaling. Sid2 arrives as the anillin-like protein Mid1 is removed from the division-site cortex, consistent with Sid2 directly driving that transition. (feoktistova2012thefissionyeast pages 3-4, willet2019ndrkinasesid2 pages 1-3)
Cdc11 is among the best-supported direct substrates. Immunopurified Sid2–Mob1 phosphorylated Cdc11 fragments in vitro, and mass spectrometry identified five major functional target residues: S121, S122, S264, S345, and S418. Alanine substitution markedly reduced phosphorylation. The cdc11-S5A allele accelerated Cdc7 asymmetry, shortened Cdc7 retention at the old SPB, impaired cytokinesis, and interacted adversely with conditional cdc7 alleles; phosphomimetic cdc11-S5D did not show the same growth defect. (feoktistova2012thefissionyeast pages 1-2, feoktistova2012thefissionyeast pages 3-4)
From SPB separation/ring formation to Cdc15-GFP disappearance, cytokinesis required 48 min in wild type, 57 min in cdc11-S5A, and 50 min in cdc11-S5D. These measurements support a causal model in which Sid2 phosphorylation of Cdc11 prolongs productive SIN signaling rather than simply marking an active pathway. Reported comparisons used approximately 10–27 cells and included significance values of p=0.0007, 0.0002, and 0.0137 for measured localization/timing differences. (feoktistova2012thefissionyeast pages 3-4, feoktistova2012thefissionyeast pages 6-7)
Mid1 is another high-confidence direct substrate. Mid1 contains nine experimentally studied Sid2-consensus serines: S110, S127, S218, S227, S329, S432, S452, S464, and S531. Seven were detected by mass spectrometry in purified Mid1, an eighth had appeared in another phosphoproteomic screen, and immunopurified Sid2 phosphorylated a wild-type Mid1 fragment in vitro but not the corresponding nine-alanine mutant. (willet2019ndrkinasesid2 pages 1-3, willet2019ndrkinasesid2 pages 6-8)
Sid2 phosphorylation removes Mid1 from the cortex as constriction begins and weakens its association with the cortical-node kinase Cdr2. Nonphosphorylatable Mid1-9A remained cortical, accumulated in interphase nodes, recruited ring components prematurely, advanced G2/M, and delayed ring maturation and constriction. Cdr2 co-immunoprecipitated about twofold more Mid1-9A than wild-type Mid1; similarly, SIN-inactive sid2-250 cells showed about a twofold increase in Mid1–Cdr2 association. Cdr2 was recruited to approximately 75% of Mid1-9A contractile rings, versus only approximately 18% weak Cdr2/Rlc1 colocalization in wild type. In sensitized node-defective backgrounds, Mid1-9A produced tilted or off-center rings, demonstrating that Sid2 helps erase the preceding division-site state and preserve medial placement in the next cycle. (willet2019ndrkinasesid2 pages 5-6)
Cdc12 is a literature-supported direct ring substrate. Sid2-dependent phosphorylation inhibits inappropriate Cdc12 multimerization and the associated F-actin-bundling state. When Sid2-target sites cannot be phosphorylated, Cdc12 persists in clusters and cytokinetic rings become prone to collapse when division is delayed. Thus, Sid2 does not simply activate ring contraction; it restrains a potentially harmful oligomeric state of the formin to maintain ring architecture. The retrieved evidence supports this relationship but did not provide the primary study’s complete site-level quantitative dataset, so confidence is high for the mechanism but lower for unquoted residue-specific details. (sinha2023ageneticstudy pages 24-29)
Clp1 is reported as a Sid2 substrate whose phosphorylation promotes cytoplasmic retention, linking SIN activation to persistence of a late-mitotic phosphatase outside the nucleus. This helps coordinate mitotic exit and cytokinesis. A useful distinction is that Clp1 directly dephosphorylates Cdk1-dependent sites on Cdc11; the retrieved later study did not indicate that Clp1 removes the Cdc11 Sid2 sites. In that study, cytokinesis failure occurred in 3% of clp1-null, 18% of csc1-null, and 35% of double-null cells at 36 °C, illustrating cooperation between phosphatase systems rather than a simple Sid2–Clp1 reversal pair. (feoktistova2012thefissionyeast pages 1-2, chen2013comprehensiveproteomicsanalysis pages 7-8, chen2013comprehensiveproteomicsanalysis pages 13-13)
Cdr2 has functional phosphosite evidence: combining cdr2-2A and mid1-9A caused off-center septa although either single mutant did not, supporting cooperative Sid2-dependent resetting of node machinery. Klp2 is also named as a Sid2 substrate linked to spindle regulation, but the retrieved excerpts lacked equivalent biochemical details. (willet2019ndrkinasesid2 pages 6-8, willet2019ndrkinasesid2 pages 5-6)
