The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is correctly identified as CLN2/YPL256C, encoding the G1/S-specific cyclin Cln2 (UniProt P20438) in Saccharomyces cerevisiae S288c. This is not the unrelated human lysosomal-disease gene historically called CLN2 (now TPP1). The yeast protein belongs to the cyclin family and contains the conserved cyclin-box/cyclin-like fold expected for a Cdk-binding regulatory subunit. Cln1 and Cln2 are 57% identical overall and 72% identical in their N-terminal cyclin-box regions, independently supporting the supplied InterPro annotations—Cyclin-like domain/superfamily, Cyclin_N, Cyclin_CLN, and cyclin box. (mendenhall1998regulationofcdc28 pages 8-9, quilis2017acomparativestudy pages 1-2)
Cln2 is not an enzyme by itself. Its primary molecular function is to bind and activate the serine/threonine kinase Cdc28, the budding-yeast CDK1 homolog. The resulting Cln2–Cdc28 complex phosphorylates selected proteins at Start, thereby coupling commitment to a new division cycle with bud emergence, cell polarization, and preparation for DNA replication. (mendenhall1998regulationofcdc28 pages 8-9, miller2005identificationofnovel pages 1-2, ercan2021buddingyeastrelies pages 9-10)
| Aspect | Best-supported conclusion | Evidence type / quantitative detail | Key source, date, DOI URL |
|---|---|---|---|
| Identity and domain | CLN2/YPL256C/P20438 is the Saccharomyces cerevisiae G1/S cyclin Cln2. It is a cyclin-family regulatory protein containing an N-terminal cyclin box, not human lysosomal CLN2/TPP1. | Sequence/domain evidence: Cln1 and Cln2 are 57% identical overall and 72% identical in their N-terminal cyclin-box regions, consistent with cyclin-family membership and CDK binding. (mendenhall1998regulationofcdc28 pages 8-9, quilis2017acomparativestudy pages 1-2) | Mendenhall & Hodge, Dec. 1998, DOI; Quilis & Igual, 2017, DOI |
| Cdc28 partner role | Cln2 is not itself an enzyme. It binds and activates the serine/threonine kinase Cdc28/CDK1, helping determine when, where, and toward which substrates Cdc28 acts in late G1. | Biochemical and genetic evidence identifies Cln2-Cdc28 kinase activity at Start; the conserved cyclin box mediates cyclin-CDK association. (mendenhall1998regulationofcdc28 pages 8-9, miller2005identificationofnovel pages 1-2) | Mendenhall & Hodge, Dec. 1998, DOI; Miller et al., Oct. 2005, DOI |
| Start feedback and Whi5 | Cln2-Cdc28 can phosphorylate the SBF repressor Whi5, reinforcing SBF-dependent CLN1/CLN2 transcription and Start commitment. Current models also incorporate Swi6 phosphorylation and Bck2-dependent activation, so Whi5 phosphorylation is not the sole Start trigger. | Biochemical evidence supports Whi5 phosphorylation by Cln2-Cdc28. In broader Start-network evidence, nonphosphorylatable WHI5-12A or SWI6-SA4 mutants individually retained wild-type size, whereas the double mutant was about 40% larger; this was not a direct Cln2-specific measurement. (bloom2007multiplelevelsof pages 3-4, ravi2024modelingthestart pages 3-5) | Bloom & Cross, Feb. 2007, DOI; Ravi et al., Aug. 2, 2024, DOI |
| Sic1 and S-phase entry | Cln1/2-Cdc28 phosphorylates the CDK inhibitor Sic1, promoting SCF-Cdc4-dependent Sic1 destruction. This releases Clb5/6-Cdc28 activity and permits replication initiation; Cln2 therefore facilitates S phase indirectly rather than catalyzing DNA replication. | Mechanistic biochemical and genetic evidence supports the phosphorylation-ubiquitylation cascade. The 2024 START-BYCC study incorporates this established mechanism into a model rather than newly testing Cln2 alone. (mendenhall1998regulationofcdc28 pages 8-9, vigano2011yeastcellsizeb pages 78-82, ravi2024modelingthestart pages 3-5) | Mendenhall & Hodge, Dec. 1998, DOI; Ravi et al., Aug. 2, 2024, DOI |
