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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 the budding-yeast G1/S-specific cyclin Cln3, encoded by CLN3/YAL040C, with historical aliases WHI1, DAF1, and FUN10, in Saccharomyces cerevisiae S288c. It is not the unrelated human CLN3 lysosomal protein associated with neuronal ceroid lipofuscinosis. The literature identifies yeast Cln3 as a cyclin containing a conserved cyclin-box-like region—approximately residues 99–210—whose predicted cyclin-fold helices are required for function and productive interaction with the Cdc28/Cdk1 cell-cycle kinase. This agrees with the supplied UniProt and InterPro cyclin-family/domain annotations. (miller2005identificationofnovel pages 1-2, brambila2021controlofcell pages 13-19)
Cln3 is not an independently catalytic enzyme, transporter, or structural protein. Its primary function is to act as a scarce, unstable regulatory cyclin for Cdc28/Cdk1, directing kinase-dependent activation of the Start transcriptional program in late G1. The most secure functional chain is:
cell growth/nutrient state → Cln3 abundance and localization → Cdc28/Cdk1-dependent activation of Start transcription → CLN1/CLN2 expression and positive feedback → commitment to budding, DNA replication, and division.
The identity of the initiating physiological phosphorylation target remains unsettled. Direct phosphorylation of the transcriptional repressor Whi5 is the traditional model, whereas newer evidence proposes promoter-localized phosphorylation of RNA polymerase II Rpb1 CTD Ser5. The genetic role of Cln3 in activating Start is firm; the precise direct substrate is not. (brambila2021controlofcell pages 23-30, koivomagi2021localizedphosphorylationof pages 3-5)
| Aspect | Best-supported conclusion | Evidence type / key quantitative result | Confidence or caveat |
|---|---|---|---|
| Identity/domain | Target is budding-yeast Cln3, encoded by CLN3/WHI1/DAF1 (YAL040C), a G1 cyclin with a cyclin-box-like region at approximately residues 99–210. Disrupting predicted cyclin-fold helices impairs function and Cdc28-related activity. | Genetic identification plus structure–function mutagenesis; linker insertions in predicted helices 1, 2, 3, and 5 abolished function. (miller2005identificationofnovel pages 1-2, brambila2021controlofcell pages 13-19) | High. Matches S. cerevisiae S288c UniProt P13365; it is unrelated to human lysosomal CLN3 despite the shared symbol. |
| Primary molecular role | Cln3 is a regulatory cyclin rather than an enzyme acting alone: it promotes activation/localization of Cdc28/Cdk1 kinase activity to initiate cell-cycle entry. | Co-immunoprecipitation, mutational, fusion-protein, and genetic evidence support functional Cln3–Cdc28 coupling; kinase-dead Cln3–Cdk1 fusions failed to support proliferation. (tyers1993comparisonofthe pages 1-2, koivomagi2021localizedphosphorylationof pages 3-5, miller2005identificationofnovel pages 1-2) | High for Cdk1-dependent function; moderate for complex biochemistry. Cln3 is extremely scarce, and some experiments did not recover a stable stoichiometric complex or strong kinase activity. (brambila2021controlofcell pages 23-30, brambila2021controlofcell pages 42-48) |
| Pathway at Start | Cln3 acts upstream in early G1 to activate Start-specific transcription through SBF and, less directly, the broader G1/S program; induction of CLN1/CLN2 creates positive feedback that reinforces Cdk1 activation and commitment. | Early CLN3 expression induced CLN1, CLN2, HCS26, CLB5, and SWI4; triple cln1 cln2 cln3 deletion is inviable and arrests in G1. (tyers1993comparisonofthe pages 1-2, brambila2021controlofcell pages 19-23) | High. This upstream transcriptional role is more firmly established than the identity of the initiating direct substrate. |
| Direct-substrate controversy | The traditional model assigns Whi5 as a direct Cln3–Cdk1 substrate, but direct phosphorylation evidence is inconsistent. A newer model proposes localized phosphorylation of RNA-polymerase-II Rpb1 CTD Ser5 at SBF promoters. | Whi5-dependent genetics and older in-vitro assays support the canonical model, whereas later assays failed to detect robust Cln3-dependent Whi5 phosphorylation. A 2021 preprint found Rpb1 to be the most specific target among more than 20 candidates; cln3Δ caused an additional 15±5% G1 CTD-Ser5-phosphorylation reduction after Kin28 inhibition, and SBF-tethered Kin28 rescued cln3Δ phenotypes. (brambila2021controlofcell pages 23-30, brambila2021controlofcell pages 19-23, koivomagi2021localizedphosphorylationof pages 3-5) | Controversial. Rpb1-CTD Ser5 is a compelling mechanistic candidate but the cited report is preprint-level; Whi5 is clearly important in Start regulation but is not securely established as Cln3’s direct physiological substrate. |