Nak1 and Sog1 have been reported as Sid2 targets connecting SIN to the competing morphogenesis-related NDR network, while Fin1/NIMA kinase is reported to be activated by Sid2, linking cytokinesis signaling to Pom1–Wee1 control of later mitotic commitment. These are biologically credible and tied to named primary studies, but because the relevant primary experimental passages were unavailable here, they should be treated as literature-supported relationships rather than revalidated site-level conclusions. Proposed effects on Cdc7, Byr4, and Plo1 in the SIN feedback loop are still less secure as direct-substrate assignments. (ozdemir2022metabolicregulationof pages 122-124, ozdemir2022metabolicregulationofa pages 122-124, sinha2023ageneticstudy pages 24-29, feoktistova2012thefissionyeast pages 7-7)
| Target/process | Sid2 action or relationship | Evidence type and key quantitative detail | Confidence/caveat |
|---|---|---|---|
| Cdc11 SIN scaffold | Sid2–Mob1 phosphorylates Cdc11 at five major sites—S121, S122, S264, S345 and S418—supporting Cdc7 retention, SIN asymmetry and maximal anaphase signaling. | Mass spectrometry, in-vitro kinase assays and phosphomutants. Cytokinesis lasted 48 min in wild type, 57 min in cdc11-S5A and 50 min in cdc11-S5D; Sid2 remained at the division site for 28.75 ± 1.1, 22.75 ± 0.6 and 30.50 ± 0.9 min, respectively. (feoktistova2012thefissionyeast pages 1-2, feoktistova2012thefissionyeast pages 3-4) | High: direct biochemical and functional evidence. The reported minimal substrate motif is RXXS. |
| Mid1/anillin | Sid2 phosphorylates nine RXXS sites—S110, S127, S218, S227, S329, S432, S452, S464 and S531—to remove Mid1 from the cortex, disengage it from Cdr2 and reset division-site organization. | Sid2 phosphorylated wild-type Mid1 but not Mid1-9A in vitro; seven sites were detected by mass spectrometry. Mid1-9A approximately doubled Cdr2 association and recruited Cdr2 into ~75% of contractile rings versus ~18% weak colocalization in wild type; it also delayed ring maturation/constriction and caused positioning defects in sensitized backgrounds. (willet2019ndrkinasesid2 pages 5-6, willet2019ndrkinasesid2 pages 1-3, willet2019ndrkinasesid2 pages 6-8) | High: direct phosphorylation and phosphosite-mutant evidence; individual contributions of the nine sites were not fully resolved. |
| Cdc12 formin | Sid2-dependent phosphorylation inhibits Cdc12 multimerization and inappropriate F-actin bundling, preventing persistent Cdc12 clusters and contractile-ring collapse when cytokinesis is delayed. | Biochemical and phosphomutant findings are reported in the primary Cdc12 study and summarized in later S. pombe literature. (sinha2023ageneticstudy pages 24-29) | Moderate–high: accepted direct substrate relationship, but the retrieved citable excerpt does not supply site-level or quantitative primary data. |
| Clp1/Cdc14 phosphatase | Sid2 phosphorylation promotes cytoplasmic retention of Clp1, linking SIN activation to persistence of a late-mitotic phosphatase at the cytokinetic compartment. | Prior direct study is identified in the retrieved literature; subsequent work distinguishes Clp1-mediated removal of Cdk1 sites on Cdc11 from Sid2-site regulation. (feoktistova2012thefissionyeast pages 1-2, chen2013comprehensiveproteomicsanalysis pages 7-8, chen2013comprehensiveproteomicsanalysis pages 13-13) | Moderate–high: Clp1 is literature-supported as a Sid2 substrate, but detailed site and assay results were not available in the retrieved excerpts. |
| Cdr2 and Klp2 | Reported Sid2 substrates implicated in clearing interphase division-site machinery and restoring interphase organization after cytokinesis; Cdr2 cooperates with Mid1 phosphorylation in medial placement. | Combining cdr2-2A with mid1-9A produced off-center septa although either single mutant did not; the retrieved text names Klp2 as a Sid2 substrate without equivalent mechanistic detail. (willet2019ndrkinasesid2 pages 6-8, willet2019ndrkinasesid2 pages 5-6) | Moderate for Cdr2; limited for Klp2: functional phosphosite evidence supports Cdr2, whereas the retrieved evidence for Klp2 is secondary. |
