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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 Sic1, also called CDK inhibitor p40, encoded by SIC1/YLR079W in Saccharomyces cerevisiae S288c. The literature examined concerns this budding-yeast protein—not a same-symbol protein from another organism. Sic1 is a nonenzymatic, stoichiometric inhibitor of B-type cyclin–Cdk1 complexes. Its best-established primary function is to bind and inhibit Clb5/Clb6–Cdk1 (Cdc28) in late mitosis and G1, thereby maintaining low S-phase CDK activity until replication origins have been licensed and the cell is ready to enter S phase. It also contributes to suppression of mitotic Clb–Cdk1 during mitotic exit. Sic1 is then eliminated through an ordered, multisite-phosphorylation-dependent SCF–Cdc4 ubiquitin–proteasome pathway, releasing S-phase CDK activity. Thus, Sic1 is best annotated as a regulated CDK inhibitor and phosphorylation-based cell-cycle switch, not as an enzyme, transporter, or structural protein. (testa2013conformationaltransitionsof pages 26-30, testa2013…disorderedprotein pages 26-30, tripodi2009proteinkinaseck2 pages 23-28)
| Annotation aspect | Current conclusion | Key molecular details or quantitative values | Strongest evidence/method | Confidence / caveat |
|---|---|---|---|---|
| Identity and domain | This is S. cerevisiae Sic1 (UniProt P38634; YLR079W), the p40 stoichiometric inhibitor of B-type cyclin–Cdk1 complexes; the supplied SIC1_C annotation agrees with the experimentally mapped C-terminal kinase-inhibitory domain. | 284 aa; calculated mass ≈32.2 kDa; minimal inhibitory region approximately residues 215–284 (C-terminal 70 aa). | Genetic and biochemical mapping of inhibitory fragments, supported by sequence and structural analyses (testa2013conformationaltransitionsof pages 157-160, testa2013conformationaltransitionsof pages 26-30, testa2013conformationaltransitionsof pages 30-34) | High. Literature usually calls the protein Sic1/p40 rather than P38634 or YLR079W; no conflicting same-symbol protein was included. |
| Primary CDK-inhibitory function | Sic1 is a nonenzymatic, stoichiometric inhibitor that binds cyclin–Cdk1 complexes and blocks phosphorylation of other substrates, principally restraining Clb5/6–Cdk1 before S phase and contributing to inhibition of mitotic Clb–Cdk1. | Sic1–Clb5–Cdk1 inhibition has a reported subnanomolar inhibition constant; related Sic1/Cdc6 interactions with cyclin–Cdk1 complexes are described as low-nanomolar affinity. | Purified-protein kinase and binding assays, inhibitory-complex analysis, genetics, and mathematical modeling (testa2013conformationaltransitionsof pages 26-30, tripodi2009proteinkinaseck2 pages 23-28, philip2022cdc6issequentially pages 1-2) | High for Clb5/6–Cdk1 inhibition; broader cyclin specificity and exact affinities can depend on assay and phosphorylation state. |
| Intrinsically disordered architecture | Free Sic1 is predominantly intrinsically disordered but samples compact conformations and contains residual structure; its flexible N terminus acts as a phosphoregulatory platform, whereas the C-terminal inhibitory region is relatively more structured. | Approximately 9% helical structure by circular dichroism; residues 178–233 are comparatively proteolysis-resistant; greatest predicted disorder occurs in the phosphorylation-rich N-terminal half. | Disorder prediction, compositional analysis, circular dichroism, nano-ESI mass spectrometry, limited proteolysis, NMR, and molecular simulation (testa2013conformationaltransitionsof pages 30-34, testa2013…disorderedprotein pages 30-34) | High for intrinsic disorder and modularity; no single static full-length structure adequately represents the free ensemble. |
| Synthesis and localization | SIC1 is induced in late anaphase, primarily by Swi5, allowing Sic1 to accumulate during mitotic exit and G1. Its replication-control function is executed in the nuclear compartment, and reported localization can vary with nutrient/carbon conditions. | Sic1 remains stable through much of G1 and is rapidly eliminated near G1/S. | Cell-cycle expression studies, protein-level measurements, GFP imaging in nutrient-signaling studies, and functional association with nuclear cyclin–CDK and replication factors (testa2013conformationaltransitionsof pages 26-30, testa2013…disorderedprotein pages 26-30, venta2020aprocessivephosphorylation pages 12-13) | Moderate. Timing of synthesis is well established, but the gathered evidence does not define a universal transport mechanism or prove that Sic1 is exclusively nuclear. |