| Localization | Cln3 is reported to be retained predominantly at the endoplasmic reticulum in early G1 and to accumulate in the nucleus in late G1, where Start transcription occurs. Whi3 binding to GCAU-rich CLN3 mRNA supports ER-associated synthesis/retention. | Localization and RNA-binding experiments; mutating CLN3 GCAU clusters reduced association with Whi3. (colomina2008whi3adevelopmental pages 1-1, colomina2009whi3regulatesmorphogenesis pages 9-9) | Moderate. Nuclear function is strongly consistent with promoter-level action, but the universality and precise trafficking mechanism of the ER-to-nucleus model require cautious interpretation. |
| Turnover/dosage | Cln3 is short-lived, and its abundance strongly controls Start timing. C-terminal truncation cln3-Δ177/CLN3-1 removes a stability determinant, markedly stabilizes Cln3, and advances division. | Wild-type half-life reported at about 10 min, versus roughly 2 h for the stabilized truncation; the allele produces about a 10-fold protein increase in later analyses. (brambila2021controlofcell pages 19-23, brambila2021controlofcell pages 30-33) | High for rapid turnover and dosage sensitivity. Exact ubiquitin-ligase assignments and the description of the deleted region vary among sources; broad SCF/Cdc34 claims should not be made from this evidence alone. |
| Growth/nutrient coupling | Cln3 abundance responds strongly to growth conditions and membrane-growth signaling, linking biosynthetic state to Start. Rich carbon supports greater G1 accumulation than poor carbon; TORC2/sphingolipid/ceramide and membrane-trafficking perturbations affect Cln3. | Quantitative immunoblotting found approximately 10-fold Cln3 accumulation during G1 in rich carbon versus 2.5-fold in poor carbon; estimated concentration rose 7-fold versus 2-fold. Poor-carbon cells were estimated to contain only 10–20 molecules, and poor carbon reduced Cln3 nearly tenfold without changing Whi5. (sommer2020growthdependentsignalsdrive pages 12-15, sommer2020growthdependentsignalsdrive pages 15-16) | Moderate. Quantitative results derive from 2020 preprint-associated evidence; competing size-control models emphasize Whi5 dilution, Cln3 accumulation, or both. |
| Mutant phenotypes | cln3Δ is viable but delays Start and produces larger cells; stabilized or overexpressed CLN3 advances Start and yields smaller cells. Loss of all three G1 cyclins is lethal. Cln3 can influence size and Cln2 production even when WHI5 or normal CLN2 transcriptional control is absent. | Classical dosage genetics; whi5Δ advanced Cln2 production by about 10 min, yet CLN3 manipulation still altered its timing. GAL1-driven CLN3 also reduced size when CLN2 was expressed from MET25. (tyers1993comparisonofthe pages 1-2, brambila2021controlofcell pages 13-19, brambila2021controlofcell pages 30-33, brambila2021controlofcell pages 33-36) | High for core size/Start phenotypes; moderate for Whi5-independent and post-transcriptional mechanisms. |
| Applications | CLN3 is used as an experimental control point for studying cell-size homeostasis, commitment, transcription–cell-cycle coupling, cyclin–CDK specificity, nutrient signaling, and quantitative network robustness. Stabilized, inducible, deletion, and degron alleles permit controlled advancement or delay of Start. | Real implementations include GAL1 induction, auxin-inducible depletion, cyclin–Cdk1 fusions, promoter tethering, phosphoproteomics, and single-cell time-lapse experiments; one mitotic study analyzed n=29 cells per GAL1-CLN3 genotype and n=49 versus 45 for control versus cln3-AID. (koivomagi2021localizedphosphorylationof pages 3-5, brambila2021controlofcell pages 39-42, brambila2021controlofcell pages 33-36) | High as a research-tool application. There is no established clinical application; conclusions from engineered overexpression or stabilized alleles may not represent endogenous low-abundance Cln3 behavior. |
Table: Evidence-weighted functional annotation of S. cerevisiae S288c Cln3/P13365, separating established roles from disputed substrate and size-control models. Quantitative findings and preprint-level evidence are explicitly identified.
