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gene_id: CDK1
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gene_info: Name=CDK1; Synonyms=CDC2, CDC28A, CDKN1, P34CDC2;
organism_full: Homo sapiens (Human).
protein_family: Belongs to the protein kinase superfamily. CMGC Ser/Thr
protein_domains: CDK. (IPR050108); Kinase-like_dom_sf. (IPR011009); Prot_kinase_dom.
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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: P06493
• Protein Description: RecName: Full=Cyclin-dependent kinase 1; Short=CDK1; EC=2.7.11.22 {ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:30704899}; EC=2.7.11.23 {ECO:0000250|UniProtKB:P11440}; AltName: Full=Cell division control protein 2 homolog; AltName: Full=Cell division protein kinase 1; AltName: Full=p34 protein kinase;
• Gene Information: Name=CDK1; Synonyms=CDC2, CDC28A, CDKN1, P34CDC2;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the protein kinase superfamily. CMGC Ser/Thr
• Key Domains: CDK. (IPR050108); Kinase-like_dom_sf. (IPR011009); Prot_kinase_dom. (IPR000719); Protein_kinase_ATP_BS. (IPR017441); Ser/Thr_kinase_AS. (IPR008271)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CDK1" matches the protein description above
2. Verify the organism is correct: Homo sapiens (Human).
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 'CDK1' 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 CDK1 (gene ID: CDK1, UniProt: P06493) in human.

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: P06493
• Protein Description: RecName: Full=Cyclin-dependent kinase 1; Short=CDK1; EC=2.7.11.22 {ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:30704899}; EC=2.7.11.23 {ECO:0000250|UniProtKB:P11440}; AltName: Full=Cell division control protein 2 homolog; AltName: Full=Cell division protein kinase 1; AltName: Full=p34 protein kinase;
• Gene Information: Name=CDK1; Synonyms=CDC2, CDC28A, CDKN1, P34CDC2;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the protein kinase superfamily. CMGC Ser/Thr
• Key Domains: CDK. (IPR050108); Kinase-like_dom_sf. (IPR011009); Prot_kinase_dom. (IPR000719); Protein_kinase_ATP_BS. (IPR017441); Ser/Thr_kinase_AS. (IPR008271)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CDK1" matches the protein description above
2. Verify the organism is correct: Homo sapiens (Human).
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 'CDK1' 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 CDK1 (gene ID: CDK1, UniProt: P06493) in human.

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.

Plan and verification
- Verified identity: Human CDK1 (cyclin-dependent kinase 1), UniProt P06493, CMGC family serine/threonine protein kinase with canonical protein kinase domain; literature and structures confirm human CDK1 in complexes with cyclin B and CKS proteins (Brown 2015) (brown2015cdk1structuresreveal pages 1-2). Organism and family/domain assignment align with the provided UniProt context (brown2015cdk1structuresreveal pages 1-2).
- Evidence strategy: Emphasize recent peer‑reviewed reviews and structural/cell‑cycle analyses (2023–2024 emphasis where available), focusing on: enzymatic function and motifs; activation/inhibition circuitry; cyclin partners and localization; pathway context; non‑mitotic roles; and translational applications.