| Multisite phosphorylation and SCF–Cdc4 degradation | Rising G1- and S-phase CDK activity phosphorylates Sic1 through an ordered, docking-assisted network. Phosphorylated degrons engage Cdc4, leading to SCF–Cdc4/Cdc34-dependent ubiquitylation and proteasomal destruction, which releases S-phase CDK activity. | Sic1 has nine canonical N-terminal CDK sites in the classical model; phosphorylation of at least six sites was associated with degradation-competent Cdc4 binding. Multiple weak phosphodegrons exchange dynamically on the Cdc4 receptor rather than forming one rigid high-affinity interface. | Site-mutant genetics, purified kinase and ubiquitylation assays, NMR, structural analysis, quantitative western blotting, and live-cell microscopy (testa2013conformationaltransitionsof pages 26-30, testa2013conformationaltransitionsof pages 30-34, venta2020aprocessivephosphorylation pages 12-13, ravi2024modelingthestart pages 31-32) | High for phosphorylation-dependent SCF–Cdc4 degradation. The simple “six-of-nine” threshold is influential but incomplete: later work supports ordered, processive routes involving Cks1 and cyclin docking rather than indiscriminate site counting. |
| Nutrient and TORC1 regulation | TORC1 couples nutrient availability to Sic1 stability. When TORC1 is downregulated, Mpk1-dependent C-terminal phosphorylation and Greatwall–endosulfine inhibition of PP2A–Cdc55 stabilize Sic1 and favor G1 arrest. | Thr173 phosphorylation can dock Cks1; together with a C-terminal Clb5-binding motif, this can sequester Clb5–Cdk1–Cks1 and convert Sic1 from a phosphorylation target into an inhibitor. | Rapamycin/nutrient perturbation, phosphosite mutants, epistasis, protein interaction assays, and pathway-focused reviews (venta2020aprocessivephosphorylation pages 12-13, foltman2023torcomplex1 pages 20-21) | High for TORC1–Mpk1–Greatwall/PP2A control; quantitative contribution varies with nutrient state and cell-cycle context. |
| Replication-origin licensing | Sic1 prevents premature or insufficiently licensed DNA replication by suppressing Clb–Cdk1 in late mitosis and G1; its loss reduces efficient origin usage and increases genome-instability risk. | SIC1 loss is associated with firing of fewer origins and a prolonged S phase. At mitotic exit, Sic1 releases Clb2–Cdk1–Cks1 from Cdc6, enabling Mcm2–7 loading onto chromatin. | Origin-firing and genome-stability genetics, chromatin-loading assays, phosphoregulation studies, and biochemical analysis of Cdc6 complexes (testa2013…disorderedprotein pages 26-30, philip2022cdc6issequentially pages 22-23, philip2022cdc6issequentially pages 1-2) | High. Sic1 is one component of a redundant licensing-control system that also includes Cdc14, PP2A–Cdc55, Cdc6, and APC/C–Cdh1. |
| Mitotic exit | Newly synthesized Sic1 contributes to the decline of mitotic Clb–Cdk1 activity and helps establish the low-CDK state required for mitotic exit and the next G1 phase. | Sic1 acts with cyclin proteolysis, APC/C–Cdh1, Cdc14, and Cdc6-dependent mechanisms; combined SIC1 and CDC6 regulatory defects produce stronger mitotic-exit phenotypes. | Genetic interaction studies and biochemical analysis of Clb2–Cdk1–Cks1 displacement from Cdc6 (tripodi2009proteinkinaseck2 pages 23-28, philip2022cdc6issequentially pages 21-22, philip2022cdc6issequentially pages 1-2) | High as a contributory mechanism, but Sic1 alone is not the sole mitotic-exit switch because substantial redundancy exists. |
| Recent 2023–2024 developments | Recent work has mainly refined the conceptual framework rather than changed Sic1’s core annotation: nonconventional CDK sites and docking can broaden phosphorylation thresholds; TORC1 reviews integrate Sic1 with growth control; modern START models use Sic1 as a central inhibitory node. | A 2024 START model reproduced phenotypes of approximately 150 mutants, while 2023 analyses emphasized nutrient integration and docking-assisted phosphorylation beyond the minimal S/T–P consensus. | Contemporary reviews and mechanistic/computational synthesis (2023 TORC1 review; 2023 CDK-site perspective; 2024 START-BYCC modeling) (foltman2023torcomplex1 pages 20-21, ravi2024modelingthestart pages 30-31) | Moderate to high. Few 2023–2024 studies focused directly on Sic1; recent sources chiefly consolidate older primary evidence and extend systems-level interpretation. |
Table: Compact evidence map for the identity, molecular mechanism, localization, regulation, and pathway roles of budding-yeast Sic1/P38634. Confidence notes distinguish firmly established functions from context-dependent or model-based interpretations.