The target matches the requested protein on all critical dimensions:
Structure–function mutagenesis localized the principal cyclin-box-like region to approximately amino acids 99–210. Linker insertions in predicted helices 1, 2, 3, and 5 abolished Cln3 function, and mutations in the cyclin box or a second C-terminal functional region impaired Cdc28 association despite increased protein accumulation. Mutating the conserved hydrophobic patch also impaired function without necessarily eliminating co-immunoprecipitation, indicating that physical association alone is insufficient for productive cyclin-CDK signaling. Miller et al., October 2005, Yeast, DOI: https://doi.org/10.1002/yea.1292. (miller2005identificationofnovel pages 1-2)
These results provide experimental support for the supplied InterPro annotations—Cyclin, Cyclin-like domain/superfamily, Cyclin N-terminal domain, and cyclin box—rather than merely inferring function from sequence.
Cln3 promotes Start through Cdc28/Cdk1 kinase activity. Classical immunoprecipitation and genetic studies detected Cdc28 in association with Cln3 and showed that early expression of CLN3 advances Start. More recent engineered Cln3–Cdk1 fusion experiments found that an active kinase fusion could rescue cln3Δ phenotypes, whereas a kinase-dead version could not support proliferation, strongly indicating that Cln3's biological effect requires Cdk1 catalysis. Tyers et al., May 1993, EMBO Journal, DOI: https://doi.org/10.1002/j.1460-2075.1993.tb05845.x; Kõivomägi et al., posted March 25, 2021, bioRxiv, DOI: https://doi.org/10.1101/2021.03.25.436872. (tyers1993comparisonofthe pages 1-2, koivomagi2021localizedphosphorylationof pages 3-5)
There is nevertheless an important biochemical qualification. Endogenous Cln3 is exceptionally scarce and has much weaker associated kinase activity than Cln1 or Cln2. Some later experiments failed to recover a stable stoichiometric Cln3–Cdk1 complex, detected only weak Cdk1 binding, or could not demonstrate convincing broad Cln3-dependent Cdk phosphorylation. Thus, Cdk1-dependent Cln3 function is strongly established genetically, but the abundance, stability, and biochemical configuration of the endogenous complex remain less secure than for conventional abundant cyclin-CDK complexes. (brambila2021controlofcell pages 23-30, brambila2021controlofcell pages 42-48)
Because Cln3 is a cyclin, “substrate specificity” refers to substrates selected by the Cln3–Cdc28 kinase complex rather than catalysis by Cln3 alone.
In the canonical model, Cln3–Cdc28 phosphorylates Whi5, an SBF-associated transcriptional inhibitor. Whi5 inhibition or removal permits SBF-dependent expression of late-G1 genes, including CLN1 and CLN2. Genetic and older in-vitro evidence supports a relationship among Cln3, Whi5, and SBF. However, Cln3-dependent Whi5 phosphorylation has not been consistently detected; several biochemical and phosphoproteomic experiments failed to recover Whi5 as a convincing direct Cln3 substrate. CLN3 overexpression can also further reduce the size of whi5Δ cells, indicating that at least part of Cln3 function is Whi5-independent. (brambila2021controlofcell pages 23-30, brambila2021controlofcell pages 19-23, brambila2021controlofcell pages 42-48)
A 2021 study proposed that the more direct Cln3–Cdk1 substrate is the C-terminal domain of Rpb1, the largest RNA polymerase II subunit. Among more than 20 candidate Cdk substrates, Rpb1 was the most selectively phosphorylated by Cln3–Cdk1 in vitro, with phosphorylation requiring Ser5 in model heptad repeats and depending on the surrounding CTD sequence. In vivo, inhibition of the canonical CTD Ser5 kinase Kin28 reduced CTD-Ser5 phosphorylation by 60±3%, while deletion of CLN3 caused a further 15±5% reduction during G1. Artificially recruiting the Ccl1–Kin28 Ser5 kinase to SBF rescued cln3Δ size and cell-cycle phenotypes in a kinase-dependent manner. (koivomagi2021localizedphosphorylationof pages 3-5)
This is a coherent mechanism: promoter-bound Cln3–Cdk1 would locally phosphorylate RNA polymerase II at SBF-regulated promoters, stimulating transcription without requiring Whi5 to be its principal direct substrate. However, the retrieved source is a bioRxiv preprint, so Rpb1 CTD Ser5 should be regarded as a strong mechanistic candidate rather than a universally settled annotation.
