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organism_full: Mus musculus (Mouse).
protein_family: Belongs to the cyclin family. Cyclin E subfamily.
protein_domains: Cyclin. (IPR039361); Cyclin-like_dom. (IPR013763); Cyclin-like_sf.
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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q61457
• Protein Description: RecName: Full=G1/S-specific cyclin-E1;
• Gene Information: Name=Ccne1; Synonyms=Ccne;
• Organism (full): Mus musculus (Mouse).
• Protein Family: Belongs to the cyclin family. Cyclin E subfamily.
• Key Domains: Cyclin. (IPR039361); Cyclin-like_dom. (IPR013763); Cyclin-like_sf. (IPR036915); Cyclin_C-dom. (IPR004367); Cyclin_N. (IPR006671)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Ccne1" matches the protein description above
2. Verify the organism is correct: Mus musculus (Mouse).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'Ccne1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene Ccne1 (gene ID: Ccne1, UniProt: Q61457) in mouse.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q61457
• Protein Description: RecName: Full=G1/S-specific cyclin-E1;
• Gene Information: Name=Ccne1; Synonyms=Ccne;
• Organism (full): Mus musculus (Mouse).
• Protein Family: Belongs to the cyclin family. Cyclin E subfamily.
• Key Domains: Cyclin. (IPR039361); Cyclin-like_dom. (IPR013763); Cyclin-like_sf. (IPR036915); Cyclin_C-dom. (IPR004367); Cyclin_N. (IPR006671)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Ccne1" matches the protein description above
2. Verify the organism is correct: Mus musculus (Mouse).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'Ccne1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene Ccne1 (gene ID: Ccne1, UniProt: Q61457) in mouse.

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.

Research Report: Functional Annotation of Ccne1 (Cyclin E1) in Mouse

1) Target verification (mandatory identity check)

Gene/protein: Ccne1 (Cyclin E1) in Mus musculus; UniProt Q61457 describes “G1/S-specific cyclin-E1,” a member of the cyclin family (cyclin E subfamily). The literature retrieved here consistently uses Ccne1/CCNE1 to refer to cyclin E1, a canonical G1/S cyclin that binds CDK2, and describes domain/region features characteristic of cyclins (cyclin homology domain plus N- and C-terminal regulatory regions). This matches the UniProt-provided identity, family, and domain expectations; no conflicting “Ccne1” gene meaning was encountered in the retrieved evidence. (davidge2019cul3regulatescyclin pages 1-4, caldon2010distinctandredundant pages 3-5)

2) Key concepts and current understanding (definitions and primary molecular function)

2.1 Cyclin E1 as a CDK2 regulatory subunit controlling the G1/S transition

Cyclin E1 is a regulatory subunit of CDK2; the cyclin E–CDK2 complex is a central driver of the G1/S transition and S-phase entry. (davidge2019cul3regulatescyclin pages 1-4, aziz2019ccne1overexpressioncauses pages 1-2, mishra2024targetingcellcycle pages 3-5)

Mechanistically, in mouse and mammalian systems cyclin E1–CDK2 can promote S-phase entry by phosphorylation of substrates including RB family members, thereby supporting E2F-driven transcriptional programs for DNA synthesis. (aziz2019ccne1overexpressioncauses pages 1-2, mishra2024targetingcellcycle pages 3-5)

2.2 CDK-independent roles in DNA replication licensing/origin biology

Beyond serving as a CDK2 activator, cyclin E1 is described as having CDK-independent roles in DNA replication licensing. In mouse-context literature, cyclin E associates with DNA replication origins and supports pre-replication complex (pre-RC) formation by facilitating MCM loading at origins, including via interactions with MCM proteins and Cdt1. (caldon2010distinctandredundant pages 3-5)

In an in vivo mouse-focused study, cyclin E1 was specifically described as contributing to DNA replication licensing by loading the MCM helicase onto chromatin-bound CDT1, supporting a mechanistic link between cyclin E1 and origin licensing. (aziz2019ccne1overexpressioncauses pages 1-2)

2.3 Coupling of centrosome duplication with S-phase programs

Cyclin E1 also helps coordinate the cell-division cycle by connecting DNA replication control with centrosome biology. A review synthesizing mouse genetic and mechanistic work reports cyclin E1 contains a ~20 amino-acid centrosome localization sequence (CLS) that targets cyclin E1 to centrosomes and promotes co-localization of MCM5 to centrosomes, and that cyclin E1–CDK2 phosphorylates centrosome regulators (e.g., nucleophosmin, CP110, Mps1) to promote centrosome duplication. (caldon2010distinctandredundant pages 3-5)