The supplied identity is internally consistent:
Published biochemical and structural work describes budding-yeast Sic1 as a 284-residue CDK inhibitor whose minimal kinase-inhibitory domain lies in approximately residues 215–284. This experimentally mapped C-terminal region agrees with the supplied SIC1_C domain assignments, IPR062579 and PF29958. The phosphorylation-rich N-terminal region instead controls Sic1 stability and signal processing. (testa2013conformationaltransitionsof pages 157-160, testa2013conformationaltransitionsof pages 26-30, testa2013conformationaltransitionsof pages 30-34)
The literature therefore supports the supplied identity and domain annotation. No evidence indicated that the retrieved studies concerned an unrelated SIC1 protein.
Sic1 forms inhibitory complexes with a B-type cyclin and Cdk1. Its principal physiological targets are Clb5/6–Cdk1, the S-phase CDK complexes that initiate DNA replication. Sic1 binding prevents these kinases from phosphorylating their normal substrates; consequently, Sic1 has no catalytic reaction or substrate specificity of its own. Its “specificity” is interaction specificity for cyclin–CDK complexes, mediated mainly by its C-terminal kinase-inhibitory region and cyclin-docking interactions. (testa2013conformationaltransitionsof pages 157-160, testa2013conformationaltransitionsof pages 26-30, tripodi2009proteinkinaseck2 pages 23-28)
Purified-protein and modeling work has described inhibition of Clb5–Cdk1 as subnanomolar, while related Sic1/Cdc6 interactions with cyclin–Cdk1 complexes are in the low-nanomolar range. This tight binding is biologically important because Sic1 both inhibits S-CDK and can remain associated while the bound kinase phosphorylates Sic1 intracomplex, creating a double-negative feedback mechanism: S-CDK promotes destruction of its inhibitor, which releases more active S-CDK. (venta2020aprocessivephosphorylation pages 12-13, philip2022cdc6issequentially pages 1-2)
Sic1 can also inhibit mitotic Clb–Cdk1 complexes. This broader activity contributes to establishment of the low-CDK state at mitotic exit, but it acts redundantly with APC/C-dependent cyclin destruction, Cdh1, Cdc14, and Cdc6-associated mechanisms. Sic1 is therefore an important component rather than the sole driver of mitotic exit. (tripodi2009proteinkinaseck2 pages 23-28, philip2022cdc6issequentially pages 21-22, philip2022cdc6issequentially pages 1-2)
Sic1 is a canonical intrinsically disordered protein. Sequence composition, disorder prediction, circular dichroism, nano-electrospray mass spectrometry, limited proteolysis, NMR, and molecular simulations show that free Sic1 lacks one stable, globular conformation. It nevertheless samples compact states and contains residual secondary structure; circular-dichroism estimates indicate approximately 9% helical structure. (testa2013conformationaltransitionsof pages 30-34, testa2013…disorderedprotein pages 30-34)
The protein is functionally modular:
This architecture explains how one small protein can operate as both a tight kinase inhibitor and a flexible phosphorylation sensor. The disordered region makes multiple motifs accessible to kinases, Cks1 and Cdc4, while the C terminus engages the inhibited cyclin–CDK complex.