Human CDK1: key concepts and definitions
- Enzymatic class and essential role: CDK1 is a conserved serine/threonine protein kinase (EC 2.7.11.22/23) that is the only CDK essential for mammalian cell-cycle progression; it drives the G2→M transition and M‑phase processes (Brown 2015; Massacci 2023) (brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 1-2).
- Substrate specificity and motifs: CDK1 typically phosphorylates S/T‑P motifs. Substrate selection is refined by cyclin docking interfaces and the CKS subunit, which promotes priming/multisite phosphorylation and processivity on CDK substrates (Brown 2015; Massacci 2023) (brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 1-2).
- Activation and inhibition logic: The catalytic activation segment T161 must be phosphorylated by the CDK‑activating kinase (CAK, CDK7–cyclin H), while T14 and Y15 are inhibitory sites set by WEE1/PKMYT1 and removed by CDC25 phosphatases (CDC25A/B/C) to trigger the switch into mitosis (Lemonnier 2020; Massacci 2023; Wang 2023) (lemonnier2020theg2tomtransition pages 1-2, massacci2023thecyclindependentkinase pages 1-2, wang2023targetingcdk1in pages 1-2).
- Cyclin partners and cofactors: The principal mitotic partner is cyclin B1 (also cyclin A can bind in some contexts). CKS1/2 act as phospho‑adaptors that dock to primed sites and facilitate multi‑site substrate phosphorylation, shaping timing and ordering of mitotic events (Brown 2015; Massacci 2023) (brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 1-2).
- Localization and timing: CDK1–cyclin complexes distribute between cytoplasm and nucleus. At mitotic entry, activation is detected at centrosomes and then across nuclear/kinetochore/spindle compartments around nuclear envelope breakdown (NEBD), coordinating mitotic onset (Brown 2015; Lemonnier 2020; Massacci 2023) (brown2015cdk1structuresreveal pages 1-2, lemonnier2020theg2tomtransition pages 1-2, massacci2023thecyclindependentkinase pages 1-2).
- Pathway context: CDK1 sits within a bistable “G2/M switch” governed by PLK1 (promotes Cdc25, inhibits Wee1), and by the Greatwall–PP2A‑B55 phosphatase axis that times dephosphorylation versus phosphorylation waves. Mitotic exit proceeds as APC/C activation and phosphatase reactivation reverse CDK1‑driven phosphorylation (Lemonnier 2020; Brown 2015; Massacci 2023) (lemonnier2020theg2tomtransition pages 1-2, brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 1-2).

Recent developments and latest research (emphasis 2023–2024)
- Comprehensive 2023 synthesis of non‑mitotic roles: A 2023 British Journal of Cancer review catalogues CDK1’s roles beyond mitosis—transcriptional control, mitochondrial metabolism (e.g., Drp1 fission; Complex I and SIRT3 regulation), apoptosis (caspase-9, Bcl‑2 family, survivin), Golgi remodeling, endocytosis and nucleocytoplasmic transport—expanding the “CDK1 substratome” and cancer‑relevance of these functions (Massacci 2023) (massacci2023thecyclindependentkinase pages 3-4, massacci2023thecyclindependentkinase pages 1-2, massacci2023thecyclindependentkinase pages 7-9).
- Structural basis and selectivity levers: Human CDK1–cyclin B–CKS complexes reveal differences versus CDK2 that affect stability, activation‑segment control and substrate sequence preferences; such differences are potential avenues for CDK1‑selective inhibitor design (Brown 2015) (brown2015cdk1structuresreveal pages 1-2).
- Phosphatase‑centric view of the mitotic switch: Recent conceptual advances synthesize how Greatwall–PP2A‑B55, Cdc25 and Wee1/Myt1 orchestrate the irreversible G2→M transition and timing through sequential dephosphorylations—highlighting phosphatases as equally central as kinases for mitotic control (Lemonnier 2020) (lemonnier2020theg2tomtransition pages 1-2).
- Oncogenic regulation via Tyr15 and resistance: Phosphoproteomic and signaling analyses link CDK1 Tyr15 phosphorylation to drug resistance circuitry (e.g., ERBB2/SRC/BRK) and show cancer‑type–specific activation states; CDK1 is transcriptionally/proteomically upregulated across many tumors (Massacci 2023) (massacci2023thecyclindependentkinase pages 7-9).