| Nak1 and Sog1; MOR pathway | Reported Sid2 phosphorylation connects active SIN to inhibition or reconfiguration of the competing morphogenesis-related NDR network during division. | Listed as Sid2 substrates in a 2023 S. pombe synthesis, without primary site-level data in the retrieved excerpt. (sinha2023ageneticstudy pages 24-29) | Provisional in this evidence set: plausible pathway crosstalk, but direct biochemical validation should be checked in the original primary study. |
| Fin1/NIMA kinase | Sid2 reportedly activates Fin1, coupling cytokinesis signaling to Pom1–Wee1 control of subsequent mitotic commitment. | Relationship identified through the primary-study citation and contemporary synthesis. (ozdemir2022metabolicregulationof pages 122-124, ozdemir2022metabolicregulationofa pages 122-124) | Moderate: supported by a named primary study, but its experimental details were unavailable in the retrieved text. |
| SPB localization | Sid2–Mob1 occupies spindle pole bodies as the terminal kinase module of the SIN; SPB recruitment provides a scaffolded signaling platform and contributes to asymmetric anaphase SIN activity. | Live-cell localization and genetic dependency studies show that Sid2 SPB localization is Spg1-independent, while Sid2 feedback through Cdc11 regulates Cdc7 dynamics. (feoktistova2012thefissionyeast pages 1-2, feoktistova2012thefissionyeast pages 7-7) | High: replicated localization and functional evidence. SPB occupancy does not by itself establish catalytic activation. |
| Contractile-ring/division-site localization | Sid2–Mob1 relocates to the medial contractile ring/division site during cytokinesis; this recruitment depends on upstream SIN signaling and coincides with Mid1 departure and ring constriction. | Live-cell imaging detected division-site Sid2 for 28.75 ± 1.1 min in wild type; localization changes in Cdc11 phosphomutants correlated with altered cytokinesis timing. (feoktistova2012thefissionyeast pages 3-4, willet2019ndrkinasesid2 pages 1-3, feoktistova2012thefissionyeast pages 1-2) | High: direct imaging evidence; Sid2 is intracellular and acts at SPBs and the cell equator rather than outside the cell. |
| Overall SIN output | As the terminal Mob1-associated NDR-family serine/threonine kinase, Sid2 converts upstream Spg1–Cdc7–Sid1 signaling into contractile-ring maintenance/constriction, septum formation, division-site resetting and feedback that establishes SIN asymmetry. | Genetic, biochemical and imaging evidence; loss-of-function disrupts or delays cytokinesis, whereas substrate phosphomutants separate specific outputs. (feoktistova2012thefissionyeast pages 1-2, ozdemir2022metabolicregulationofa pages 29-31, willet2019ndrkinasesid2 pages 1-3) | High for the core cytokinesis function: the pathway is often drawn as linear, but direct biochemical proof for every upstream activation step remains incomplete. |
Table: Evidence matrix summarizing validated and proposed substrates, localization dynamics, and pathway outputs of the S. pombe Sid2 kinase. Confidence labels distinguish direct biochemical findings from relationships supported mainly by secondary or incomplete retrieved evidence.
The primary function of Sid2 is to execute and spatially coordinate late cytokinesis. Its phosphorylation program:
Loss of Sid2 or Mob1 can block or delay cytokinesis and may cause lysis during division. The phenotypic diversity of conditional alleles cautions against defining Sid2 solely by the classic multinucleate phenotype of upstream SIN mutants. Likewise, overexpression of sid2 is not by itself strongly toxic, unlike overactivation of Spg1 or Cdc7, implying that Sid2 activity is constrained by Mob1, localization, upstream activation, and cell-cycle context. (ozdemir2022metabolicregulationofa pages 29-31)
The 2023–2024 literature located for this report largely consolidates Sid2 within increasingly detailed models of fission-yeast cytokinesis rather than overturning its established molecular function. Two 2024 reviews emphasize that contractile-ring assembly, maturation, constriction, septum deposition, septin organization, and membrane remodeling are coordinated processes, with SIN activity—and Sid2 at the ring—serving as a central regulatory axis. Relevant publications are Zheng, Zheng & Fu, “The Roles of Septins in Regulating Fission Yeast Cytokinesis,” January 2024, DOI 10.3390/jof10020115, and Rezig, Yaduma & McInerny, “Processes Controlling the Contractile Ring during Cytokinesis in Fission Yeast, Including the Role of ESCRT Proteins,” February 2024, DOI 10.3390/jof10020154.
