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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target is unambiguously human cyclin-dependent kinase 4 (CDK4; UniProt P11802), not a similarly named protein. The supplied identity, organism, enzyme class, and domain annotations agree with the literature: CDK4 is a CMGC-family, cyclin-dependent, proline-directed serine/threonine kinase whose principal physiological role is to connect mitogenic signaling to the G1-to-S cell-cycle transition. Its best-established catalytic substrates are the nuclear retinoblastoma-family pocket proteins RB1/pRb, RBL1/p107, and RBL2/p130. Their phosphorylation reduces repression of E2F-dependent transcription, enabling expression of genes required for DNA synthesis and cell-cycle commitment. (takaki2009thestructureof pages 1-1, sheppard2013thecellcycleregulator pages 1-3)
| Category | Evidence-based annotation | Confidence/caveat |
|---|---|---|
| Identity / organism | Human CDK4 (cyclin-dependent kinase 4), corresponding to UniProt P11802; the literature consistently describes the same D-cyclin-dependent cell-cycle kinase. (takaki2009thestructureof pages 1-1, sheppard2013thecellcycleregulator pages 1-3) | High. No conflicting similarly named protein or organism was identified. |
| Enzyme class and reaction | Cyclin-dependent, proline-directed Ser/Thr protein kinase (EC 2.7.11.22): ATP + protein-OH → ADP + phosphoprotein. Catalytic competence depends on regulatory complex formation rather than CDK4 abundance alone. (takaki2009thestructureof pages 1-1) | High for kinase class and phosphotransfer reaction. |
| Domain / family | Member of the CMGC protein-kinase superfamily, with a canonical bilobal protein-kinase domain containing ATP-binding, catalytic, and activation-loop elements. (takaki2009thestructureof pages 1-1, wood2018structuralinsightsinto pages 18-19) | High. Literature and the supplied InterPro/UniProt annotations are concordant. |
| Activating partners | Associates principally with cyclins D1, D2, and D3; mitogenic signaling raises D-cyclin availability, coupling extracellular growth signals to G1 progression. (takaki2009thestructureof pages 1-1, safaroghliazar2026cellcycletargetedcancer pages 1-2) | High. Cyclin binding is necessary but may not by itself produce the fully active conformation. |
| Inhibitors / regulators | INK4 proteins—p16^INK4A, p15^INK4B, p18^INK4C, and p19^INK4D—bind CDK4/6 and oppose cyclin activation. p21 and p27 have context-dependent roles in assembly, inhibition, nuclear targeting, and activation; phosphorylated p27 can allosterically activate cyclin-D1–CDK4. (sheppard2013thecellcycleregulator pages 1-3, guiley2019p27allostericallyactivates pages 16-17) | High, but the simple classification of p21/p27 as only inhibitors is obsolete. |
| Activation site | Phosphorylation of activation-loop Thr172 is a regulated determinant of cyclin-D–CDK4 activity; cyclin engagement exposes/repositions the T loop for activation. (takaki2009thestructureof pages 1-1, safaroghliazar2026cellcycletargetedcancer pages 1-2) | High. Structural studies show that cyclin binding plus phosphorylation can still permit inactive conformations. |
| Primary substrates and motif | Best-established physiological substrates are RB1/pRb and related pocket proteins RBL1/p107 and RBL2/p130. CDK4 is proline-directed, favoring Ser/Thr-Pro sites; substrate selection also uses cyclin-D docking interactions, including RXL-type motifs. (takaki2009thestructureof pages 1-1, safaroghliazar2026cellcycletargetedcancer pages 1-2) | High for RB-family substrates; moderate for applying a short consensus motif alone, because docking and complex context strongly affect specificity. |
| Core pathway consequence | RB-family phosphorylation weakens repression of E2F, inducing genes needed for late G1 and DNA synthesis—including E-type cyclins—and promoting passage through the G1 restriction point into S phase. (takaki2009thestructureof pages 1-1, sheppard2013thecellcycleregulator pages 1-3) | High. RB status is therefore central to biological and therapeutic response. |
| Cellular localization | The substrate-directed function is carried out predominantly in the nucleus during G1, where cyclin-D–CDK4 phosphorylates nuclear RB-family proteins. Unassembled CDK4 can also occur in cytoplasmic/chaperone-associated pools before complex assembly and nuclear accumulation. (wood2018structuralinsightsinto pages 18-19) | Moderate–high. Localization is dynamic and depends on cyclin/CKI binding, mitogenic state, and cell type. |
| Disease mechanisms | Oncogenic activation occurs through CDK4 amplification, increased D-cyclin signaling, loss of INK4 inhibition, or RB-pathway rewiring. The Arg24Cys CDK4 variant disrupts p16^INK4A-mediated inhibition and is associated with familial melanoma susceptibility. (OpenTargets Search: -CDK4, takaki2009thestructureof pages 1-1, sheppard2013thecellcycleregulator pages 1-3) | High. Most cancers activate the pathway indirectly rather than through recurrent CDK4 coding mutations. |