| Budding and polarity | Cln2-Cdc28 has a cyclin-specific role in initiating polarized growth and bud emergence, beyond merely increasing total CDK activity. Its substrate specificity couples cell-cycle progression to morphogenesis. | Direct synthetic-cell-cycle experiments showed that a mitotic cyclin could support much of ordered cell-cycle progression but could not replace G1-cyclin function in polarization and budding. LP-motif docking contributes but does not fully explain Cln2 specificity. (ercan2021buddingyeastrelies pages 9-10) | Ercan et al., June 4, 2021, DOI |
| Localization | Cln2 is predominantly cytoplasmic and can occur at polarized-growth sites, while a nuclear pool supports Start-related functions. Cdc28-dependent phosphorylation and nuclear import/export signals regulate this distribution. | Localization and rescue experiments found that cytoplasmic Cln2 could rescue budding-related defects; mutation of Cdc28 consensus sites caused nuclear localization. Forced nuclear export compromises some Cln2 activity, supporting functional pools in both compartments. (vigano2011yeastcellsize pages 78-82, bloom2007multiplelevelsof pages 3-4, vigano2011yeastcellsizeb pages 78-82) | Bloom & Cross, Feb. 2007, DOI; localization synthesis reported in 2011. (vigano2011yeastcellsize pages 78-82) |
| Turnover and E3-ligase disagreement | Cln2 is a short-lived phosphoprotein degraded through SCF ubiquitin ligases and the proteasome. SCF-Grr1 involvement is strongly supported; SCF-Cdc4 involvement is context-dependent and disputed. | Reported half-life is approximately 10 minutes or generally under 15 minutes. One study concluded that cytoplasmic Cln2 is targeted in vivo by SCF-Grr1, although Cdc4 can recognize phosphorylated Cln2 when forced into the cytoplasm. A later study reported contributions from both SCF-Grr1 and SCF-Cdc4. Deleting residues 373-409 stabilizes Cln2, with further stabilization after deleting 373-545. (zheng2024probingcellcycle pages 26-30, brambila2024evidencefornovel pages 5-6, quilis2017acomparativestudy pages 1-2) | Landry et al., July 2012, DOI; Quilis & Igual, 2017, DOI; Brambila et al., Apr. 2024, DOI |
| Redundancy and essentiality | CLN2 is not individually essential under standard laboratory conditions because Cln1 and Cln3 provide overlapping G1-cyclin activity. At least one of CLN1, CLN2, or CLN3 is required for Start. | Loss of any two CLN genes is viable, whereas loss of all three causes Start/G1 arrest. cln1Δ cln2Δ cells grow slowly, have abnormal morphology, and delay bud emergence and DNA-synthesis initiation, demonstrating incomplete redundancy. (mendenhall1998regulationofcdc28 pages 8-9, measday1998rolesofthe pages 33-37) | Mendenhall & Hodge, Dec. 1998, DOI |
| 2024 post-transcriptional regulation | Cell-cycle-dependent Cln2 accumulation is not controlled solely by the canonical CLN2 promoter. Cln3 can influence Cln2 protein accumulation through post-transcriptional mechanisms, potentially including modulation of SCF-Grr1-dependent turnover. | Direct experiments found that periodic Cln2 protein expression persisted without normal CLN2-promoter functions. The proposed Cln3-SCF-Grr1 mechanism is supported but remains less established than the core Grr1 turnover pathway. (brambila2024evidencefornovel pages 5-6) | Brambila et al., Apr. 2024, DOI |
| 2024 integrated Start modeling | A contemporary model places Cln1/2 downstream of Cln3/Bck2-SBF/MBF and upstream of bud emergence, Sic1/Cdc6 degradation, and Clb5/6 activation. It emphasizes redundant and spatially distributed control rather than a single irreversible Whi5 switch. | Model, not a direct Cln2 experiment: START-BYCC reportedly reproduces phenotypes of approximately 150 Start mutants. Simulations define Start by origin-firing activation and model daughter-cell size at approximately 0.46 times total size at division. (ravi2024modelingthestart pages 30-31, ravi2024modelingthestart pages 12-14, ravi2024modelingthestart pages 2-3) | Ravi et al., Aug. 2, 2024, DOI |
Table: Evidence summary for S. cerevisiae Cln2, distinguishing direct biochemical and genetic findings from network models. The table also highlights quantitative observations and the unresolved disagreement over SCF-Cdc4 involvement in Cln2 turnover.