Cln3 acts near the top of the budding-yeast Start network. Inducing CLN3 early in G1 accelerates Start and induces CLN1, CLN2, HCS26, CLB5, and SWI4. SBF is composed of Swi4 and Swi6 and controls many late-G1 genes; MBF contains Mbp1 and Swi6 and controls an overlapping G1/S program. Cln1/2–Cdc28 then amplify the initial signal through positive feedback, producing the abrupt transcriptional and kinase transition associated with cell-cycle commitment. (tyers1993comparisonofthe pages 1-2, brambila2021controlofcell pages 19-23)
Cln3 is therefore best described as an upstream Start activator, whereas Cln1 and Cln2 provide much of the stronger downstream G1-CDK activity that executes budding and reinforces transcription. This explains how a low-abundance and weakly active Cln3 complex can exert a disproportionate effect on commitment. (tyers1993comparisonofthe pages 1-2, zheng2024probingcellcycle pages 26-30)
The three G1 cyclins have overlapping essential capacity: individual and some double deletions are viable, but deleting CLN1, CLN2, and CLN3 together is lethal and arrests cells in G1. By itself, cln3Δ is viable but delays Start and increases cell size. Stabilized or overexpressed CLN3 advances Start and produces smaller cells. (tyers1993comparisonofthe pages 1-2, brambila2021controlofcell pages 13-19)
Cln3 connects growth to division, but the exact size-sensing mechanism remains debated.
One model proposes that Cln3 remains approximately constant in concentration while cell growth dilutes Whi5, lowering inhibition until positive feedback triggers Start. Other experiments instead found that Cln3 concentration rises markedly during G1 and that this growth-dependent accumulation, rather than Whi5 dilution, is the principal trigger. A 2024 synthesis notes that Cln3 abundance is estimated to be 5–100-fold lower and its activity 2–20-fold lower than Cln1/2, illustrating why direct measurement is technically difficult. (brambila2021controlofcell pages 23-30, zheng2024probingcellcycle pages 26-30)
The most defensible current interpretation is that Cln3 abundance, Whi5 abundance/activity, promoter occupancy, and positive feedback all contribute; available evidence does not justify reducing Start to a single universal molecular “size sensor.”
Cln3's function is spatially regulated. It is reported to be associated predominantly with the endoplasmic reticulum during early G1 and to accumulate in the nucleus during late G1, consistent with its role at SBF-regulated promoters. The ER-associated RNA-binding protein Whi3 binds CLN3 mRNA and promotes efficient ER retention of newly synthesized Cln3, limiting premature nuclear accumulation. Clusters of GCAU motifs in CLN3 mRNA act as cis determinants: mutating them reduced association with Whi3. Colomina et al., October 17, 2008, Journal of Biological Chemistry, DOI: https://doi.org/10.1074/jbc.M804604200. (colomina2008whi3adevelopmental pages 1-1)
Related work links late-G1 release of ER-retained Cln3 to the Ydj1 chaperone and describes Whi3 as restricting nuclear accumulation of the G1 cyclin-CDK complex until late G1. These findings support an ER-to-nucleus control model, although the exact universality and kinetics of that trafficking mechanism are less firmly established than Cln3's nuclear Start function. Colomina et al., June 2009, Cell Cycle, DOI: https://doi.org/10.4161/cc.8.12.8740. (colomina2009whi3regulatesmorphogenesis pages 9-9)
Accordingly, the likely site of decisive Cln3 action is the nucleus, particularly Start-regulated promoters. The ER is better understood as an early-G1 site of synthesis, sequestration, or maturation rather than the site of its final transcriptional output.