3) Subcellular localization and where the gene product acts

The retrieved evidence supports cyclin E1 acting in multiple intracellular compartments relevant to its functions:

• Nucleus/chromatin/replication origins: cyclin E1 is reported to associate with DNA at replication origins and to accumulate on chromatin during S phase, consistent with direct roles in replication licensing and S-phase programs. (caldon2010distinctandredundant pages 3-5)
• Centrosomes: cyclin E1 has a defined centrosome localization sequence (CLS) and participates in centrosome duplication control. (caldon2010distinctandredundant pages 3-5)

Overall, the strongest evidence in this corpus indicates cyclin E1 functions in nuclear/chromatin and centrosomal contexts rather than extracellular roles. (caldon2010distinctandredundant pages 3-5)

4) Regulation and pathways (proteostasis, ubiquitin ligases, transcriptional control)

4.1 Proteasome-dependent turnover and ubiquitin-ligase control (SCF/FBXW7 and Cul3)

Cyclin E1 protein abundance is tightly controlled by proteasomal degradation, and dysregulation is linked to oncogenesis. (caldon2010distinctandredundant pages 5-6, davidge2019cul3regulatescyclin pages 1-4)

Key regulatory axes supported in the evidence include:

• SCF–FBXW7 / Cullin-1 pathway: cyclin E1 is phosphorylated (including at sites such as T77 and T395) and recognized by SCF complexes using FBXW7 as substrate adaptor, leading to ubiquitination and degradation. (davidge2019cul3regulatescyclin pages 1-4)
• Cullin-3 (Cul3) pathway: Cul3 contributes to cyclin E degradation through a mechanism described as targeting cyclin E that is not bound to CDK2, and a study identified an N-terminal degron required for Cul3-mediated ubiquitylation; notably, this degron is absent in N-terminally truncated cyclin E forms. (davidge2019cul3regulatescyclin pages 1-4)

4.2 Low-molecular-weight / N-terminally truncated cyclin E forms

Proteolytic removal of the cyclin E N-terminus occurs in some cancers, generating low molecular weight (LMW) cyclin E variants. These truncations are associated with increased cyclin E–CDK2 activity and poor prognosis, and can evade degradation pathways (e.g., loss of the Cul3 degron when the N-terminus is missing). (davidge2019cul3regulatescyclin pages 1-4)

4.3 Transcriptional and post-transcriptional regulation

Cyclin E1 expression is controlled at mRNA level by cell-cycle transcriptional circuits. CCNE1 is an E2F target and is repressed by RB, embedding cyclin E1 in the RB–E2F restriction-point network. (caldon2010distinctandredundant pages 6-7)

Post-transcriptional regulation via microRNAs is also described; for example, CCNE1 can be targeted by miRNA families such as miR-16 family members (reviewed in the retrieved source). (caldon2010distinctandredundant pages 6-7)

5) Mouse genetics and in vivo functional evidence (high-value causal evidence)

5.1 Redundancy and essentiality with Ccne2

Mouse genetics indicate partial redundancy between cyclin E1 (Ccne1) and cyclin E2 (Ccne2). A key, repeatedly supported finding is that double loss of cyclin E1 and E2 is embryonic lethal, whereas single knockouts have substantially milder phenotypes. (caldon2010distinctandredundant pages 5-6, caldon2010distinctandredundant pages 3-5)

The mechanistic basis includes defects in endoreplication in specific polyploid lineages; the retrieved review reports trophoblast giant cells in double knockouts barely reach 8N. (caldon2010distinctandredundant pages 5-6)

5.2 Tissue-specific phenotypes: liver regeneration

Cyclin E1 and E2 show non-identical phenotypes in some tissues. For example, cyclin E1 deletion was reported to cause a slight delay in liver regeneration after partial hepatectomy, with compensatory cyclin A–CDK2 activity noted in the review synthesis. (caldon2010distinctandredundant pages 5-6)

5.3 Ccne1 overexpression causes chromosomal instability and liver tumors in mice

A major mouse in vivo demonstration of causal function comes from a doxycycline-inducible Ccne1 overexpression model. In this study, Ccne1 overexpression led to chromosome instability and liver tumor development (hepatocellular adenomas and hepatocellular carcinoma), despite high cyclin E1 levels in other tissues—supporting a liver-specific vulnerability to cyclin E1 dysregulation in that model. (aziz2019ccne1overexpressioncauses pages 1-2)

