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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity is verified. The requested target is unambiguously human CDKN1B, encoding cyclin-dependent kinase inhibitor 1B (p27Kip1/p27), corresponding to the supplied UniProt accession P46527. Literature describes a 198-amino-acid Cip/Kip-family cyclin-dependent kinase regulator and clearly distinguishes it from CDKN1A/p21Cip1 and CDKN1C/p57Kip2. The reported N-terminal kinase-inhibitory region is concordant with the supplied CDI domain annotations (InterPro IPR003175/IPR044898; Pfam PF02234). No conflicting gene, organism, or similarly named protein was found. (cusan2018landscapeofcdkn1b pages 1-2)
CDKN1B is not an enzyme or transporter. Its primary product, p27, is a non-catalytic, intrinsically disordered regulatory protein. Its best-established function is to bind cyclin–CDK complexes in the nucleus—especially cyclin E–CDK2 and cyclin A–CDK2—and restrain RB phosphorylation and G1-to-S-phase progression. However, p27 is not a universal CDK inhibitor: in appropriate phosphorylation and stoichiometric states it also assembles, transports, and can permit or allosterically support cyclin D–CDK4/6 activity. Localization and post-translational state are therefore essential parts of its functional annotation. (wafa2014theroleof pages 46-51, bencivenga2025p27kip1andtumors pages 1-2, bencivenga2025p27kip1andtumorsa pages 25-26)
The human protein is commonly called p27Kip1 or p27 and belongs to the Cip/Kip family, together with p21 and p57. These proteins share an N-terminal cyclin/CDK-interaction region but are encoded by separate genes and have distinct regulatory programs. Human p27 is 198 residues long and is largely intrinsically disordered in isolation. Its principal N-terminal cell-cycle inhibitory region—often called the kinase inhibitory domain or KID, approximately residues 25–93—contains separable cyclin- and CDK-contacting elements. (cusan2018landscapeofcdkn1b pages 1-2)
Intrinsic disorder is functionally important rather than evidence of an incomplete structure. On binding cyclin A–CDK2, the N-terminal region undergoes coupled folding and binding into an extended conformation, while the C-terminal portion remains flexible. This conformational plasticity allows one small protein to engage cyclin–CDK complexes, trafficking factors, ubiquitin machinery, cytoskeletal proteins, and numerous modifying enzymes. It also makes p27 unusually sensitive to missense, truncating, and phosphorylation-site changes. (cusan2018landscapeofcdkn1b pages 2-4)
In quiescent cells and early G1, nuclear p27 binds the cyclin and CDK components of a complex simultaneously. Its N-terminal domain occludes or distorts the catalytic machinery, reducing CDK activity. Strongly established targets include cyclin E–CDK2 and cyclin A–CDK2. Consequently, CDK-dependent phosphorylation of retinoblastoma-family proteins is reduced, E2F-dependent transcription remains constrained, and cells remain in G0/G1 or enter S phase more slowly. p27 itself catalyzes no reaction and has no chemical substrate; its “specificity” concerns protein-complex partners rather than enzymatic substrates. (wafa2014theroleof pages 46-51, bencivenga2025p27kip1andtumors pages 1-2)