Wild-type Cln3 is short-lived, with a reported half-life of roughly 10 minutes. The classic CLN3-1/whi1-1/daf1-1/cln3-Δ177 gain-of-function allele removes the final 177 residues and stabilizes the protein to a reported half-life of approximately 2 hours. Later measurements reported about a tenfold increase in protein abundance. Stabilization shortens G1 and produces abnormally small cells, demonstrating that rapid Cln3 turnover is central to proper Start timing. (brambila2021controlofcell pages 19-23, brambila2021controlofcell pages 13-19, brambila2021controlofcell pages 30-33)
The retrieved evidence supports ubiquitin/proteolysis-dependent regulation but is insufficient to assign every aspect of endogenous Cln3 turnover conclusively to a particular SCF F-box protein or to Cdc34. Such specific ligase claims should therefore remain qualified.
Quantitative immunoblotting found that Cln3 molecules per cell increased approximately tenfold during G1 in rich carbon but only 2.5-fold in poor carbon; estimated concentration rose approximately sevenfold and twofold, respectively. Poor-carbon growth reduced Cln3 levels nearly tenfold without a corresponding change in Whi5, and poor-carbon cells were estimated to contain only 10–20 Cln3 molecules per cell. (sommer2020growthdependentsignalsdrive pages 12-15, sommer2020growthdependentsignalsdrive pages 15-16)
Blocking Sec7-dependent membrane trafficking in early G1 blocked growth and Cln3 accumulation. Perturbations of TORC2, sphingolipid, and ceramide metabolism also changed Cln3 abundance: loss of Lac1/Lag1 reduced Cln3, while exogenous phytosphingosine rapidly eliminated it, followed by ceramide-synthase-dependent recovery. In contrast, inhibiting the TORC1 effector Sch9 had relatively minor effects. These observations suggest that Cln3 integrates multiple growth and membrane-biogenesis signals rather than reporting bulk translation alone. Sommer et al., October 2020 preprint associated with eLife, DOI: https://doi.org/10.1101/2020.09.30.321182. (sommer2020growthdependentsignalsdrive pages 12-15, sommer2020growthdependentsignalsdrive pages 15-16)
These quantitative findings are influential but should be read alongside conflicting measurements supporting Whi5 dilution. The very low endogenous copy number makes epitope-tagging, synchronization, carbon source, and strain background consequential experimental variables.
A targeted search prioritizing 2023–2024 found little new peer-reviewed primary work that overturns the 2020–2021 mechanistic picture. A 2024 dissertation synthesizes single-molecule and cell-cycle work and supports the view that Cln3 is unusually scarce, rapidly turned over, and associated with Start-regulated promoters, but it does not by itself settle the direct-substrate controversy. (zheng2024probingcellcycle pages 26-30)
The principal recent conceptual development remains the proposal that Cln3–Cdk1 acts more like a localized transcriptional CDK, phosphorylating Rpb1 CTD Ser5 at SBF promoters, rather than simply serving as the first kinase in a linear Cln3→Whi5 pathway. This model elegantly explains Cln3's promoter association and weak global kinase signal, but it requires further independent peer-reviewed validation. (koivomagi2021localizedphosphorylationof pages 3-5)
An evidence-weighted expert interpretation is therefore:
CLN3 is primarily a research and biotechnology model-system tool, not a clinical target. Its deletion, inducible overexpression, stabilized truncation, auxin-inducible degradation, cyclin–Cdk1 fusion, and promoter-tethering constructs are used to:
Recent implementations include GAL1-driven CLN3 induction, cln3-AID acute depletion, time-lapse microscopy, phosphoproteomics, and synthetic recruitment of Kin28 to SBF. One mitotic perturbation series analyzed 29 cells per GAL1-CLN3 genotype and 49 control versus 45 cln3-AID cells, illustrating its use in temporally controlled single-cell experiments. (koivomagi2021localizedphosphorylationof pages 3-5, brambila2021controlofcell pages 39-42)
Cln3/P13365 is a short-lived, growth-regulated G1 cyclin whose principal cellular role is to direct Cdc28/Cdk1-dependent activation of Start-specific transcription in the nucleus. It operates upstream of SBF/MBF-associated G1/S transcription and induces CLN1/CLN2 positive feedback, thereby committing sufficiently grown yeast cells to budding and DNA replication. Early-G1 ER association and Whi3-dependent retention help regulate when Cln3 reaches its nuclear site of action. Unlike an enzyme with a single freely diffusible substrate, Cln3 confers temporal and spatial specificity on Cdc28; the leading candidate direct outputs are regulation of Whi5 and localized phosphorylation of RNA polymerase II Rpb1 CTD Ser5, with the latter currently supported by compelling but not yet definitive evidence. (tyers1993comparisonofthe pages 1-2, koivomagi2021localizedphosphorylationof pages 3-5, colomina2008whi3adevelopmental pages 1-1)
References
(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.