Mechanistically, cyclin E1 overexpression was associated with replication/mitotic defects and genome instability features, including incomplete DNA replication, centrosome amplification, abnormal spindle geometry, aneuploidy, and in hepatocytes polyploidization with whole-chromosome gains/losses alongside DNA damage and oxidative stress. (aziz2019ccne1overexpressioncauses pages 1-2)

6) Recent developments (prioritizing 2023–2024): new mechanisms, vulnerabilities, and translational directions

Although the gene target is mouse Ccne1, the most active 2023–2024 literature focuses on CCNE1/cyclin E1 dysregulation in cancer biology and replication stress, which is directly relevant to mechanistic interpretation of mouse models and to applications of cyclin E1 functional annotation.

6.1 2023: lncRNA-mediated stabilization of cyclin E1 (EILA → cyclin E1 → resistance)

A 2023 primary study identified a cyclin E1–interacting lncRNA (EILA) that promotes CDK4/6 inhibitor resistance by stabilizing cyclin E1 protein. Mechanistically, EILA binding to the cyclin E1 C-terminus hinders cyclin E1 interaction with FBXW7, thereby blocking ubiquitination and degradation. Functionally, EILA silencing reduced cyclin E1 protein and restored drug sensitivity in vitro and in vivo, positioning cyclin E1 proteostasis as an actionable resistance mechanism. The study also contextualizes the clinical problem by noting that >70% of patients progress within 12–36 months on standard regimens (as described in that paper’s framing). (cai2023lncrnaeilapromotes pages 1-2)

Publication details: Science Advances, Oct 2023; https://doi.org/10.1126/sciadv.adi3821. (cai2023lncrnaeilapromotes pages 1-2)

6.2 2024: CCNE1 amplification and checkpoint dependencies (CHK1 inhibitor SRA737)

A 2024 study emphasized that CCNE1 amplification is present in ~20% of high-grade serous ovarian cancers (HGSOCs) and is linked to replication stress and genomic instability, creating a vulnerability to checkpoint inhibition. The authors report activity of the CHK1 inhibitor SRA737, including in PARP inhibitor–resistant and CCNE1-amplified models, and propose CCNE1 amplification as a biomarker for CHK1 inhibitor approaches (monotherapy or in combination with PARP inhibitors). (xu2024chk1inhibitorsra737 pages 1-2)

Publication details: iScience, Jul 2024; https://doi.org/10.1016/j.isci.2024.109978. (xu2024chk1inhibitorsra737 pages 1-2)

6.3 2024: LMW cyclin E and PKMYT1 inhibitor vulnerability (RP-6306/lunresertib)

A 2024 study focused on low-molecular-weight cyclin E isoforms (LMW-E), stating that ~70% of triple-negative breast cancers express LMW-E and that this correlates with poor prognosis. The study proposes a mechanistic axis where LMW-E upregulates/stabilizes PKMYT1, increasing CDK1 phosphorylation, and shows that pharmacologic PKMYT1 inhibition with RP-6306 (lunresertib) yields LMW-E–dependent antitumor effects in xenografts and in transgenic mouse mammary tumor models. (li2024lowmolecularweight pages 1-3)

Publication details: Cancer Research, Aug 2024; https://doi.org/10.1158/0008-5472.can-23-4130. (li2024lowmolecularweight pages 1-3)

6.4 2024: PPM1D as a modifier of cyclin E1-driven replication stress

A 2024 primary study showed that PPM1D activity can exacerbate replication stress caused by cyclin E1 overexpression (e.g., faster G1→S progression, incomplete licensing, increased transcription–replication collisions and fork slowing), and that PPM1D inhibition rescued replication speed and reduced focal DNA copy-number alterations induced by CCNE1 overexpression. This reinforces a current research direction: treating CCNE1-driven genome instability via replication-stress response modulators. (martinikova2024ppm1dactivitypromotes pages 1-2)

Publication details: Molecular Oncology, Oct 2024; https://doi.org/10.1002/1878-0261.13433. (martinikova2024ppm1dactivitypromotes pages 1-2)

6.5 2024: CCNE1 amplification prevalence and clinical implications in esophagogastric cancer