For cyclin D–CDK4/6, p27 has a more nuanced role. It can promote ternary-complex assembly in the cytoplasm and facilitate nuclear delivery. Depending on abundance, tyrosine phosphorylation, cyclin/CDK identity, and complex conformation, p27 can inhibit the complex, serve as an assembly factor, or permit/allosterically support CDK4 activity. Tyr74 phosphorylation has been linked to activation of p27-containing cyclin D–CDK4 complexes. This explains why annotating p27 simply as a broad-spectrum CDK inhibitor is incomplete and why p27 state may influence response to CDK4/6 inhibitors such as palbociclib. (bencivenga2025p27kip1andtumors pages 1-2, bencivenga2025p27kip1andtumorsa pages 25-26)
The canonical checkpoint function is performed predominantly by nuclear p27. Nuclear retention gives p27 access to cyclin E/A–CDK2 and thereby supports quiescence, differentiation, and checkpoint restraint. Cancer-associated truncations that remove or disrupt its nuclear-localization region can cause cytoplasmic retention and loss of cell-cycle inhibition. (cusan2018landscapeofcdkn1b pages 2-4)
Ser10 phosphorylation is linked to p27 stabilization and CRM1/Ran-dependent nuclear export. C-terminal phosphorylation, including Thr198 phosphorylation by p90 RSK-family kinases, promotes 14-3-3 association and cytoplasmic localization. AKT-dependent mechanisms can additionally impair nuclear import. JAB1-mediated shuttling has been mapped to a p27 interaction region around residues 97–151. Thus, cytoplasmic accumulation may reflect active trafficking rather than merely reduced expression. (bencivenga2025p27kip1andtumors pages 25-27, bencivenga2025p27kip1andtumorsa pages 29-30, cusan2018landscapeofcdkn1b pages 4-5)
A major cell-cycle-regulated route is phosphorylation of Thr187 by active cyclin E/A–CDK2, followed by recognition through Cks1 and the SCF^SKP2 ubiquitin ligase and proteasomal degradation. This creates a switch-like positive-feedback mechanism: initial CDK2 activation marks p27 for destruction, which releases further CDK2 activity. SKP2 and Cks1 overexpression in tumors can therefore lower p27 protein without requiring loss of CDKN1B mRNA or DNA. Additional proteasomal and endolysosomal routes have been reported, but Thr187–SCF^SKP2 is the central established S-phase pathway. (bencivenga2025p27kip1andtumors pages 2-4, bencivenga2025p27kip1andtumors pages 25-27)
Cytoplasmic p27 is not necessarily inactive. Its disordered C-terminus interacts with proteins including stathmin and regulators of Rho-family GTPases, thereby affecting microtubule dynamics, actin organization, migration, invasion, and cytokinesis. Other reported functions involve microtubule acetylation, autophagic-vesicle trafficking, and Ragulator–mTOR signaling during nutrient stress. These functions can be independent of CDK inhibition and, in some tumors, cytoplasmic p27 may favor motility despite loss of its nuclear tumor-suppressive effect. (bencivenga2025p27kip1andtumorsa pages 29-30, bencivenga2025p27kip1andtumors pages 24-25, bencivenga2025p27kip1andtumorsa pages 25-26, cusan2018landscapeofcdkn1b pages 2-4)
A compact pathway model is:
Mitogenic signaling → cyclin D–CDK4/6 assembly → RB phosphorylation → E2F/cyclin E induction → cyclin E–CDK2 activation → p27 Thr187 phosphorylation → SCF^SKP2/Cks1-dependent p27 destruction → reinforced CDK2 activity and S-phase entry.
Antimitogenic, differentiation, or quiescence signals generally stabilize nuclear p27, whereas PI3K–AKT, RAS–MAPK/RSK, Src-family kinases, SKP2, and related oncogenic routes can change its synthesis, phosphorylation, localization, or degradation. The decisive biological variable is therefore often p27 protein abundance and compartment, not CDKN1B transcript alone. (bencivenga2025p27kip1andtumors pages 2-4, bencivenga2025p27kip1andtumors pages 25-27, cusan2018landscapeofcdkn1b pages 2-4)
The following table separates established annotation from newer translational findings.