| Current drugs / applications | ATP-competitive palbociclib, ribociclib, and abemaciclib target CDK4/6 and are established therapies—usually with endocrine therapy—for HR-positive/HER2-negative breast cancer. Trilaciclib is used transiently before selected chemotherapy to protect bone-marrow cells through reversible CDK4/6 arrest. (OpenTargets Search: -CDK4, hawash2024advancesincancer pages 3-5, mizukami2025progressinclinical pages 2-3) | High clinically, but these agents generally inhibit both CDK4 and CDK6 and may have additional kinase or non-catalytic effects. |
| 2023–2024 clinical milestones | Abemaciclib’s US adjuvant indication was broadened in 2023. In monarchE, 5-year disease-free survival was 83.6% versus 79.4% with endocrine therapy alone. Ribociclib gained US adjuvant approval in September 2024 after NATALEE; 4-year invasive disease-free survival was 88.5% versus 83.6% (HR 0.715). (li2025exploringthepotential pages 6-7) | High for the cited trial outcomes; cross-trial comparisons are inappropriate because eligibility, dose, and treatment duration differed. |
| Resistance | Resistance commonly reflects loss or bypass of RB dependence, especially RB1 loss, cyclin-E–CDK2 activation, PI3K–AKT–mTOR or MAPK signaling, altered CDK4/6 regulation, and tumor-microenvironment adaptation. Biomarker-guided combinations and more selective next-generation inhibitors remain active research areas. (asciolla2025resistancemechanismsand pages 12-14, gao2025cdk46inhibitorsin pages 3-4, mizukami2025progressinclinical pages 1-2) | Moderate–high. Mechanisms are heterogeneous, frequently coexist, and no single resistance biomarker explains most clinical failures. |
Table: Concise evidence-based annotation of human CDK4 (UniProt P11802), spanning molecular function, regulation, localization, disease relevance, clinical implementation, and resistance. Caveats distinguish firmly established biology from context-dependent or evolving interpretations.
The literature uses CDK4 for cyclin-dependent kinase 4, including structural studies of human CDK4 in complexes with D-type cyclins. This matches UniProt accession P11802, the supplied protein name “cyclin-dependent kinase 4,” and the organism Homo sapiens. No evidence of symbol ambiguity or a conflicting same-symbol protein was encountered. Open Targets independently maps human CDK4/ENSG00000135446 to breast cancer, familial melanoma, and other neoplastic diseases. (OpenTargets Search: -CDK4, takaki2009thestructureof pages 1-1)
CDK4 is a member of the cyclin-dependent branch of the CMGC serine/threonine kinase superfamily. Its compact, bilobal kinase domain contains the expected ATP-binding pocket, catalytic machinery, αC helix, and activation segment/T loop. These findings align with the supplied InterPro annotations—CDK, protein-kinase domain, kinase-like fold, ATP-binding site, and serine/threonine-kinase active site. Structural comparisons also show that CDK4 has conformational features distinct from better-known CDKs such as CDK2, explaining why sequence-level family assignment does not imply identical activation behavior. (takaki2009thestructureof pages 1-1, wood2018structuralinsightsinto pages 18-19)
CDK4 is an ATP-dependent protein serine/threonine kinase (EC 2.7.11.22). Its net reaction is:
ATP + protein–Ser/Thr–OH → ADP + protein–Ser/Thr–OPO₃²⁻ + H⁺
CDK4 is described as proline-directed because preferred phosphoacceptor sites commonly contain serine or threonine followed by proline. However, a minimal Ser/Thr-Pro motif is insufficient to define physiological specificity: substrate docking through D-type cyclins, accessibility in the assembled holoenzyme, localization, and cell-cycle timing are also important. CDK4 therefore should not be annotated as a broadly promiscuous kinase on the basis of motif occurrence alone. (takaki2009thestructureof pages 1-1, safaroghliazar2026cellcycletargetedcancer pages 1-2)
The most firmly established substrates are:
Phosphorylation of these nuclear pocket proteins weakens their repression of E2F-regulated genes. E2F then induces proteins required for late G1 and S phase, including E-type cyclins, which activate CDK2 and reinforce cell-cycle commitment. CDK4 is thus best understood as an upstream, mitogen-responsive trigger in a kinase cascade rather than as the sole executor of RB hyperphosphorylation. (takaki2009thestructureof pages 1-1, sheppard2013thecellcycleregulator pages 1-3, mizukami2025progressinclinical pages 1-2)
A mechanistic nuance is that cyclin-D–CDK4 may initially produce limited or site-selective RB phosphorylation, after which cyclin-E/A–CDK2 activity completes the transition. Different experimental systems have yielded somewhat different models of RB mono- versus multisite phosphorylation; the robust functional consensus is that CDK4 activity relieves RB-family repression and facilitates E2F activation.