Current applications and real‑world implementations
- Therapeutic positioning and inhibitors: CDK1 is widely overexpressed in tumors and is a prioritized target; however, first‑generation pan‑CDK inhibitors suffered from toxicity. Newer strategies include more selective CDK1 tool compounds (e.g., RO‑3306), combination regimens, and targeting upstream gatekeepers (WEE1/PKMYT1) to modulate the CDK1 switch and radiosensitize or chemosensitize tumors (Wang 2023; Massacci 2023) (wang2023targetingcdk1in pages 1-2, massacci2023thecyclindependentkinase pages 9-9).
- Biomarker and resistance context: Analyses across The Cancer Genome Atlas show CDK1 expression elevation in roughly 71% (17/24) of cancer types examined, consistent with proliferative state and poor outcomes; inhibitory Y15 phosphorylation circuitry can contribute to resistance to taxanes and kinase inhibitors, suggesting actionable biomarkers and combination partners (Wang 2023; Massacci 2023) (wang2023targetingcdk1in pages 1-2, massacci2023thecyclindependentkinase pages 7-9).

Expert opinions and analysis from authoritative sources
- Brown 2015 (Nature Communications): CDK1 is uniquely essential; structures of CDK1 with cyclin B and CKS define conserved activation principles and unique features differentiating it from CDK2, with implications for substrate recognition and inhibitor selectivity (brown2015cdk1structuresreveal pages 1-2).
- Lemonnier 2020 (Cell Division): Emphasizes phosphatase control (PP2A‑B55, Cdc25) as the counterweight to kinase networks in G2→M, explaining robustness and irreversibility of mitotic entry (lemonnier2020theg2tomtransition pages 1-2).
- Massacci 2023 (British Journal of Cancer): Integrates curated substrates and upstream regulators, argues for broad non‑mitotic functions of CDK1 in cancer biology, and frames therapeutic opportunities and open questions (massacci2023thecyclindependentkinase pages 1-2, massacci2023thecyclindependentkinase pages 3-4, massacci2023thecyclindependentkinase pages 6-7, massacci2023thecyclindependentkinase pages 7-9).
- Wang 2023 (NPJ Precision Oncology): Reviews targeting CDK1 in cancer, summarizing regulatory mechanisms, expression patterns across cancers, and development status of direct and indirect (checkpoint‑level) inhibitors (wang2023targetingcdk1in pages 1-2).

Relevant statistics and data from recent studies
- Tumor overexpression prevalence: Across large cancer datasets, CDK1 expression is elevated in about 70.8% (17/24) of cancer types, reinforcing its translational relevance as a target and biomarker (Wang 2023) (wang2023targetingcdk1in pages 1-2).
- Substrate landscape: Contemporary curation collates many direct human CDK1 substrates across mitotic and non‑mitotic processes, with site‑ and outcome‑level annotations (activation vs inhibition), providing a reference “substratome” for hypothesis generation (Massacci 2023) (massacci2023thecyclindependentkinase pages 6-7).
- Resistance circuitry: Cancer‑type–specific modulation of CDK1 activation state (e.g., Tyr15) correlates with drug resistance mechanisms, including ERBB2/SRC/BRK signaling, informing combination therapy design (Massacci 2023) (massacci2023thecyclindependentkinase pages 7-9).

Key substrates and cellular localizations (selected examples)
- Mitotic machinery and cytoskeleton: CDK1 phosphorylates numerous spindle, kinetochore, and microtubule‑associated proteins (e.g., KIF11/EG5, BUB1B, MAP4, intermediate filaments such as vimentin and lamin A), coordinating chromosome segregation and cell morphology changes; localization includes centrosomes, nucleus, kinetochores and spindle during M‑phase (Brown 2015; Massacci 2023) (brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 6-7).
- Transcription, metabolism and organelles: Curated substrates include regulators of transcription/translation and mitochondrial and Golgi proteins (e.g., Drp1/mitochondrial fission; GRASP65/GM130 for Golgi remodeling), highlighting non‑mitotic localization and functions (Massacci 2023) (massacci2023thecyclindependentkinase pages 3-4, massacci2023thecyclindependentkinase pages 7-9).