| Topic | Key finding | Evidence/model | Interpretation/status |
|---|---|---|---|
| Identity and structure | Human CDKN1B encodes the 198-aa p27Kip1 protein (UniProt P46527), a largely intrinsically disordered Cip/Kip-family CDK regulator. Its N-terminal kinase-inhibitory/CDI domain folds upon cyclin–CDK binding, whereas much of the C-terminus remains disordered. | Biochemical, structural, mutational, and protein-annotation evidence | Identity is unambiguous and distinct from CDKN1A/p21 and CDKN1C/p57; the supplied CDI-family/domain annotations are concordant with the literature. |
| Canonical nuclear function | Nuclear p27 binds and inhibits cyclin E–CDK2 and cyclin A–CDK2, limiting RB phosphorylation and E2F-dependent G1-to-S progression; it is a regulator, not an enzyme, and therefore catalyzes no reaction. | Direct binding and kinase assays; cell-cycle arrest studies; cyclin A–CDK2 structural analysis | Core, well-established molecular function and principal basis for tumor-suppressive activity. |
| Cyclin D–CDK4/6 role | p27 can assemble and escort cyclin D–CDK4/6 complexes to the nucleus; depending on phosphorylation and stoichiometry, it may inhibit, permit, or allosterically support CDK4 activity rather than acting as a universal inhibitor. | Ternary-complex, phosphorylation, localization, and kinase studies | Context-dependent function; partner identity and post-translational state must be considered when annotating p27 activity. |
| Localization and degradation | Ser10 phosphorylation supports CRM1-dependent nuclear export; Thr198 promotes 14-3-3 binding and cytoplasmic retention. CDK2-dependent Thr187 phosphorylation enables Cks1–SCF^SKP2 recognition, ubiquitination, and proteasomal turnover. Cytoplasmic p27 also regulates RhoA/stathmin, migration, microtubules, trafficking, and mTOR/autophagy. | Phosphosite mutants, trafficking assays, protein-interaction studies, ubiquitination assays, and genetic models | Nuclear p27 chiefly enforces cell-cycle restraint; cytoplasmic redistribution can remove this restraint and enable noncanonical, sometimes pro-migratory functions. |
| MEN4 clinical genetics | Heterozygous germline loss-of-function CDKN1B variants cause autosomal-dominant multiple endocrine neoplasia type 4. Fewer than 100 cases had been reported in a 2024 review; primary hyperparathyroidism occurs in approximately 75–80% of reported patients, often with pituitary or neuroendocrine tumors. | Families and MEN1-negative patients with MEN1-like disease; sequencing and functional variant studies | CDKN1B testing has genuine clinical use in MEN1-like cases after negative MEN1 testing, but penetrance, variant-specific risks, and surveillance evidence remain limited. |
| Breast cancer, 2023–2024 | A 3,794-patient analysis associated higher CDKN1B with better outcomes and more CD8+ T cells; multivariable HRs were 0.530 for disease-free survival and 0.498 for overall survival. A separate luminal-breast study used 868 patients plus METABRIC (1,500) and GEO (855), ranking p27 second after nodal stage in one survival model. | Retrospective cohorts, public datasets, machine learning, immune deconvolution, and cell-line drug screens | Promising prognostic marker; low-CDKN1B cells showed exploratory sensitivity to BMS-345541, voxtalisib, and serdemetan, but no prospective biomarker-guided clinical use is established. |
| Colorectal cancer, 2024 | Meta-analysis of 21 studies and 3,378 patients associated low p27 with worse overall survival (HR 0.44, 95% CI 0.31–0.61) and disease-free survival (HR 0.40, 95% CI 0.28–0.59). | Immunohistochemical studies, meta-analysis, and database validation | Prognostically promising but inconsistent: GEPIA and UALCAN analyses did not reproduce several survival or expression associations. |
| Ovarian cancer, 2024 | Low total p27 independently predicted worse overall survival (HR 2.097, 95% CI 1.121–3.922) and progression-free survival (HR 2.483, 95% CI 1.364–4.518); cytoplasmic Ser10-phosphorylated p27 showed different prognostic behavior. | Tumor immunohistochemistry, outcome analysis, chemotherapy-response assessment, and cisplatin-sensitive/resistant cell lines | Supports measuring abundance, phosphorylation, and compartment together; remains an investigational biomarker without validated clinical cutoffs. |
| Mechanistic cancer studies, 2024 | In HCC, FASN knockdown lowered SKP2 and increased p27 protein without changing CDKN1B mRNA; dominant-negative SKP2 or p27-T187A blocked AKT-driven hepatocarcinogenesis. In prostate cancer, WWP1 bound, ubiquitinated, and destabilized p27 downstream of an eccDNA–FAM84B–MYC circuit; androgen studies placed p27 in a BHLHE40–LYL1 senescence loop. | HCC cell lines, human tumors, AKT-driven mouse models, prostate-cancer cells, xenografts, metastasis models, ChIP-seq, knockdown, and rescue experiments | Strong preclinical evidence identifies multiple actionable routes for restoring p27, but tumor specificity and absence of validated p27-directed therapies limit current translation. |
Table: Summary of the verified identity, molecular mechanism, localization, clinical genetics, and recent translational evidence for human CDKN1B/p27Kip1. The table distinguishes established functions from context-dependent or investigational findings.