A 2023 synthesis also places Sid2–Mob1 downstream of Cdc7 and Sid1 and highlights Cdc12, Klp2, Nak1, and Sog1 as outputs connecting cytokinesis, spindle behavior, and MOR-network suppression. However, its Sid2 statements mostly synthesize earlier mechanistic studies rather than report a new purified-kinase or structural analysis. (sinha2023ageneticstudy pages 24-29)
Accordingly, the most precise current interpretation is that recent work has broadened the cellular context, whereas substrate-defining evidence remains concentrated in foundational primary studies from 2008–2019. Absence of a Sid2-focused 2023–2024 paper should not be misconstrued as uncertainty about the core annotation; Cdc11 and Mid1 phosphorylation, SPB-to-ring localization, and terminal SIN function are strongly established.
Sid2 itself has no established clinical or industrial implementation. Its current application is principally as a research tool and conserved-pathway model:
The translational relevance is therefore conceptual rather than direct: cytokinesis failure can generate multinucleate or genomically unstable cells, and NDR/LATS signaling is broadly conserved, but findings about Sid2 should not be equated automatically with a therapeutic target in humans.
High-confidence annotation: Sid2 is an essential Mob1-associated NDR/LATS-family serine/threonine kinase, terminal SIN component, and intracellular regulator at SPBs and the medial contractile ring. Its best-established consensus is RXXS, and its primary function is cytokinesis/septation. (feoktistova2012thefissionyeast pages 1-2, ozdemir2022metabolicregulationofa pages 29-31, willet2019ndrkinasesid2 pages 1-3)
Strongest substrate evidence: Cdc11 and Mid1 have convergent in-vitro phosphorylation, mass-spectrometric site mapping, phosphosite mutants, quantitative imaging, and functional phenotypes. Cdc12 and Clp1 are accepted direct targets in the literature, although fewer details from their primary experiments were recoverable in this search. (feoktistova2012thefissionyeast pages 3-4, willet2019ndrkinasesid2 pages 1-3, chen2013comprehensiveproteomicsanalysis pages 13-13)
Important unresolved issues: a complete quantitative Sid2 substrate atlas is lacking; RXXS occurs by chance in many proteins; the biochemical mechanism by which each upstream SIN module activates Sid2–Mob1 remains incompletely reconstructed; and several reported targets need modern site-resolved validation. It also remains important to separate Sid2’s direct catalytic outputs from secondary changes caused by failed cytokinesis or altered cell-cycle progression.
References
(feoktistova2012thefissionyeast pages 1-2): Anna Feoktistova, Jennifer Morrell-Falvey, Jun-Song Chen, N. Sadananda Singh, Mohan K. Balasubramanian, and Kathleen L. Gould. The fission yeast septation initiation network (sin) kinase, sid2, is required for sin asymmetry and regulates the sin scaffold, cdc11. May 2012. URL: https://doi.org/10.1091/mbc.e11-09-0792, doi:10.1091/mbc.e11-09-0792. This article has 60 citations and is from a domain leading peer-reviewed journal.
(ozdemir2022metabolicregulationofa pages 29-31): Ö Uysal Özdemir. Metabolic regulation of cytokinesis in schizosaccharomyces pombe. Unknown journal, 2022.
(willet2019ndrkinasesid2 pages 1-3): Alaina H. Willet, Ashley K. DeWitt, Janel R. Beckley, Dawn M. Clifford, and Kathleen L. Gould. Ndr kinase sid2 drives anillin-like mid1 from the membrane to promote cytokinesis and medial division site placement. Current Biology, 29:1055-1063.e2, Mar 2019. URL: https://doi.org/10.1016/j.cub.2019.01.075, doi:10.1016/j.cub.2019.01.075. This article has 28 citations and is from a highest quality peer-reviewed journal.