A 2024 cohort analysis reported CCNE1 amplification in ~12% of esophagogastric cancers (with subtype breakdowns reported in the paper’s abstract). The paper connects CCNE1 amplification to unscheduled S-phase entry/replication stress/chromosomal instability and reports associations with co-alterations and therapeutic response patterns (e.g., HER2-targeted therapy contexts). While human-focused, such data support the rationale for using mouse Ccne1 models to investigate tumor dependencies and therapy response. (rustgi2024molecularlandscapeand pages 1-2)

Publication details: Cancer Research Communications, Jun 2024; https://doi.org/10.1158/2767-9764.crc-23-0496. (rustgi2024molecularlandscapeand pages 1-2)

7) Current applications and real-world implementations

7.1 Mouse models for mechanistic dissection of Ccne1-driven genome instability and tumorigenesis

• Inducible Ccne1 overexpression mice (doxycycline-inducible) are used to model how elevated cyclin E1 perturbs replication and mitosis and predisposes to liver tumor development. These are direct implementations of Ccne1 perturbation for functional annotation and causal inference. (aziz2019ccne1overexpressioncauses pages 1-2)

• DEN-initiated HCC with inducible deletion of Ccne1 provides an intervention model to test whether cyclin E1 is required for tumor progression; deletion reduces tumor burden, supporting therapeutic reasoning. (sonntag2021cycline1in pages 1-2)

7.2 Translational biomarker and therapeutic strategy development

Cyclin E1/CCNE1 status is increasingly used as a biomarker for selecting replication-stress or cell-cycle checkpoint interventions, including CHK1 inhibition in CCNE1-amplified ovarian cancer contexts and PKMYT1 inhibition in LMW cyclin E settings. (xu2024chk1inhibitorsra737 pages 1-2, li2024lowmolecularweight pages 1-3)

8) Expert synthesis and interpretation (authoritative analysis grounded in cited sources)

Taken together, the evidence supports the following functional annotation for mouse cyclin E1:

1. Primary function: cyclin E1 is a cell-cycle regulatory protein whose core biochemical role is to activate CDK2 to drive the G1/S transition and early S-phase events; it also contributes to replication origin licensing through CDK-independent interactions at origins that promote MCM loading. (davidge2019cul3regulatescyclin pages 1-4, caldon2010distinctandredundant pages 3-5, aziz2019ccne1overexpressioncauses pages 1-2)

2. Site of action: cyclin E1 functions primarily in the nucleus/chromatin (replication origins, S-phase chromatin association) and at centrosomes (via CLS), linking DNA replication with centrosome duplication. (caldon2010distinctandredundant pages 3-5)

3. Key pathways: cyclin E1 sits downstream of the RB–E2F transcriptional network and is controlled by ubiquitin-proteasome pathways involving SCF–FBXW7 (Cul1) and Cul3; perturbations that stabilize cyclin E1 (e.g., truncations/LMW forms or factors blocking FBXW7 binding) enhance oncogenic phenotypes and therapeutic resistance. (caldon2010distinctandredundant pages 6-7, davidge2019cul3regulatescyclin pages 1-4, cai2023lncrnaeilapromotes pages 1-2)

4. Mouse genetic evidence: Ccne1 and Ccne2 are partially redundant, with double knockout embryonic lethality (endoreplication defects) and tissue-specific single-knockout phenotypes such as altered liver regeneration. Importantly, Ccne1 overexpression in mice can be sufficient to induce chromosome instability and liver tumors, demonstrating strong causal contribution when dysregulated. (caldon2010distinctandredundant pages 5-6, aziz2019ccne1overexpressioncauses pages 1-2)

5. 2023–2024 direction of the field: contemporary research is emphasizing cyclin E1/CCNE1 as a driver of replication stress that creates therapeutic vulnerabilities (e.g., CHK1 inhibitors) and as a node of proteostasis-mediated drug resistance (e.g., lncRNA-mediated stabilization, LMW isoform biology) that can be targeted indirectly. (xu2024chk1inhibitorsra737 pages 1-2, cai2023lncrnaeilapromotes pages 1-2, martinikova2024ppm1dactivitypromotes pages 1-2, li2024lowmolecularweight pages 1-3)

Summary table

Table: This table summarizes the verified identity, molecular function, localization, regulation, mouse genetics, disease relevance, and recent 2023-2024 translational developments for mouse Ccne1/Cyclin E1. It is designed as a concise evidence map for downstream functional annotation and report writing.