CDK4 principally associates with cyclins D1, D2, and D3. Growth-factor and oncogenic pathways—including RAS–MAPK and PI3K–AKT signaling—raise D-cyclin abundance and stability, thereby coupling extracellular mitogens to the cell-cycle engine. Cyclin binding helps organize the kinase active site and expose the activation segment, but structural studies show that binding alone does not guarantee a fully active kinase. (takaki2009thestructureof pages 1-1, safaroghliazar2026cellcycletargetedcancer pages 1-2)
Phosphorylation of Thr172 in the CDK4 T loop is an important regulated determinant of activity. Productive activation requires coordinated αC-helix positioning, placement of the conserved catalytic glutamate, stabilization of the phosphorylated activation loop, and displacement of the loop from the substrate-binding region. A 2.3-Å structure showed that even cyclin-bound, phosphorylated CDK4 can adopt an inactive conformation, making CDK4 activation more conformationally complex than the simple formula “cyclin binding plus T-loop phosphorylation.” (takaki2009thestructureof pages 1-1)
The INK4 proteins—p16INK4A/CDKN2A, p15INK4B/CDKN2B, p18INK4C/CDKN2C, and p19INK4D/CDKN2D—selectively inhibit CDK4/6. They bind the kinase, distort or stabilize an inactive state, and oppose productive D-cyclin assembly. Cancer-associated mutations at the CDK4–p16 interface can abolish this brake. (sheppard2013thecellcycleregulator pages 1-3, wood2018structuralinsightsinto pages 18-19)
The older description of p21 and p27 as universal CDK inhibitors is incomplete. These proteins can assist cyclin-D–CDK4 assembly and nuclear accumulation, act as reservoirs that indirectly regulate CDK2, or inhibit activity depending on abundance and phosphorylation state. Structural and biochemical work showed that tyrosine-phosphorylated p27 can remodel cyclin-D1–CDK4 into an active RB kinase. That active trimer was relatively refractory to palbociclib in the tested systems, suggesting that approved inhibitors can influence both catalytic activity and complex assembly/distribution. (guiley2019p27allostericallyactivates pages 16-17)
This model remains mechanistically important but should not be overgeneralized: other cellular studies support direct catalytic inhibition of CDK4/6 together with non-catalytic redistribution of p21. The best current interpretation is that drug action depends on the conformational and assembly state of CDK4, rather than on one uniform pool of enzyme.
CDK4’s defining substrate-directed function occurs predominantly in the nucleus during G1, where cyclin-D–CDK4 complexes phosphorylate nuclear RB-family proteins. Nuclear accumulation is coordinated with cyclin D and p21/p27 binding and therefore changes with mitogenic state and cell-cycle phase. Before assembly, CDK4 can occupy cytoplasmic, Hsp90–Cdc37 chaperone-associated pools; the chaperone system stabilizes kinase conformations before maturation into regulatory complexes. Thus, “nuclear and cytoplasmic, dynamically regulated” is more accurate than assigning CDK4 to a single permanent compartment. (wood2018structuralinsightsinto pages 18-19)
There is no evidence that P11802 is a secreted, membrane-spanning, or extracellular protein. Its catalytic pathway role is intracellular and chiefly nuclear.