(feoktistova2012thefissionyeast pages 3-4): Anna Feoktistova, Jennifer Morrell-Falvey, Jun-Song Chen, N. Sadananda Singh, Mohan K. Balasubramanian, and Kathleen L. Gould. The fission yeast septation initiation network (sin) kinase, sid2, is required for sin asymmetry and regulates the sin scaffold, cdc11. May 2012. URL: https://doi.org/10.1091/mbc.e11-09-0792, doi:10.1091/mbc.e11-09-0792. This article has 60 citations and is from a domain leading peer-reviewed journal.
(feoktistova2012thefissionyeast pages 6-7): Anna Feoktistova, Jennifer Morrell-Falvey, Jun-Song Chen, N. Sadananda Singh, Mohan K. Balasubramanian, and Kathleen L. Gould. The fission yeast septation initiation network (sin) kinase, sid2, is required for sin asymmetry and regulates the sin scaffold, cdc11. May 2012. URL: https://doi.org/10.1091/mbc.e11-09-0792, doi:10.1091/mbc.e11-09-0792. This article has 60 citations and is from a domain leading peer-reviewed journal.
(willet2019ndrkinasesid2 pages 6-8): Alaina H. Willet, Ashley K. DeWitt, Janel R. Beckley, Dawn M. Clifford, and Kathleen L. Gould. Ndr kinase sid2 drives anillin-like mid1 from the membrane to promote cytokinesis and medial division site placement. Current Biology, 29:1055-1063.e2, Mar 2019. URL: https://doi.org/10.1016/j.cub.2019.01.075, doi:10.1016/j.cub.2019.01.075. This article has 28 citations and is from a highest quality peer-reviewed journal.
(willet2019ndrkinasesid2 pages 5-6): Alaina H. Willet, Ashley K. DeWitt, Janel R. Beckley, Dawn M. Clifford, and Kathleen L. Gould. Ndr kinase sid2 drives anillin-like mid1 from the membrane to promote cytokinesis and medial division site placement. Current Biology, 29:1055-1063.e2, Mar 2019. URL: https://doi.org/10.1016/j.cub.2019.01.075, doi:10.1016/j.cub.2019.01.075. This article has 28 citations and is from a highest quality peer-reviewed journal.
(sinha2023ageneticstudy pages 24-29): D Sinha. A genetic study of fission yeast pkd2. Unknown journal, 2023.
(chen2013comprehensiveproteomicsanalysis pages 7-8): Jun-Song Chen, Matthew R. Broadus, Janel R. McLean, Anna Feoktistova, Liping Ren, and Kathleen L. Gould. Comprehensive proteomics analysis reveals new substrates and regulators of the fission yeast clp1/cdc14 phosphatase. May 2013. URL: https://doi.org/10.1074/mcp.m112.025924, doi:10.1074/mcp.m112.025924. This article has 74 citations and is from a domain leading peer-reviewed journal.
(chen2013comprehensiveproteomicsanalysis pages 13-13): Jun-Song Chen, Matthew R. Broadus, Janel R. McLean, Anna Feoktistova, Liping Ren, and Kathleen L. Gould. Comprehensive proteomics analysis reveals new substrates and regulators of the fission yeast clp1/cdc14 phosphatase. May 2013. URL: https://doi.org/10.1074/mcp.m112.025924, doi:10.1074/mcp.m112.025924. This article has 74 citations and is from a domain leading peer-reviewed journal.
(ozdemir2022metabolicregulationof pages 122-124): Ö Uysal Özdemir. Metabolic regulation of cytokinesis in schizosaccharomyces pombe. Unknown journal, 2022.
(ozdemir2022metabolicregulationofa pages 122-124): Ö Uysal Özdemir. Metabolic regulation of cytokinesis in schizosaccharomyces pombe. Unknown journal, 2022.
(feoktistova2012thefissionyeast pages 7-7): Anna Feoktistova, Jennifer Morrell-Falvey, Jun-Song Chen, N. Sadananda Singh, Mohan K. Balasubramanian, and Kathleen L. Gould. The fission yeast septation initiation network (sin) kinase, sid2, is required for sin asymmetry and regulates the sin scaffold, cdc11. May 2012. URL: https://doi.org/10.1091/mbc.e11-09-0792, doi:10.1091/mbc.e11-09-0792. This article has 60 citations and is from a domain leading peer-reviewed journal.