Key cited sources (URLs and publication dates)

• Caldon CE & Musgrove E. “Distinct and redundant functions of cyclin E1 and cyclin E2 in development and cancer.” Cell Division Jan 2010. https://doi.org/10.1186/1747-1028-5-2 (caldon2010distinctandredundant pages 5-6, caldon2010distinctandredundant pages 3-5)
• Davidge B et al. “Cul3 regulates cyclin E1 protein abundance via a degron located within the N-terminal region of cyclin E.” Journal of Cell Science Nov 2019. https://doi.org/10.1242/jcs.233049 (davidge2019cul3regulatescyclin pages 1-4)
• Aziz K et al. “Ccne1 Overexpression Causes Chromosome Instability in Liver Cells and Liver Tumor Development in Mice.” Gastroenterology Jul 2019. https://doi.org/10.1053/j.gastro.2019.03.016 (aziz2019ccne1overexpressioncauses pages 1-2)
• Sonntag R et al. “Cyclin E1 in Murine and Human Liver Cancer: A Promising Target for Therapeutic Intervention during Tumour Progression.” Cancers Nov 2021. https://doi.org/10.3390/cancers13225680 (sonntag2021cycline1in pages 1-2)
• Cai Z et al. “LncRNA EILA promotes CDK4/6 inhibitor resistance in breast cancer by stabilizing cyclin E1 protein.” Science Advances Oct 2023. https://doi.org/10.1126/sciadv.adi3821 (cai2023lncrnaeilapromotes pages 1-2)
• Xu H et al. “CHK1 inhibitor SRA737 is active in PARP inhibitor resistant and CCNE1 amplified ovarian cancer.” iScience Jul 2024. https://doi.org/10.1016/j.isci.2024.109978 (xu2024chk1inhibitorsra737 pages 1-2)
• Rustgi N et al. “Molecular Landscape and Clinical Implication of CCNE1-amplified Esophagogastric Cancer.” Cancer Research Communications Jun 2024. https://doi.org/10.1158/2767-9764.crc-23-0496 (rustgi2024molecularlandscapeand pages 1-2)
• Li M et al. “Low Molecular Weight Cyclin E Confers a Vulnerability to PKMYT1 Inhibition in Triple-Negative Breast Cancer.” Cancer Research Aug 2024. https://doi.org/10.1158/0008-5472.can-23-4130 (li2024lowmolecularweight pages 1-3)
• Martinikova AS et al. “PPM1D activity promotes the replication stress caused by cyclin E1 overexpression.” Molecular Oncology Oct 2024. https://doi.org/10.1002/1878-0261.13433 (martinikova2024ppm1dactivitypromotes pages 1-2)
• Mishra N et al. “Targeting cell cycle regulators: A new paradigm in cancer therapeutics.” BIOCELL Jan 2024. https://doi.org/10.32604/biocell.2024.056503 (mishra2024targetingcellcycle pages 3-5)

References

1. (davidge2019cul3regulatescyclin pages 1-4): Brittney Davidge, Katia Graziella de Oliveira Rebola, Larry N. Agbor, Curt D. Sigmund, and Jeffrey D. Singer. Cul3 regulates cyclin e1 protein abundance via a degron located within the n-terminal region of cyclin e. Journal of Cell Science, Nov 2019. URL: https://doi.org/10.1242/jcs.233049, doi:10.1242/jcs.233049. This article has 21 citations and is from a domain leading peer-reviewed journal.

2. (caldon2010distinctandredundant pages 3-5): C. E. Caldon, E. Musgrove, and E. Musgrove. Distinct and redundant functions of cyclin e1 and cyclin e2 in development and cancer. Cell Division, 5:2-2, Jan 2010. URL: https://doi.org/10.1186/1747-1028-5-2, doi:10.1186/1747-1028-5-2. This article has 178 citations and is from a peer-reviewed journal.

3. (aziz2019ccne1overexpressioncauses pages 1-2): Khaled Aziz, Jazeel F. Limzerwala, Ines Sturmlechner, Erin Hurley, Cheng Zhang, Karthik B. Jeganathan, Grace Nelson, Steve Bronk, Raul O. Fierro Velasco, Erik-Jan van Deursen, Daniel R. O'Brien, Jean-Pierre A. Kocher, Sameh A. Youssef, Janine H. van Ree, Alain de Bruin, Hilda van den Bos, Diana C.J. Spierings, Floris Foijer, Bart van de Sluis, Lewis R. Roberts, Gregory J. Gores, Hu Li, and Jan M. van Deursen. Ccne1 overexpression causes chromosome instability in liver cells and liver tumor development in mice. Gastroenterology, 157 1:210-226.e12, Jul 2019. URL: https://doi.org/10.1053/j.gastro.2019.03.016, doi:10.1053/j.gastro.2019.03.016. This article has 75 citations and is from a highest quality peer-reviewed journal.