CDKN1B behaves chiefly as a dosage-sensitive tumor suppressor. Reduced nuclear p27 removes a key G1 restraint, but total loss is not required: accelerated degradation, impaired translation, phosphorylation-driven export, or truncation can produce functional insufficiency. In addition, cytoplasmic p27 may acquire pro-migratory activities. Consequently, DNA sequence, mRNA, total protein, phosphorylation state, and nuclear/cytoplasmic distribution are not interchangeable biomarkers. (bencivenga2025p27kip1andtumors pages 2-4, cusan2018landscapeofcdkn1b pages 2-4, cusan2018landscapeofcdkn1b pages 4-5)
Heterozygous germline loss-of-function CDKN1B variants cause multiple endocrine neoplasia type 4 (MEN4), a rare autosomal-dominant MEN1-like syndrome. A 2024 review reported fewer than 100 cases; primary hyperparathyroidism occurs in approximately 75–80% of reported patients and is often the first manifestation. Pituitary adenomas and neuroendocrine tumors also occur, generally with later onset and milder disease than classic MEN1. MEN4-associated hyperparathyroidism more often involves a single adenoma than the multigland disease typical of MEN1. [Brunetti et al., published October 2024, DOI URL: https://doi.org/10.3390/ijms252111586] (brunetti2024molecularpathophysiologyof pages 6-7)
A separate 2024 review estimated MEN4 at approximately 3–5% of MEN1-like states and diagnosis roughly 20 years later than genetically confirmed MEN1, although estimates vary because cohorts and ascertainment differ. [Trukhina et al., 2024, DOI URL: https://doi.org/10.32364/2587-6821-2024-8-9-4] (trukhina2024possiblecausesof pages 1-2)
The clearest current real-world application is therefore germline CDKN1B testing in patients with MEN1-like endocrine tumors after negative MEN1 testing, ordinarily within a multigene panel. Interpretation remains difficult because penetrance and variant-specific risks are poorly quantified, and very rare missense variants may remain variants of uncertain significance despite plausible functional effects. (bencivenga2025p27kip1andtumors pages 2-4, bencivenga2025p27kip1andtumors pages 8-9)
A 2023/2024 analysis encompassing 3,794 patients associated higher CDKN1B expression with greater CD8-positive T-cell infiltration and better outcome. In the authors’ cohort, higher expression was independently associated with improved disease-free survival (HR 0.530, 95% CI 0.330–0.852) and overall survival (HR 0.498, 95% CI 0.315–0.788); directionally similar associations occurred in TCGA and METABRIC. Low-CDKN1B cell lines were more sensitive to BMS-345541 in an exploratory screen of 50 lines. These results are retrospective and computational/preclinical rather than evidence for a clinically validated treatment rule. [Kim et al., published December 2023, DOI URL: https://doi.org/10.3390/jpm14010030] (kim2023lowcdkn1bexpression pages 6-9, kim2023lowcdkn1bexpression pages 1-2)
A September 2024 luminal-breast study analyzed 868 patients and external METABRIC and GEO cohorts of 1,500 and 855 patients. p27 ranked second after nodal stage in one machine-learning survival model, although adding it yielded only slight overall improvement. Low-CDKN1B cell lines showed greater sensitivity to voxtalisib and serdemetan (p=0.008 and p=0.023); palbociclib showed a nonsignificant trend. These are hypothesis-generating drug-screen findings, not prospective predictive validation. [Park et al., published September 2024, DOI URL: https://doi.org/10.4048/jbc.2024.0107] (park2024p27cellcycle pages 1-2, park2024p27cellcycle pages 12-13, park2024p27cellcycle pages 13-15)