(brambila2021controlofcell pages 13-19): A Brambila. Control of cell growth and cell size at cell cycle entry in budding yeast. Unknown journal, 2021.
(brambila2021controlofcell pages 23-30): A Brambila. Control of cell growth and cell size at cell cycle entry in budding yeast. Unknown journal, 2021.
(koivomagi2021localizedphosphorylationof pages 3-5): Mardo Kõivomägi, Matthew P. Swaffer, Jonathan J. Turner, Georgi Marinov, and Jan M. Skotheim. Localized phosphorylation of rna polymerase ii by g1 cyclin-cdk promotes cell cycle entry. bioRxiv, Mar 2021. URL: https://doi.org/10.1101/2021.03.25.436872, doi:10.1101/2021.03.25.436872. This article has 5 citations.
(tyers1993comparisonofthe pages 1-2): M. Tyers, George, '. Tokiwa, and Bruce Futcher. Comparison of the saccharomyces cerevisiae g1 cyclins: cln3 may be an upstream activator of cln1, cln2 and other cyclins. The EMBO Journal, 12:1955-1968, May 1993. URL: https://doi.org/10.1002/j.1460-2075.1993.tb05845.x, doi:10.1002/j.1460-2075.1993.tb05845.x. This article has 645 citations.
(brambila2021controlofcell pages 42-48): A Brambila. Control of cell growth and cell size at cell cycle entry in budding yeast. Unknown journal, 2021.
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(colomina2008whi3adevelopmental pages 1-1): Neus Colomina, Francisco Ferrezuelo, Hongyin Wang, Martí Aldea, and Eloi Garí. Whi3, a developmental regulator of budding yeast, binds a large set of mrnas functionally related to the endoplasmic reticulum*♦. Journal of Biological Chemistry, 283:28670-28679, Oct 2008. URL: https://doi.org/10.1074/jbc.m804604200, doi:10.1074/jbc.m804604200. This article has 65 citations and is from a domain leading peer-reviewed journal.
(colomina2009whi3regulatesmorphogenesis pages 9-9): Neus Colomina, Francisco Ferrezuelo, Emili Vergés, Martí Aldea, and Eloi Garí. Whi3 regulates morphogenesis in budding yeast by enhancing cdk functions in apical growth. Cell Cycle, 8:1912-1920, Jun 2009. URL: https://doi.org/10.4161/cc.8.12.8740, doi:10.4161/cc.8.12.8740. This article has 18 citations and is from a peer-reviewed journal.
(brambila2021controlofcell pages 30-33): A Brambila. Control of cell growth and cell size at cell cycle entry in budding yeast. Unknown journal, 2021.
(sommer2020growthdependentsignalsdrive pages 12-15): Robert A. Sommer, Jerry T. DeWitt, Raymond Tan, and Douglas R. Kellogg. Growth-dependent signals drive an increase in early g1 cyclin concentration to link cell cycle entry with cell growth. eLife, Oct 2020. URL: https://doi.org/10.1101/2020.09.30.321182, doi:10.1101/2020.09.30.321182. This article has 1 citations and is from a domain leading peer-reviewed journal.
(sommer2020growthdependentsignalsdrive pages 15-16): Robert A. Sommer, Jerry T. DeWitt, Raymond Tan, and Douglas R. Kellogg. Growth-dependent signals drive an increase in early g1 cyclin concentration to link cell cycle entry with cell growth. eLife, Oct 2020. URL: https://doi.org/10.1101/2020.09.30.321182, doi:10.1101/2020.09.30.321182. This article has 1 citations and is from a domain leading peer-reviewed journal.
(brambila2021controlofcell pages 33-36): A Brambila. Control of cell growth and cell size at cell cycle entry in budding yeast. Unknown journal, 2021.
(brambila2021controlofcell pages 39-42): A Brambila. Control of cell growth and cell size at cell cycle entry in budding yeast. Unknown journal, 2021.
(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.