The cyclin box provides the structural interface through which Cln2 associates with Cdc28. Cdc28 supplies catalytic kinase activity, whereas Cln2 supplies activation, timing, localization, and substrate-selection functions. Accordingly, no independent catalytic reaction or small-molecule substrate should be assigned to Cln2. The relevant biochemical reaction is Cdc28-catalyzed protein phosphorylation using ATP, with Cln2 directing that kinase toward a late-G1 substrate repertoire. (mendenhall1998regulationofcdc28 pages 8-9, miller2005identificationofnovel pages 1-2)
Cln2 is one of three partially redundant G1 cyclins, with Cln1 being its closest paralog. Loss of any one—or even any two—CLN genes can be tolerated under standard laboratory conditions, but removal of all three causes arrest at Start. A cln1Δ cln2Δ strain grows slowly, has abnormal morphology, and delays both bud emergence and DNA-replication initiation, demonstrating that redundancy is substantial but incomplete. (mendenhall1998regulationofcdc28 pages 8-9, measday1998rolesofthe pages 33-37)
Cln2–Cdc28 preferentially acts on regulatory proteins bearing suitable CDK phosphosites plus cyclin-docking elements. LP-motif docking contributes to G1-cyclin substrate recognition, but synthetic-cell-cycle experiments indicate that this docking surface alone does not account for all Cln2 specificity. Thus, the current view is that substrate selection combines phosphosite context, docking motifs, localization, and additional interactions that remain incompletely defined. (ercan2021buddingyeastrelies pages 9-10)
This qualitative specificity has physiological importance. A mitotic cyclin can replace G1 cyclins sufficiently to drive much of the ordered nuclear cell cycle, yet such cells fail to polarize and bud. Restoring Cln2 restores access to morphogenetic substrates. Consequently, Cln2 does more than raise bulk Cdc28 activity: it couples cell-cycle commitment to the spatial program of daughter-cell construction. (ercan2021buddingyeastrelies pages 9-10)
In the canonical Start network, growth- and nutrient-sensitive inputs through Cln3 and Bck2 activate the SBF and MBF transcription factors. SBF induces CLN1 and CLN2, after which Cln1/2–Cdc28 reinforces the transition by phosphorylating the SBF repressor Whi5. This creates positive feedback that sharpens late-G1 transcription and promotes commitment. (bloom2007multiplelevelsof pages 3-4, ravi2024modelingthestart pages 3-5)
The pathway is not a simple one-protein switch. Recent integrated analysis emphasizes partially redundant control through Whi5, Swi6, Bck2, and spatially distributed cyclin activity. Individually, nonphosphorylatable WHI5-12A and SWI6-SA4 mutants had approximately wild-type cell size, whereas the double mutant was about 40% larger, indicating that phosphorylation of either branch can support timely Start. This statistic concerns the broader Start network, not a direct Cln2 perturbation. (ravi2024modelingthestart pages 3-5)
Cln1/2–Cdc28 phosphorylates Sic1, an inhibitor of Clb5/6–Cdc28. Multisite phosphorylation creates recognition signals for SCF^Cdc4, leading to Sic1 ubiquitylation and proteasomal degradation. Removing Sic1 inhibition activates the S-phase cyclins Clb5 and Clb6 and permits replication-origin firing. Cln2 therefore promotes DNA replication indirectly, by dismantling a CDK-inhibitory barrier; it is neither a replication enzyme nor an origin component. (mendenhall1998regulationofcdc28 pages 8-9, vigano2011yeastcellsizeb pages 78-82, ravi2024modelingthestart pages 3-5, ravi2024modelingthestart pages 2-3)
Cln1/2 activity is also associated with Cdc6 turnover, spindle-pole-body duplication, repression of the pheromone response, and passage through the Start commitment point. These outputs coordinate DNA-replication competence with centrosome-equivalent duplication and the decision to continue mitotic growth rather than mating differentiation. (mendenhall1998regulationofcdc28 pages 8-9, ravi2024modelingthestart pages 2-3)