A December 2024 colorectal-cancer meta-analysis pooled 21 studies and 3,378 patients. Low p27 was associated with poorer overall survival (reported HR 0.44, 95% CI 0.31–0.61) and disease-free survival (HR 0.40, 95% CI 0.28–0.59), as well as right-sided location and poorer differentiation. However, GEPIA and UALCAN analyses did not reproduce several survival or tumor-versus-normal findings, underscoring assay and cohort heterogeneity. [Zou et al., December 2024, DOI URL: https://doi.org/10.3389/fonc.2024.1495476] (zou2024prognosticsignificanceof pages 1-2)
In ovarian cancer, low total p27 independently predicted worse overall survival (HR 2.097, 95% CI 1.121–3.922) and progression-free survival (HR 2.483, 95% CI 1.364–4.518). Cytoplasmic Ser10-phosphorylated p27 showed a different association, reinforcing that total abundance and compartment-specific phospho-p27 should not be treated as equivalent measurements. The study also used cisplatin-sensitive and resistant cell lines, but did not establish a clinically actionable cutoff. [Zhu et al., published May 2024, DOI URL: https://doi.org/10.14670/hh-18-761] (zhu2024p27kip1andcytoplasmic pages 1-3)
In hepatocellular carcinoma, FASN knockdown across five cell lines reduced SKP2 mRNA and protein and increased p27 protein without materially changing CDKN1B mRNA, supporting post-transcriptional stabilization. Experiments were repeated in triplicate and reported p<0.0001. In AKT-driven mouse liver-tumor models, dominant-negative SKP2 or nonphosphorylatable p27-T187A blocked hepatocarcinogenesis in vitro and in vivo. The effect was not reproduced in tested colorectal-cancer or glioblastoma lines, indicating tumor-context specificity. [Cigliano et al., July 2024, DOI URL: https://doi.org/10.3390/medicina60071160] (cigliano2024fattyacidsynthase pages 14-16, cigliano2024fattyacidsynthase pages 5-7, cigliano2024fattyacidsynthase pages 1-2)
In prostate cancer, a 2024 study placed p27 in an eccDNA–FAM84B–MYC–WWP1 circuit. WWP1 co-immunoprecipitated with p27, increased its ubiquitination, and reduced p27 protein without changing CDKN1B mRNA. CDKN1B overexpression restrained FAM84B-driven proliferation, migration, xenograft growth, and metastatic activity, whereas WWP1 depletion restored p27. [Jin et al., July 2024, DOI URL: https://doi.org/10.1186/s11658-024-00616-3] (jin2024extrachromosomalcirculardna pages 18-20)
A December 2024 prostate-cancer study further implicated p27 in supraphysiological-androgen-induced senescence. In C4-2 and LNCaP models, androgen receptor/BHLHE40 signaling induced LYL1, and knockdown/rescue experiments placed p27 within a BHLHE40–LYL1 feedback circuit mediating senescence. This is relevant to the mechanism of bipolar androgen therapy but remains cell-model evidence rather than a validated patient-selection biomarker. [Horestani et al., December 2024, DOI URL: https://doi.org/10.1186/s12964-024-01970-7] (horestani2024functionalcircuitsof pages 1-3)
Recommended primary annotation: “Intrinsically disordered cyclin-dependent kinase regulator that binds cyclin–CDK complexes through an N-terminal CDI/KID domain; inhibits cyclin E/A–CDK2 and restrains RB–E2F-dependent G1/S progression, while context-dependently assembling and regulating cyclin D–CDK4/6.”