The central pathway is:
Mitogen/receptor signaling → D-cyclin synthesis or stabilization → cyclin-D–CDK4 assembly and activation → RB-family phosphorylation → E2F derepression → cyclin E/CDK2 and S-phase gene expression → G1 restriction-point passage.
CDK4 is therefore a biochemical integrator of extracellular growth cues and the nuclear cell-division program. Its activity contributes to exit from quiescence, G1 progression, and the decision to commit to DNA replication. CDK6 overlaps substantially with this kinase function, which creates physiological redundancy and explains why many drugs inhibit both enzymes. (takaki2009thestructureof pages 1-1, sheppard2013thecellcycleregulator pages 1-3, mizukami2025progressinclinical pages 1-2)
The CDK4–cyclin-D structures revealed a less completely activated arrangement than canonical CDK2–cyclin complexes. Activation involves αC-helix movement, reorganization of the ATP-binding pocket, and activation-loop remodeling. More recent structural work with phosphorylated p27 demonstrated how an accessory protein can allosterically complete this remodeling. Together, these studies explain why assays using free CDK4, binary CDK4–cyclin complexes, and cellular trimeric complexes may produce different inhibitor potencies and catalytic behavior. (takaki2009thestructureof pages 1-1, guiley2019p27allostericallyactivates pages 16-17)
Substrate selection has at least three levels:
The annotation “RB-family-directed G1 kinase” is consequently more biologically informative than simply “Ser/Thr kinase.”
CDK4-pathway activation is common in cancer, but most tumors activate it indirectly rather than through recurrent CDK4 coding mutations. Mechanisms include:
The activating germline CDK4 Arg24Cys variant disrupts p16INK4A-mediated inhibition and causes inherited melanoma susceptibility. Literature and Open Targets evidence support a strong CDK4 association with familial/cutaneous melanoma and breast cancer. (OpenTargets Search: -CDK4, takaki2009thestructureof pages 1-1, sheppard2013thecellcycleregulator pages 1-3)
Crucially, tumors lacking functional RB may no longer depend on CDK4-mediated RB phosphorylation. RB loss can therefore both drive disease and confer resistance to CDK4/6 inhibition.
The principal clinical implementation is inhibition of CDK4/6 with palbociclib, ribociclib, or abemaciclib, usually combined with endocrine therapy in HR-positive/HER2-negative breast cancer. These agents are ATP-competitive inhibitors, but they are not CDK4-only drugs; their CDK4/CDK6 balance, off-target kinome profiles, pharmacokinetics, and toxicities differ. Open Targets records approval-stage evidence linking CDK4 to breast-cancer treatment. (OpenTargets Search: -CDK4, hawash2024advancesincancer pages 3-5)
In established metastatic settings, representative pivotal outcomes include:
These are cross-trial descriptive data, not evidence that one agent is superior to another.
Trilaciclib, another CDK4/6-family inhibitor, is administered before selected chemotherapy regimens to transiently arrest susceptible hematopoietic progenitors and reduce chemotherapy-induced marrow injury. This is conceptually distinct from chronic tumor-cell suppression. (hawash2024advancesincancer pages 3-5)
RB competence is mechanistically necessary for canonical cytostatic response, but no single biomarker—including CDK4 abundance, CCND1 amplification, p16 loss, or RB staining—perfectly predicts clinical benefit. Measuring pathway activity or activation-state markers may be more informative than gene copy number alone, but such assays are not yet universal standards.
The US adjuvant indication for abemaciclib was broadened in 2023, removing the earlier requirement for a high Ki-67 score in the principal high-risk cohort. Updated monarchE evidence showed 5-year disease-free survival of 83.6% with abemaciclib plus endocrine therapy versus 79.4% with endocrine therapy alone (HR 0.68, 95% CI 0.599–0.772). Continued curve separation after therapy ended suggests a sustained carry-over effect, although mature overall-survival assessment was still needed at that analysis. (li2025exploringthepotential pages 6-7)
The phase III NATALEE program broadened adjuvant CDK4/6 treatment to a larger stage II–III HR-positive/HER2-negative population, including selected node-negative patients. Four-year invasive disease-free survival was 88.5% with ribociclib plus endocrine therapy versus 83.6% with endocrine therapy alone (HR 0.715, 95% CI 0.609–0.840; p<0.001). Ribociclib received US adjuvant approval in September 2024. (li2025exploringthepotential pages 6-7)
The two adjuvant agents have distinct toxicity patterns. In comparative trial summaries, grade 3 neutropenia occurred in approximately 45% of ribociclib-treated participants versus 18.7% with abemaciclib; diarrhea was much more frequent with abemaciclib (84% any grade; 8% grade ≥3) than ribociclib (15% any grade; <1% grade ≥3). Ribociclib was also associated with liver-related events and QTc prolongation. Treatment completion was approximately 62.8% for three years of ribociclib in NATALEE and 69% for two years of abemaciclib in monarchE. Quality-of-life measures were not materially worsened in those analyses. (li2025exploringthepotential pages 11-13)
These figures illustrate why authoritative reviews emphasize individualized selection: efficacy must be balanced against duration, recurrence risk, comorbidity, monitoring requirements, and toxicity.