Embedded summary artifact
| Section | Topic / Area | Key facts / 2023–24 highlight | Primary sources (label, year) |
|---|---|---|---|
| Core biology | Enzymatic class (EC) | Ser/Thr protein kinase (CDK family). Catalytic activity annotated as EC 2.7.11.22/23 and essential for M-phase progression. | Brown 2015; Massacci 2023 (brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 1-2) |
| Core biology | Consensus motifs & docking | Prefers S/T-P motifs; substrate specificity enhanced by cyclin docking sites and CKS-mediated priming/multisite phosphorylation. | Brown 2015; Massacci 2023 (brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 1-2) |
| Core biology | Activation / inhibition sites & regulators | Activating phosphorylation: Thr161 by CAK (CDK7–cyclin H). Inhibitory phosphorylations: Thr14 and Tyr15 by WEE1/PKMYT1; removed by CDC25 phosphatases to activate CDK1. | Lemonnier 2020; Massacci 2023; Wang 2023 (lemonnier2020theg2tomtransition pages 1-2, massacci2023thecyclindependentkinase pages 1-2, wang2023targetingcdk1in pages 1-2) |
| Core biology | Cyclin partners & CKS roles | Principal mitotic partner: cyclin B1; cyclin A can also pair. CKS1/2 act as phospho-adaptors to promote multisite phosphorylation and substrate recruitment. | Brown 2015; Massacci 2023 (brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 1-2) |
| Core biology | Localization dynamics & timing | CDK1–cyclin complexes traffic between nucleus and cytoplasm; activity/local activation detected at centrosomes, then nucleus/kinetochores and spindle during G2→M and around NEBD. | Brown 2015; Lemonnier 2020; Massacci 2023 (brown2015cdk1structuresreveal pages 1-2, lemonnier2020theg2tomtransition pages 1-2, massacci2023thecyclindependentkinase pages 1-2) |
| Core biology | Pathway context (mitotic switch & exit) | Interacts with PLK1-driven activation cascade, Greatwall–PP2A‑B55 controls substrate dephosphorylation timing, and APC/C–separase axis effects mitotic exit downstream of CDK1 inactivation. | Lemonnier 2020; Brown 2015; Massacci 2023 (lemonnier2020theg2tomtransition pages 1-2, brown2015cdk1structuresreveal pages 1-2, massacci2023thecyclindependentkinase pages 1-2) |
| Updates & applications | Non-mitotic roles (2023 review) | 2023 synthesis highlights CDK1 roles in transcription, metabolism, mitochondrial dynamics and apoptosis beyond classical cell-cycle control. | Massacci 2023 (massacci2023thecyclindependentkinase pages 1-2) |
| Updates & applications | Therapeutic targeting (oncology) | 2023 NPJ review positions CDK1 as a cancer-relevant target; many tumors show CDK1 upregulation and strategies include direct inhibitors or targeting upstream regulators (e.g., WEE1). | Wang 2023; Massacci 2023 (wang2023targetingcdk1in pages 1-2, massacci2023thecyclindependentkinase pages 1-2) |
| Updates & applications | Structural insights (implications for inhibitors) | High-resolution CDK1–cyclin/CKS structures reveal conserved and unique features that could enable selective inhibitor design and explain substrate specificity. | Brown 2015 (brown2015cdk1structuresreveal pages 1-2) |
| Updates & applications | Phosphatase & timing advances | Reviews emphasize the Greatwall–PP2A‑B55 and Cdc25/WEE1 circuits as the molecular switch controlling irreversible G2→M transition, informing targets like WEE1. | Lemonnier 2020; Massacci 2023 (lemonnier2020theg2tomtransition pages 1-2, massacci2023thecyclindependentkinase pages 1-2) |
| Updates & applications | Substrate maps & phosphoproteomics | 2023 curation compiles an extensive CDK1 substratome (many residues/sites); quantitative maps aid prioritizing functional substrates in mitosis and disease. | Massacci 2023 (massacci2023thecyclindependentkinase pages 6-7, massacci2023thecyclindependentkinase pages 7-9) |
| Updates & applications | Inhibitor landscape & strategies | Historic pan‑CDK inhibitors had toxicity; selective tools (e.g., RO‑3306) and approaches targeting upstream kinases (WEE1/PKMYT1) or combination regimens are current translational focuses. | Massacci 2023; Wang 2023 (massacci2023thecyclindependentkinase pages 9-9, wang2023targetingcdk1in pages 1-2) |
| Updates & applications | Emerging extramitotic roles & metabolism | Emerging evidence (reviewed 2023) links basal/extramitotic CDK1 activity to metabolic and signalling regulation, suggesting contexts beyond dividing cells for therapeutic consideration. | Massacci 2023; Wang 2023 (massacci2023thecyclindependentkinase pages 1-2, wang2023targetingcdk1in pages 1-2) |