Recommended localization annotation: “Functions principally in the nucleus for canonical cell-cycle inhibition; shuttles between nucleus and cytoplasm through phosphorylation-dependent import/export. Cytoplasmic p27 regulates cytoskeletal dynamics, migration, microtubules, trafficking, and nutrient-stress signaling.”
Confidence assessment: The identity, cyclin–CDK binding, nuclear G1/S function, intrinsic disorder, and SKP2-dependent turnover are high-confidence, mechanistically established functions. MEN4 association is clinically established but penetrance and variant interpretation are incompletely resolved. Recent tumor biomarkers and proposed p27-restoration strategies are promising but remain investigational because most evidence is retrospective, assay-heterogeneous, or preclinical.
References
(cusan2018landscapeofcdkn1b pages 1-2): Martina Cusan, Giorgia Mungo, Mara De Marco Zompit, Ilenia Segatto, Barbara Belletti, and Gustavo Baldassarre. Landscape of cdkn1b mutations in luminal breast cancer and other hormone-driven human tumors. Frontiers in Endocrinology, Jul 2018. URL: https://doi.org/10.3389/fendo.2018.00393, doi:10.3389/fendo.2018.00393. This article has 43 citations.
(wafa2014theroleof pages 46-51): K Wafa. The role of a cyclin d2 splice variant in the regulation of the cell cycle: connecting cell cycle to cancer biology. Unknown journal, 2014.
(bencivenga2025p27kip1andtumors pages 1-2): Debora Bencivenga, Emanuela Stampone, Jahanzaib Azhar, Daniela Parente, Waqar Ali, Vitale Del Vecchio, Fulvio Della Ragione, and Adriana Borriello. P27kip1 and tumors: characterization of cdkn1b variants identified in men4 and breast cancer. Cells, 14:188, Jan 2025. URL: https://doi.org/10.3390/cells14030188, doi:10.3390/cells14030188. This article has 11 citations.
(bencivenga2025p27kip1andtumorsa pages 25-26): D Bencivenga, E Stampone, J Azhar, D Parente, and W Ali. P27kip1 and tumors: characterization of cdkn1b variants identified in men4 and breast cancer. cells 2025, 14, 188. Unknown journal, 2025.
(cusan2018landscapeofcdkn1b pages 2-4): Martina Cusan, Giorgia Mungo, Mara De Marco Zompit, Ilenia Segatto, Barbara Belletti, and Gustavo Baldassarre. Landscape of cdkn1b mutations in luminal breast cancer and other hormone-driven human tumors. Frontiers in Endocrinology, Jul 2018. URL: https://doi.org/10.3389/fendo.2018.00393, doi:10.3389/fendo.2018.00393. This article has 43 citations.
(bencivenga2025p27kip1andtumors pages 25-27): Debora Bencivenga, Emanuela Stampone, Jahanzaib Azhar, Daniela Parente, Waqar Ali, Vitale Del Vecchio, Fulvio Della Ragione, and Adriana Borriello. P27kip1 and tumors: characterization of cdkn1b variants identified in men4 and breast cancer. Cells, 14:188, Jan 2025. URL: https://doi.org/10.3390/cells14030188, doi:10.3390/cells14030188. This article has 11 citations.
(bencivenga2025p27kip1andtumorsa pages 29-30): D Bencivenga, E Stampone, J Azhar, D Parente, and W Ali. P27kip1 and tumors: characterization of cdkn1b variants identified in men4 and breast cancer. cells 2025, 14, 188. Unknown journal, 2025.
(cusan2018landscapeofcdkn1b pages 4-5): Martina Cusan, Giorgia Mungo, Mara De Marco Zompit, Ilenia Segatto, Barbara Belletti, and Gustavo Baldassarre. Landscape of cdkn1b mutations in luminal breast cancer and other hormone-driven human tumors. Frontiers in Endocrinology, Jul 2018. URL: https://doi.org/10.3389/fendo.2018.00393, doi:10.3389/fendo.2018.00393. This article has 43 citations.