Resistance is heterogeneous and can be intrinsic or acquired. Recurrently implicated mechanisms include:
Expert reviews consequently view resistance not as one mutation but as convergence on renewed E2F/cell-cycle activity. Current strategies include combining CDK4/6 inhibition with next-generation endocrine agents, PI3K/AKT/mTOR-pathway inhibitors, or other cell-cycle drugs; developing CDK4-selective inhibitors; and longitudinally monitoring circulating tumor DNA. Most proposed combinations remain context-dependent, and immune-checkpoint combinations require caution because liver, pulmonary, and hematologic toxicities can be substantial. (asciolla2025resistancemechanismsand pages 12-14, li2025exploringthepotential pages 16-17, li2025exploringthepotential pages 14-16)
Recommended concise annotation: Human CDK4/P11802 is an intracellular, predominantly nuclear G1-phase serine/threonine kinase activated by D-type cyclins and regulated by Thr172 phosphorylation, INK4 proteins, and context-dependent p21/p27 interactions. It transfers phosphate from ATP primarily to proline-directed sites in RB-family pocket proteins. This reduces RB-mediated E2F repression and promotes restriction-point passage and S-phase entry. CDK4-pathway hyperactivation is oncogenic, and dual CDK4/6 inhibition is clinically established in HR-positive/HER2-negative breast cancer.
The molecular core of this annotation is supported by precise biochemical and structural studies. Localization is dynamic and more context-dependent than database labels imply. Clinical drugs generally target both CDK4 and CDK6, so therapeutic outcomes cannot be attributed exclusively to CDK4. Finally, several recent clinical statistics were retrieved from later reviews summarizing 2023–2024 trial updates; they should be interpreted alongside the underlying trial protocols and patient-selection criteria rather than compared directly across studies.
References
(takaki2009thestructureof pages 1-1): T. Takaki, A. Echalier, N. R. Brown, T. Hunt, J. A. Endicott, and M. E. M. Noble. The structure of cdk4/cyclin d3 has implications for models of cdk activation. Proceedings of the National Academy of Sciences, 106:4171-4176, Mar 2009. URL: https://doi.org/10.1073/pnas.0809674106, doi:10.1073/pnas.0809674106. This article has 158 citations and is from a highest quality peer-reviewed journal.
(sheppard2013thecellcycleregulator pages 1-3): Karen E. Sheppard and Grant A. McArthur. The cell-cycle regulator cdk4: an emerging therapeutic target in melanoma. Clinical Cancer Research, 19:5320-5328, Oct 2013. URL: https://doi.org/10.1158/1078-0432.ccr-13-0259, doi:10.1158/1078-0432.ccr-13-0259. This article has 350 citations and is from a highest quality peer-reviewed journal.
(wood2018structuralinsightsinto pages 18-19): Daniel J. Wood and Jane A. Endicott. Structural insights into the functional diversity of the cdk–cyclin family. Open Biology, Sep 2018. URL: https://doi.org/10.1098/rsob.180112, doi:10.1098/rsob.180112. This article has 337 citations and is from a peer-reviewed journal.
(safaroghliazar2026cellcycletargetedcancer pages 1-2): Ava Safaroghli-azar, Laychiluh B. Mekonnen, Jimma Lenjisa, Robert Milne, and Shudong Wang. Cell-cycle targeted cancer therapy: clinical advances, biological gaps, and the emergence of selective cdk4 inhibitors. Journal of Hematology & Oncology, Apr 2026. URL: https://doi.org/10.1186/s13045-026-01794-7, doi:10.1186/s13045-026-01794-7. This article has 3 citations and is from a domain leading peer-reviewed journal.