Phosphorylated Sic1 does not engage Cdc4 through one rigid, high-affinity degron. Multiple weak phosphorylated motifs dynamically exchange on the Cdc4 substrate-binding surface. NMR and structural work supports a “dynamic polyvalency” model in which several suboptimal degrons collectively generate degradation-competent recognition. This is a major reason Sic1 has become a model for how intrinsic disorder and multisite phosphorylation produce switch-like biological decisions. (testa2013conformationaltransitionsof pages 30-34, testa2013…disorderedprotein pages 30-34)
SIC1 transcription rises in late anaphase under control principally of the transcription factor Swi5, with a lesser contribution from Ace2. Sic1 then accumulates during mitotic exit and remains stable through much of G1. Its accumulation suppresses residual mitotic CDK and prevents premature activation of S-CDK. (testa2013conformationaltransitionsof pages 26-30, testa2013…disorderedprotein pages 26-30, tripodi2009proteinkinaseck2 pages 23-28)
As G1 cyclin–Cdk1 activity rises, Cln1/2–Cdk1 phosphorylates the disordered N-terminal region of Sic1. The classical model identifies nine N-terminal CDK consensus sites, with phosphorylation of at least six producing efficient Cdc4 binding and degradation. The resulting phosphodegrons are recognized by the F-box substrate receptor Cdc4 within the SCF–Cdc4 ubiquitin ligase. Cdc34 supplies E2 activity, polyubiquitylated Sic1 is degraded by the proteasome, and Clb5/6–Cdk1 is released. (testa2013conformationaltransitionsof pages 26-30, testa2013…disorderedprotein pages 26-30, ravi2024modelingthestart pages 31-32)
The influential “six-of-nine” threshold is useful but is not the complete modern mechanism. Later biochemical studies show an ordered, processive phosphorylation circuit involving priming sites, Cks1 phospho-adaptor docking, cyclin-specific docking motifs, and competing phosphorylation routes. G1-CDK provides priming input, while emerging S-CDK can phosphorylate Sic1 within the inhibitory complex. This arrangement integrates kinase activities without prematurely releasing S-CDK toward other substrates. The 2020 study used purified kinase assays, quantitative immunoblotting, and live-cell microscopy to support this circuit. Published April 2020: https://doi.org/10.1038/s41467-020-15685-z. (venta2020aprocessivephosphorylation pages 12-13)
A 2023 perspective further argues that nonconventional CDK sites lacking the standard +1 proline can become physiologically useful when Cks1 and cyclin docking supply specificity. This recent framework suggests that analyses restricted to canonical S/T–P motifs may underestimate the functional Sic1 phosphorylation network. Published November 2023: https://doi.org/10.1091/mbc.e22-06-0196.
CK2 phosphorylates Sic1 at Ser201, within the more structured C-terminal region. This modification increases affinity for cyclin–kinase complexes and strengthens inhibition, linking cell size and growth conditions to G1/S control. Mpk1-dependent phosphorylation and stress-activated Hog1 signaling can also stabilize Sic1 in appropriate environmental contexts. (testa2013conformationaltransitionsof pages 26-30, testa2013conformationaltransitionsof pages 30-34, testa2013…disorderedprotein pages 26-30)
Sic1 delays S-CDK action until late G1. Its destruction produces a rapid rise in Clb5/6–Cdk1 activity, promoting origin firing and S-phase entry. The Sic1–S-CDK system is therefore a double-negative feedback switch: Sic1 inhibits S-CDK, but S-CDK contributes to Sic1 phosphorylation and destruction. This creates an abrupt, coordinated transition rather than a gradual, partially activated S phase. (testa2013conformationaltransitionsof pages 26-30, venta2020aprocessivephosphorylation pages 12-13)