Table: A concise two‑section table summarizing core biology of human CDK1 (P06493) and key 2023–2024 advances/applications, with primary source labels and context citations for each item.

Conclusions
Human CDK1 (P06493) is the essential mitotic CDK that integrates cyclin docking, CKS‑facilitated multisite phosphorylation, and phosphoregulation at T161/T14/Y15 to control the abrupt, robust G2→M transition. Recent work emphasizes the equal importance of phosphatase networks (Greatwall–PP2A‑B55), and expands CDK1 biology beyond mitosis to transcription, metabolism, membrane trafficking, and apoptosis. In oncology, CDK1 is frequently upregulated and functionally implicated in resistance circuitry; translational strategies include direct inhibition and modulation of upstream checkpoint kinases (e.g., WEE1), often in rational combinations. Structural distinctions from CDK2 and curated, site‑resolved substrate maps now provide concrete levers for designing selective inhibitors and for prioritizing actionable substrates in disease contexts (brown2015cdk1structuresreveal pages 1-2, lemonnier2020theg2tomtransition pages 1-2, massacci2023thecyclindependentkinase pages 1-2, wang2023targetingcdk1in pages 1-2).

Source URLs and publication dates
- Brown NR et al. CDK1 structures reveal conserved and unique features. Nature Communications. 2015-04-23. URL: https://doi.org/10.1038/ncomms7769 (brown2015cdk1structuresreveal pages 1-2)
- Lemonnier T et al. The G2-to-M transition from a phosphatase perspective. Cell Division. 2020-05-27. URL: https://doi.org/10.1186/s13008-020-00065-2 (lemonnier2020theg2tomtransition pages 1-2)
- Massacci G et al. The Cyclin-dependent kinase 1: more than a cell cycle regulator. Br J Cancer. 2023-10-30. URL: https://doi.org/10.1038/s41416-023-02468-8 (massacci2023thecyclindependentkinase pages 1-2, massacci2023thecyclindependentkinase pages 3-4, massacci2023thecyclindependentkinase pages 6-7, massacci2023thecyclindependentkinase pages 7-9)
- Wang Q et al. Targeting CDK1 in cancer: mechanisms and implications. NPJ Precision Oncology. 2023-06-02. URL: https://doi.org/10.1038/s41698-023-00407-7 (wang2023targetingcdk1in pages 1-2)

References

1. (brown2015cdk1structuresreveal pages 1-2): Nicholas R. Brown, Svitlana Korolchuk, Mathew P. Martin, Will A. Stanley, Rouslan Moukhametzianov, Martin E. M. Noble, and Jane A. Endicott. Cdk1 structures reveal conserved and unique features of the essential cell cycle cdk. Nature Communications, Apr 2015. URL: https://doi.org/10.1038/ncomms7769, doi:10.1038/ncomms7769. This article has 244 citations and is from a highest quality peer-reviewed journal.