(guiley2019p27allostericallyactivates pages 16-17): Keelan Z. Guiley, Jack W. Stevenson, Kevin Lou, Krister J. Barkovich, Vishnu Kumarasamy, Tilini U. Wijeratne, Katharine L. Bunch, Sarvind Tripathi, Erik S. Knudsen, Agnieszka K. Witkiewicz, Kevan M. Shokat, and Seth M. Rubin. P27 allosterically activates cyclin-dependent kinase 4 and antagonizes palbociclib inhibition. Science, Dec 2019. URL: https://doi.org/10.1126/science.aaw2106, doi:10.1126/science.aaw2106. This article has 278 citations and is from a highest quality peer-reviewed journal.
(OpenTargets Search: -CDK4): Open Targets Query (-CDK4, 27 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(hawash2024advancesincancer pages 3-5): Mohammed Hawash. Advances in cancer therapy: a comprehensive review of cdk and egfr inhibitors. Oct 2024. URL: https://doi.org/10.3390/cells13191656, doi:10.3390/cells13191656. This article has 23 citations.
(mizukami2025progressinclinical pages 2-3): Takae Mizukami and Alberto J. Montero. Progress in clinical trials of cdk4/6 inhibitors. Current Breast Cancer Reports, Oct 2025. URL: https://doi.org/10.1007/s12609-025-00606-0, doi:10.1007/s12609-025-00606-0. This article has 3 citations.
(li2025exploringthepotential pages 6-7): Jianbin Li. Exploring the potential of adjuvant cdk4/6 inhibitors in hormone receptor-positive early breast cancer: a consistent approach for all. Cancers, 17:561, Feb 2025. URL: https://doi.org/10.3390/cancers17040561, doi:10.3390/cancers17040561. This article has 2 citations.
(asciolla2025resistancemechanismsand pages 12-14): James J. Asciolla, Xuewei Wu, Christos Adamopoulos, Evripidis Gavathiotis, and Poulikos I. Poulikakos. Resistance mechanisms and therapeutic strategies of cdk4 and cdk6 kinase targeting in cancer. Nature Cancer, 6:24-40, Jan 2025. URL: https://doi.org/10.1038/s43018-024-00893-z, doi:10.1038/s43018-024-00893-z. This article has 63 citations and is from a highest quality peer-reviewed journal.
(gao2025cdk46inhibitorsin pages 3-4): Tong Gao, Ying Sun, Ping Leng, Donghua Liu, Qie Guo, and Jing Li. Cdk4/6 inhibitors in breast cancer therapy: mechanisms of drug resistance and strategies for treatment. Frontiers in Pharmacology, May 2025. URL: https://doi.org/10.3389/fphar.2025.1549520, doi:10.3389/fphar.2025.1549520. This article has 24 citations.
(mizukami2025progressinclinical pages 1-2): Takae Mizukami and Alberto J. Montero. Progress in clinical trials of cdk4/6 inhibitors. Current Breast Cancer Reports, Oct 2025. URL: https://doi.org/10.1007/s12609-025-00606-0, doi:10.1007/s12609-025-00606-0. This article has 3 citations.
(li2025exploringthepotential pages 11-13): Jianbin Li. Exploring the potential of adjuvant cdk4/6 inhibitors in hormone receptor-positive early breast cancer: a consistent approach for all. Cancers, 17:561, Feb 2025. URL: https://doi.org/10.3390/cancers17040561, doi:10.3390/cancers17040561. This article has 2 citations.
(li2025exploringthepotential pages 16-17): Jianbin Li. Exploring the potential of adjuvant cdk4/6 inhibitors in hormone receptor-positive early breast cancer: a consistent approach for all. Cancers, 17:561, Feb 2025. URL: https://doi.org/10.3390/cancers17040561, doi:10.3390/cancers17040561. This article has 2 citations.
(li2025exploringthepotential pages 14-16): Jianbin Li. Exploring the potential of adjuvant cdk4/6 inhibitors in hormone receptor-positive early breast cancer: a consistent approach for all. Cancers, 17:561, Feb 2025. URL: https://doi.org/10.3390/cancers17040561, doi:10.3390/cancers17040561. This article has 2 citations.