SIC1 is not individually essential under standard laboratory conditions, reflecting regulatory redundancy. Nevertheless, sic1 loss causes firing from fewer replication origins, prolonged S phase, and increased genome-instability risk. Conversely, degradation-resistant Sic1 delays DNA replication because S-CDK remains inhibited. These reciprocal phenotypes strongly support a causal licensing-and-timing role. (testa2013…disorderedprotein pages 26-30, tripodi2009proteinkinaseck2 pages 23-28)
Sic1 also promotes origin licensing during the transition from mitosis into G1. By suppressing Clb–Cdk1, it helps permit assembly of prereplicative complexes. Foundational experiments connected Sic1 loss to deficient late-G1 origin licensing and genome instability; DOI: https://doi.org/10.1016/S1097-2765(02)00513-0. (philip2022cdc6issequentially pages 22-23)
More recent mechanistic work showed that Sic1 releases Clb2–Cdk1–Cks1 from Cdc6, allowing Mcm2–7 loading onto chromatin after mitotic exit. Sic1 functions here alongside PP2A–Cdc55 and Cdc14, which reverse different inhibitory Cdc6 phosphorylation events. Published 10 February 2022: https://doi.org/10.7554/eLife.74437. (philip2022cdc6issequentially pages 22-23, philip2022cdc6issequentially pages 1-2)
Late-anaphase Sic1 synthesis helps extinguish Clb–Cdk1 activity. Genetic interactions indicate that Sic1 and Cdc6-associated inhibition cooperate: combining SIC1 deletion with loss of the regulatory N terminus of Cdc6 produces stronger mitotic-exit defects than either perturbation alone. The expert interpretation is therefore that Sic1 reinforces a redundant low-CDK network, rather than acting as a single master off-switch. (philip2022cdc6issequentially pages 21-22, philip2022cdc6issequentially pages 1-2)
TORC1 connects nutrient availability to Sic1 stability. Under nutrient-rich conditions, TORC1 promotes G1/S progression by favoring G1 cyclin expression and Sic1 destabilization. Following TORC1 inhibition by rapamycin or nutrient limitation, Mpk1-dependent C-terminal phosphorylation and Greatwall-kinase/endosulfine-mediated inhibition of PP2A–Cdc55 stabilize Sic1, promoting G1 arrest. (venta2020aprocessivephosphorylation pages 12-13, foltman2023torcomplex1 pages 20-21)
Thr173 phosphorylation can create a Cks1 docking site. Together with a C-terminal Clb5-binding motif, this permits Sic1 to sequester Clb5–Cdk1–Cks1 and resist the same phosphorylation cascade that would otherwise mark it for degradation—a context-dependent conversion from kinase substrate to kinase inhibitor. The 2023 TORC1 review treats this mechanism as an important molecular connection between nutrient sensing, growth, and chromosome-cycle entry. Published October 2023: https://doi.org/10.3390/ijms242115745. (foltman2023torcomplex1 pages 20-21)
Sic1 carries out its best-established functions in the nucleus, where it encounters Clb5/6–Cdk1 and DNA-replication licensing factors. Endogenously tagged Sic1 has been examined by GFP microscopy in nutrient-signaling studies, and carbon source has been reported to alter its subcellular distribution. Sic1 abundance and nuclear accumulation are consequently coupled to both cell-cycle phase and metabolic state. (testa2013…disorderedprotein pages 26-30, venta2020aprocessivephosphorylation pages 12-13)
The evidence does not justify annotating Sic1 as exclusively nuclear under every condition. At approximately 32 kDa it is small enough that passive nuclear-pore diffusion could contribute, and the retrieved studies do not define one universal import/export mechanism. The defensible annotation is therefore predominantly nuclear during the G1 and mitotic-exit functions described here, with condition-dependent nucleocytoplasmic distribution.
Few 2023–2024 studies were devoted exclusively to Sic1. Recent work has chiefly refined its interpretation within wider regulatory systems:
Noncanonical CDK signaling (2023). A mechanistic perspective emphasizes that Cks1 and cyclin docking permit phosphorylation of noncanonical sites and generate a wider range of CDK thresholds than consensus motifs alone. Sic1 is a principal example. DOI: https://doi.org/10.1091/mbc.e22-06-0196.