2. (massacci2023thecyclindependentkinase pages 1-2): Giorgia Massacci, Livia Perfetto, and Francesca Sacco. The cyclin-dependent kinase 1: more than a cell cycle regulator. British Journal of Cancer, 129:1707-1716, Oct 2023. URL: https://doi.org/10.1038/s41416-023-02468-8, doi:10.1038/s41416-023-02468-8. This article has 108 citations and is from a domain leading peer-reviewed journal.

3. (lemonnier2020theg2tomtransition pages 1-2): Tom Lemonnier, Aude Dupré, and Catherine Jessus. The g2-to-m transition from a phosphatase perspective: a new vision of the meiotic division. Cell Division, May 2020. URL: https://doi.org/10.1186/s13008-020-00065-2, doi:10.1186/s13008-020-00065-2. This article has 40 citations and is from a peer-reviewed journal.

4. (wang2023targetingcdk1in pages 1-2): Qiushi Wang, Ann M. Bode, and Tianshun Zhang. Targeting cdk1 in cancer: mechanisms and implications. NPJ Precision Oncology, Jun 2023. URL: https://doi.org/10.1038/s41698-023-00407-7, doi:10.1038/s41698-023-00407-7. This article has 164 citations and is from a peer-reviewed journal.

5. (massacci2023thecyclindependentkinase pages 3-4): Giorgia Massacci, Livia Perfetto, and Francesca Sacco. The cyclin-dependent kinase 1: more than a cell cycle regulator. British Journal of Cancer, 129:1707-1716, Oct 2023. URL: https://doi.org/10.1038/s41416-023-02468-8, doi:10.1038/s41416-023-02468-8. This article has 108 citations and is from a domain leading peer-reviewed journal.

6. (massacci2023thecyclindependentkinase pages 7-9): Giorgia Massacci, Livia Perfetto, and Francesca Sacco. The cyclin-dependent kinase 1: more than a cell cycle regulator. British Journal of Cancer, 129:1707-1716, Oct 2023. URL: https://doi.org/10.1038/s41416-023-02468-8, doi:10.1038/s41416-023-02468-8. This article has 108 citations and is from a domain leading peer-reviewed journal.

7. (massacci2023thecyclindependentkinase pages 9-9): Giorgia Massacci, Livia Perfetto, and Francesca Sacco. The cyclin-dependent kinase 1: more than a cell cycle regulator. British Journal of Cancer, 129:1707-1716, Oct 2023. URL: https://doi.org/10.1038/s41416-023-02468-8, doi:10.1038/s41416-023-02468-8. This article has 108 citations and is from a domain leading peer-reviewed journal.

8. (massacci2023thecyclindependentkinase pages 6-7): Giorgia Massacci, Livia Perfetto, and Francesca Sacco. The cyclin-dependent kinase 1: more than a cell cycle regulator. British Journal of Cancer, 129:1707-1716, Oct 2023. URL: https://doi.org/10.1038/s41416-023-02468-8, doi:10.1038/s41416-023-02468-8. This article has 108 citations and is from a domain leading peer-reviewed journal.

Citations

1. massacci2023thecyclindependentkinase pages 7-9
2. massacci2023thecyclindependentkinase pages 6-7
3. massacci2023thecyclindependentkinase pages 1-2
4. massacci2023thecyclindependentkinase pages 3-4
5. massacci2023thecyclindependentkinase pages 9-9
6. https://doi.org/10.1038/ncomms7769
7. https://doi.org/10.1186/s13008-020-00065-2
8. https://doi.org/10.1038/s41416-023-02468-8
9. https://doi.org/10.1038/s41698-023-00407-7
10. https://doi.org/10.1038/ncomms7769,
11. https://doi.org/10.1038/s41416-023-02468-8,
12. https://doi.org/10.1186/s13008-020-00065-2,
13. https://doi.org/10.1038/s41698-023-00407-7,