A particularly well-supported Cln2 function is activation of polarized growth. Cln2–Cdc28 phosphorylates components of the budding and polarity machinery, triggering cortical polarization, localized cell-wall growth, and bud emergence. Historical deletion phenotypes and modern cyclin-replacement experiments agree that this function is not fully interchangeable with mitotic-cyclin activity. (vigano2011yeastcellsize pages 78-82, mendenhall1998regulationofcdc28 pages 8-9, ercan2021buddingyeastrelies pages 9-10)
This finding resolves a long-standing “quantitative versus qualitative” question in CDK biology. Rising CDK activity can order many cell-cycle events quantitatively, but budding yeast additionally requires G1-cyclin-specific substrate access to coordinate morphogenesis with nuclear-cycle progression. Ercan and colleagues’ synthetic-cycle study is especially strong experimental evidence for this interpretation because it separates general Cdc28 activation from Cln2-dependent morphogenesis. Published June 4, 2021: https://doi.org/10.1126/sciadv.abg0007. (ercan2021buddingyeastrelies pages 9-10)
Cln2 is predominantly cytoplasmic and can concentrate at sites of polarized growth, consistent with its role in budding. Cytoplasmic Cln2 can rescue defects involving budding proteins where nuclear-restricted forms cannot, providing functional—not merely imaging—evidence for a cytoplasmic morphogenetic pool. (vigano2011yeastcellsize pages 78-82, vigano2011yeastcellsizeb pages 78-82)
A nuclear pool is nevertheless important for Start transcription and nuclear substrates such as Whi5 and Sic1. Artificially increasing nuclear export compromises some Cln2 functions. Cdc28-dependent phosphorylation helps control the balance: mutation of Cdc28 consensus sites can drive Cln2 into the nucleus, implicating phosphorylation-regulated import/export signals. The most accurate annotation is therefore dynamic nucleocytoplasmic localization with prominent cytoplasmic and polarized-growth-site function, rather than an exclusively nuclear or cytoplasmic protein. (bloom2007multiplelevelsof pages 3-4, vigano2011yeastcellsizeb pages 78-82)
Localization also influences degradation. The Cln2 N terminus participates in nuclear import, while exported forms can be less stable. Compartmental separation of Cln2 from particular F-box proteins helps explain why different studies have assigned somewhat different ubiquitin ligases to its turnover. (quilis2017acomparativestudy pages 1-2)
CLN2 transcription and protein accumulation rise in late G1 around Start, coinciding with maximal Cln1/2-associated kinase activity. Cln2 then disappears rapidly, restricting its activity to a narrow interval and preventing inappropriate persistence of G1-specific phosphorylation. (mendenhall1998regulationofcdc28 pages 8-9, zheng2024probingcellcycle pages 26-30, measday1998rolesofthe pages 33-37)
The protein is highly unstable, with an estimated half-life of approximately 10 minutes, and older measurements generally place it below 15 minutes. C-terminal PEST-rich sequences contribute to instability: deletion of residues 373–409 substantially stabilizes Cln2, and deletion through residue 545 causes additional stabilization. Transferring Cln2 residues 376–545 can confer instability on another protein. (zheng2024probingcellcycle pages 26-30, quilis2017acomparativestudy pages 1-2)
SCF^Grr1-mediated ubiquitylation and proteasomal destruction are strongly established. Loss of SCF^Grr1 activity impairs normal Cln2 turnover and causes abnormal accumulation. A 2024 study continues to treat this as the principal known pathway. (bloom2007multiplelevelsof pages 3-4, brambila2024evidencefornovel pages 5-6)
The role of SCF^Cdc4 is less settled. Landry and colleagues reported that cytoplasmic Cln2 is targeted in vivo chiefly by Grr1, although Cdc4 can bind phosphorylated Cln2 and degrade it when Cdc4 is experimentally redirected to the cytoplasm. Quilis and Igual later concluded that both SCF^Grr1 and SCF^Cdc4 contribute to Cln2 degradation and mapped the Cdc4-dependent behavior to the Cln2 N terminus. The difference likely reflects strain, assay, compartment, or indirect effects; therefore, annotation should state secure SCF^Grr1 dependence, with context-dependent evidence for SCF^Cdc4, rather than treating either formulation as universally resolved. Quilis and Igual, published 2017: https://doi.org/10.1002/2211-5463.12157. (quilis2017acomparativestudy pages 1-2)