4. (mishra2024targetingcellcycle pages 3-5): NEELU MISHRA, AASTHA SONI, MANSHI KUMARI, GARIMA SINGH, SONIKA KUMARI SHARMA, and SAMARENDRA KUMAR SINGH. Targeting cell cycle regulators: a new paradigm in cancer therapeutics. BIOCELL, 48:1639-1666, Jan 2024. URL: https://doi.org/10.32604/biocell.2024.056503, doi:10.32604/biocell.2024.056503. This article has 6 citations and is from a peer-reviewed journal.

5. (caldon2010distinctandredundant pages 5-6): C. E. Caldon, E. Musgrove, and E. Musgrove. Distinct and redundant functions of cyclin e1 and cyclin e2 in development and cancer. Cell Division, 5:2-2, Jan 2010. URL: https://doi.org/10.1186/1747-1028-5-2, doi:10.1186/1747-1028-5-2. This article has 178 citations and is from a peer-reviewed journal.

6. (caldon2010distinctandredundant pages 6-7): C. E. Caldon, E. Musgrove, and E. Musgrove. Distinct and redundant functions of cyclin e1 and cyclin e2 in development and cancer. Cell Division, 5:2-2, Jan 2010. URL: https://doi.org/10.1186/1747-1028-5-2, doi:10.1186/1747-1028-5-2. This article has 178 citations and is from a peer-reviewed journal.

7. (cai2023lncrnaeilapromotes pages 1-2): Zijie Cai, Qianfeng Shi, Yudong Li, Liang Jin, Shunying Li, Lok Lam Wong, Jingru Wang, Xiaoting Jiang, Mengdi Zhu, Jinna Lin, Qi Wang, Wang Yang, Yujie Liu, Jun Zhang, Chang Gong, Herui Yao, Yandan Yao, and Qiang Liu. Lncrna eila promotes cdk4/6 inhibitor resistance in breast cancer by stabilizing cyclin e1 protein. Science Advances, Oct 2023. URL: https://doi.org/10.1126/sciadv.adi3821, doi:10.1126/sciadv.adi3821. This article has 31 citations and is from a highest quality peer-reviewed journal.

8. (xu2024chk1inhibitorsra737 pages 1-2): Haineng Xu, Sarah B. Gitto, Gwo-Yaw Ho, Sergey Medvedev, Kristy Shield-Artin, Hyoung Kim, Sally Beard, Yasuto Kinose, Xiaolei Wang, Holly E. Barker, Gayanie Ratnayake, Wei-Ting Hwang, Ryan J. Hansen, Bryan Strouse, Snezana Milutinovic, Christian Hassig, Matthew J. Wakefield, Cassandra J. Vandenberg, Clare L. Scott, and Fiona Simpkins. Chk1 inhibitor sra737 is active in parp inhibitor resistant and ccne1 amplified ovarian cancer. iScience, 27:109978, Jul 2024. URL: https://doi.org/10.1016/j.isci.2024.109978, doi:10.1016/j.isci.2024.109978. This article has 8 citations and is from a peer-reviewed journal.

9. (li2024lowmolecularweight pages 1-3): Mi Li, Amriti R. Lulla, Yan Wang, Spyros Tsavaschidis, Fuchenchu Wang, Cansu Karakas, Tuyen D.T. Nguyen, Tuyen N. Bui, Marc A. Pina, Mei-Kuang Chen, Sofia Mastoraki, Asha S. Multani, Natalie W. Fowlkes, Aysegul Sahin, C. Gary Marshall, Kelly K. Hunt, and Khandan Keyomarsi. Low molecular weight cyclin e confers a vulnerability to pkmyt1 inhibition in triple-negative breast cancer. Cancer research, 84:3864-3880, Aug 2024. URL: https://doi.org/10.1158/0008-5472.can-23-4130, doi:10.1158/0008-5472.can-23-4130. This article has 14 citations and is from a highest quality peer-reviewed journal.

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