(bencivenga2025p27kip1andtumors pages 2-4): Debora Bencivenga, Emanuela Stampone, Jahanzaib Azhar, Daniela Parente, Waqar Ali, Vitale Del Vecchio, Fulvio Della Ragione, and Adriana Borriello. P27kip1 and tumors: characterization of cdkn1b variants identified in men4 and breast cancer. Cells, 14:188, Jan 2025. URL: https://doi.org/10.3390/cells14030188, doi:10.3390/cells14030188. This article has 11 citations.
(bencivenga2025p27kip1andtumors pages 24-25): Debora Bencivenga, Emanuela Stampone, Jahanzaib Azhar, Daniela Parente, Waqar Ali, Vitale Del Vecchio, Fulvio Della Ragione, and Adriana Borriello. P27kip1 and tumors: characterization of cdkn1b variants identified in men4 and breast cancer. Cells, 14:188, Jan 2025. URL: https://doi.org/10.3390/cells14030188, doi:10.3390/cells14030188. This article has 11 citations.
(brunetti2024molecularpathophysiologyof pages 6-7): Alessandro Brunetti, Roberta Cosso, Fabio Vescini, and Alberto Falchetti. Molecular pathophysiology of parathyroid tumorigenesis—the lesson from a rare disease: the “men1 model”. International Journal of Molecular Sciences, 25:11586, Oct 2024. URL: https://doi.org/10.3390/ijms252111586, doi:10.3390/ijms252111586. This article has 4 citations.
(trukhina2024possiblecausesof pages 1-2): D.A. Trukhina, E.O. Mamedova, Zh.E. Belaya, and G.A. Melnichenko. Possible causes of phenocopy syndrome in multiple endocrine neoplasia type 1. Russian Medical Inquiry, 8:526-530, Jan 2024. URL: https://doi.org/10.32364/2587-6821-2024-8-9-4, doi:10.32364/2587-6821-2024-8-9-4. This article has 1 citations.
(bencivenga2025p27kip1andtumors pages 8-9): Debora Bencivenga, Emanuela Stampone, Jahanzaib Azhar, Daniela Parente, Waqar Ali, Vitale Del Vecchio, Fulvio Della Ragione, and Adriana Borriello. P27kip1 and tumors: characterization of cdkn1b variants identified in men4 and breast cancer. Cells, 14:188, Jan 2025. URL: https://doi.org/10.3390/cells14030188, doi:10.3390/cells14030188. This article has 11 citations.
(kim2023lowcdkn1bexpression pages 6-9): Hyung-Suk Kim, Yung-Kyun Noh, Kyueng-Whan Min, and Dong-Hoon Kim. Low cdkn1b expression associated with reduced cd8+ t lymphocytes predicts poor outcome in breast cancer in a machine learning analysis. Journal of Personalized Medicine, 14:30, Dec 2023. URL: https://doi.org/10.3390/jpm14010030, doi:10.3390/jpm14010030. This article has 4 citations.
(kim2023lowcdkn1bexpression pages 1-2): Hyung-Suk Kim, Yung-Kyun Noh, Kyueng-Whan Min, and Dong-Hoon Kim. Low cdkn1b expression associated with reduced cd8+ t lymphocytes predicts poor outcome in breast cancer in a machine learning analysis. Journal of Personalized Medicine, 14:30, Dec 2023. URL: https://doi.org/10.3390/jpm14010030, doi:10.3390/jpm14010030. This article has 4 citations.
(park2024p27cellcycle pages 1-2): In Ah Park, Yung-Kyun Noh, Kyueng-Whan Min, Dong-Hoon Kim, Jeong-Yeon Lee, Byoung Kwan Son, Mi Jung Kwon, Myung-Hoon Han, Joon Young Hur, and Jung Soo Pyo. P27 cell cycle inhibitor and survival in luminal-type breast cancer: gene ontology, machine learning, and drug screening analysis. Journal of Breast Cancer, 27:305-322, Sep 2024. URL: https://doi.org/10.4048/jbc.2024.0107, doi:10.4048/jbc.2024.0107. This article has 2 citations and is from a peer-reviewed journal.