Brambila and colleagues challenged the assumption that periodic Cln2 expression is generated solely at the CLN2 promoter. They found that cell-cycle-dependent Cln2 protein accumulation persisted without normal promoter functions and that Cln3 can influence Cln2 through post-transcriptional mechanisms. They proposed modulation of SCF^Grr1-dependent turnover as one possibility because Cln3 can associate with the complex and altered Cln3 forms bind its components less effectively. The core evidence for post-transcriptional regulation is stronger than the still-developing mechanistic assignment to direct Cln3–SCF regulation. Published April 2024: https://doi.org/10.1091/mbc.e23-05-0174. (brambila2024evidencefornovel pages 5-6)
The 2024 START-BYCC model integrates Cln1/2 downstream of Cln3/Bck2–SBF/MBF and upstream of budding, Sic1/Cdc6 degradation, and Clb5/6 activation. It reportedly reproduces phenotypes for approximately 150 Start mutants and explicitly incorporates localization, nutrient effects, transcriptional feedback, and inhibitor dynamics. This is a systems-level synthesis rather than a new direct Cln2 biochemical experiment. Published August 2, 2024: https://doi.org/10.1371/journal.pcbi.1012048. (ravi2024modelingthestart pages 30-31, ravi2024modelingthestart pages 12-14, ravi2024modelingthestart pages 2-3)
The model and associated recent evidence replace an overly simple irreversible Whi5 switch with a distributed network containing redundant phosphorylation routes and conditional reversibility under starvation. Cln2 remains a central positive-feedback and effector module, but it is embedded in a network capable of buffering single perturbations. (ravi2024modelingthestart pages 12-14, ravi2024modelingthestart pages 3-5)
CLN2 is principally a research and engineering tool, not a clinical target or industrial catalyst. Current uses include:
Recommended primary annotation:
G1/S cyclin that binds and activates Cdc28/CDK1 at Start. The Cln2–Cdc28 kinase promotes positive feedback in G1/S transcription, phosphorylates inhibitors including Sic1 to permit activation of S-phase cyclin–CDK complexes, and provides cyclin-specific substrate recognition required for cell polarization and bud emergence.
Recommended localization annotation:
Dynamic nuclear–cytoplasmic protein, predominantly cytoplasmic and enriched at polarized-growth sites during late G1, with a functional nuclear pool for Start-regulatory substrates.
Recommended process terms: G1/S transition, Start commitment, positive regulation of CDK activity, protein phosphorylation through Cdc28 activation, Sic1-dependent control of DNA-replication initiation, bud emergence, establishment of cell polarity, spindle-pole-body duplication, response to mating pheromone, and ubiquitin-dependent proteolysis.
Confidence assessment: High for identity, cyclin-family classification, Cdc28 activation, late-G1 timing, Sic1/Start function, and morphogenesis. Moderate-to-high for compartment-specific functions. High for SCF^Grr1 turnover, but only moderate for a general physiological SCF^Cdc4 contribution because the published localization-dependent and genetic results do not fully agree. (mendenhall1998regulationofcdc28 pages 8-9, bloom2007multiplelevelsof pages 3-4, ercan2021buddingyeastrelies pages 9-10, quilis2017acomparativestudy pages 1-2)
References
(mendenhall1998regulationofcdc28 pages 8-9): Michael D. Mendenhall and Amy E. Hodge. Regulation of cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast saccharomyces cerevisiae. Microbiology and Molecular Biology Reviews, 62:1191-1243, Dec 1998. URL: https://doi.org/10.1128/mmbr.62.4.1191-1243.1998, doi:10.1128/mmbr.62.4.1191-1243.1998. This article has 706 citations and is from a domain leading peer-reviewed journal.
(quilis2017acomparativestudy pages 1-2): Inma Quilis and J. Carlos Igual. A comparative study of the degradation of yeast cyclins cln1 and cln2. FEBS Open Bio, 7:74-87, Dec 2017. URL: https://doi.org/10.1002/2211-5463.12157, doi:10.1002/2211-5463.12157. This article has 23 citations and is from a peer-reviewed journal.