TORC1 integration (2023). A current review places Sic1 stabilization within the Mpk1–Greatwall–endosulfine–PP2A–Cdc55 pathway, consolidating its role as the molecular interface between nutrient availability and Start. DOI: https://doi.org/10.3390/ijms242115745. (foltman2023torcomplex1 pages 20-21)
START-BYCC modeling (published 2 August 2024). A detailed budding-yeast Start model incorporates Sic1 as a central inhibitory node and reproduces phenotypes for approximately 150 mutant backgrounds, including nutritional and spatial regulation. This is a systems-level validation and hypothesis-generation tool, not new direct biochemical proof of Sic1 interactions. DOI: https://doi.org/10.1371/journal.pcbi.1012048. (ravi2024modelingthestart pages 30-31)
Current IDP interpretation (2024). Contemporary IDP research treats Sic1–Cdc4 as a paradigm for a dynamic, phosphorylation-dependent interaction in which an ensemble of motifs, rather than one folded interface, generates selective recognition. This reinforces rather than overturns the NMR-derived dynamic-polyvalency model.
Sic1 has no direct clinical or industrial application comparable with a therapeutic target or production enzyme. Its important implementations are experimental and computational:
These applications are scientifically mature, but proposals to use Sic1 circuitry as a synthetic switch or as a direct guide to human CKI therapeutics remain translational analogies rather than established implementations.
The strongest conclusions are supported by convergent genetics, purified-protein biochemistry, cell-cycle synchronization, protein stability assays, phosphosite mutants, microscopy, origin-licensing assays, NMR, and structural analysis. These establish that Sic1 is a C-terminally mediated Clb–Cdk1 inhibitor whose phosphorylation-rich disordered region controls SCF–Cdc4-dependent degradation. (testa2013conformationaltransitionsof pages 26-30, testa2013conformationaltransitionsof pages 30-34, testa2013…disorderedprotein pages 26-30)
Three qualifications are important:
SIC1 encodes a predominantly nuclear, intrinsically disordered, stoichiometric inhibitor of B-type cyclin–Cdk1 complexes. Its C-terminal SIC1_C region binds and inhibits principally Clb5/6–Cdk1, while its disordered N-terminal region integrates G1-CDK, S-CDK, Cks1, stress-kinase, and nutrient-dependent phosphorylation inputs. Multisite phosphorylation enables SCF–Cdc4/Cdc34-mediated ubiquitylation and proteasomal destruction at G1/S, releasing S-CDK to initiate DNA replication. Sic1 also reinforces mitotic CDK inactivation and promotes replication-origin licensing during mitotic exit and G1.
References
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(testa2013conformationaltransitionsof pages 30-34): L Testa. Conformational transitions of the intrinsically disordered protein sic1 from the yeast saccharomyces cerevisiae. towards structural and functional characterization of …. Unknown journal, 2013.
(philip2022cdc6issequentially pages 1-2): Jasmin Philip, Mihkel Örd, Andriele Silva, Shaneen Singh, John FX Diffley, Dirk Remus, Mart Loog, and Amy E Ikui. Cdc6 is sequentially regulated by pp2a-cdc55, cdc14, and sic1 for origin licensing in s. cerevisiae. eLife, Feb 2022. URL: https://doi.org/10.7554/elife.74437, doi:10.7554/elife.74437. This article has 10 citations and is from a domain leading peer-reviewed journal.
(testa2013…disorderedprotein pages 30-34): L Testa. … disordered protein sic1 from the yeast saccharomyces cerevisiae. towards structural and functional characterization of the whibitory complex with cdk1-clb5. Unknown journal, 2013.
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(philip2022cdc6issequentially pages 22-23): Jasmin Philip, Mihkel Örd, Andriele Silva, Shaneen Singh, John FX Diffley, Dirk Remus, Mart Loog, and Amy E Ikui. Cdc6 is sequentially regulated by pp2a-cdc55, cdc14, and sic1 for origin licensing in s. cerevisiae. eLife, Feb 2022. URL: https://doi.org/10.7554/elife.74437, doi:10.7554/elife.74437. This article has 10 citations and is from a domain leading peer-reviewed journal.
(philip2022cdc6issequentially pages 21-22): Jasmin Philip, Mihkel Örd, Andriele Silva, Shaneen Singh, John FX Diffley, Dirk Remus, Mart Loog, and Amy E Ikui. Cdc6 is sequentially regulated by pp2a-cdc55, cdc14, and sic1 for origin licensing in s. cerevisiae. eLife, Feb 2022. URL: https://doi.org/10.7554/elife.74437, doi:10.7554/elife.74437. This article has 10 citations and is from a domain leading peer-reviewed journal.
(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.