(miller2005identificationofnovel pages 1-2): Mary E. Miller, Frederick R. Cross, Alison L. Groeger, and Katherine L. Jameson. Identification of novel and conserved functional and structural elements of the g1 cyclin cln3 important for interactions with the cdk cdc28 in saccharomyces cerevisiae. Yeast, 22:1021-1036, Oct 2005. URL: https://doi.org/10.1002/yea.1292, doi:10.1002/yea.1292. This article has 23 citations and is from a peer-reviewed journal.
(ercan2021buddingyeastrelies pages 9-10): Deniz Pirincci Ercan, Florine Chrétien, Probir Chakravarty, Helen R. Flynn, Ambrosius P. Snijders, and Frank Uhlmann. Budding yeast relies on g 1 cyclin specificity to couple cell cycle progression with morphogenetic development. Jun 2021. URL: https://doi.org/10.1126/sciadv.abg0007, doi:10.1126/sciadv.abg0007. This article has 33 citations and is from a highest quality peer-reviewed journal.
(bloom2007multiplelevelsof pages 3-4): Joanna Bloom and Frederick R. Cross. Multiple levels of cyclin specificity in cell-cycle control. Nature Reviews Molecular Cell Biology, 8:149-160, Feb 2007. URL: https://doi.org/10.1038/nrm2105, doi:10.1038/nrm2105. This article has 743 citations and is from a domain leading peer-reviewed journal.
(ravi2024modelingthestart pages 3-5): Janani Ravi, Kewalin Samart, and Jason Zwolak. Modeling the start transition in the budding yeast cell cycle. Aug 2024. URL: https://doi.org/10.1371/journal.pcbi.1012048, doi:10.1371/journal.pcbi.1012048. This article has 1 citations and is from a highest quality peer-reviewed journal.
(vigano2011yeastcellsizeb pages 78-82): M Vigano. Yeast cell size control: an interplay among ribosome biogenesis, protein synthesis and mapk routes. Unknown journal, 2011.
(vigano2011yeastcellsize pages 78-82): M Vigano. Yeast cell size control: an interplay among ribosome biogenesis, protein synthesis and mapk routes. Unknown journal, 2011.
(zheng2024probingcellcycle pages 26-30): H Zheng. Probing cell cycle commitment and global transcription regulation at the single-molecule level in budding yeast. Unknown journal, 2024.
(brambila2024evidencefornovel pages 5-6): Amanda Brambila, Beth E. Prichard, Jerry T. DeWitt, and Douglas R. Kellogg. Evidence for novel mechanisms that control cell-cycle entry and cell size. Molecular Biology of the Cell, Apr 2024. URL: https://doi.org/10.1091/mbc.e23-05-0174, doi:10.1091/mbc.e23-05-0174. This article has 9 citations and is from a domain leading peer-reviewed journal.
(measday1998rolesofthe pages 33-37): VR Measday. Roles of the pho85 cyclin-dependent kinase in budding yeast. Unknown journal, 1998.
(ravi2024modelingthestart pages 30-31): Janani Ravi, Kewalin Samart, and Jason Zwolak. Modeling the start transition in the budding yeast cell cycle. Aug 2024. URL: https://doi.org/10.1371/journal.pcbi.1012048, doi:10.1371/journal.pcbi.1012048. This article has 1 citations and is from a highest quality peer-reviewed journal.
(ravi2024modelingthestart pages 12-14): Janani Ravi, Kewalin Samart, and Jason Zwolak. Modeling the start transition in the budding yeast cell cycle. Aug 2024. URL: https://doi.org/10.1371/journal.pcbi.1012048, doi:10.1371/journal.pcbi.1012048. This article has 1 citations and is from a highest quality peer-reviewed journal.
(ravi2024modelingthestart pages 2-3): Janani Ravi, Kewalin Samart, and Jason Zwolak. Modeling the start transition in the budding yeast cell cycle. Aug 2024. URL: https://doi.org/10.1371/journal.pcbi.1012048, doi:10.1371/journal.pcbi.1012048. This article has 1 citations and is from a highest quality peer-reviewed journal.