(park2024p27cellcycle pages 12-13): In Ah Park, Yung-Kyun Noh, Kyueng-Whan Min, Dong-Hoon Kim, Jeong-Yeon Lee, Byoung Kwan Son, Mi Jung Kwon, Myung-Hoon Han, Joon Young Hur, and Jung Soo Pyo. P27 cell cycle inhibitor and survival in luminal-type breast cancer: gene ontology, machine learning, and drug screening analysis. Journal of Breast Cancer, 27:305-322, Sep 2024. URL: https://doi.org/10.4048/jbc.2024.0107, doi:10.4048/jbc.2024.0107. This article has 2 citations and is from a peer-reviewed journal.
(park2024p27cellcycle pages 13-15): In Ah Park, Yung-Kyun Noh, Kyueng-Whan Min, Dong-Hoon Kim, Jeong-Yeon Lee, Byoung Kwan Son, Mi Jung Kwon, Myung-Hoon Han, Joon Young Hur, and Jung Soo Pyo. P27 cell cycle inhibitor and survival in luminal-type breast cancer: gene ontology, machine learning, and drug screening analysis. Journal of Breast Cancer, 27:305-322, Sep 2024. URL: https://doi.org/10.4048/jbc.2024.0107, doi:10.4048/jbc.2024.0107. This article has 2 citations and is from a peer-reviewed journal.
(zou2024prognosticsignificanceof pages 1-2): Jing Zou, Dong Wang, Gaoping Yin, Kexiang Lu, Kaibin Chang, and He Li. Prognostic significance of p27 in colorectal cancer: a meta-analysis and bioinformatics analysis. Frontiers in Oncology, Dec 2024. URL: https://doi.org/10.3389/fonc.2024.1495476, doi:10.3389/fonc.2024.1495476. This article has 3 citations.
(zhu2024p27kip1andcytoplasmic pages 1-3): Mengna Zhu, Si Sun, Lin Huang, Lingling Gao, Mengqing Chen, Jing Cai, Zehua Wang, and Minggang Peng. P27kip1 and cytoplasmic pser10p27 are promising biomarkers for predicting prognosis and chemotherapy response in ovarian cancer. Histology and histopathology, pages 18761, May 2024. URL: https://doi.org/10.14670/hh-18-761, doi:10.14670/hh-18-761. This article has 1 citations and is from a peer-reviewed journal.
(cigliano2024fattyacidsynthase pages 14-16): Antonio Cigliano, Maria M. Simile, Gianpaolo Vidili, Giovanni M. Pes, Maria P. Dore, Francesco Urigo, Eleonora Cossu, Li Che, Claudio Feo, Sara M. Steinmann, Silvia Ribback, Rosa M. Pascale, Matthias Evert, Xin Chen, and Diego F. Calvisi. Fatty acid synthase promotes hepatocellular carcinoma growth via s-phase kinase-associated protein 2/p27kip1 regulation. Jul 2024. URL: https://doi.org/10.3390/medicina60071160, doi:10.3390/medicina60071160. This article has 12 citations.
(cigliano2024fattyacidsynthase pages 5-7): Antonio Cigliano, Maria M. Simile, Gianpaolo Vidili, Giovanni M. Pes, Maria P. Dore, Francesco Urigo, Eleonora Cossu, Li Che, Claudio Feo, Sara M. Steinmann, Silvia Ribback, Rosa M. Pascale, Matthias Evert, Xin Chen, and Diego F. Calvisi. Fatty acid synthase promotes hepatocellular carcinoma growth via s-phase kinase-associated protein 2/p27kip1 regulation. Jul 2024. URL: https://doi.org/10.3390/medicina60071160, doi:10.3390/medicina60071160. This article has 12 citations.
(cigliano2024fattyacidsynthase pages 1-2): Antonio Cigliano, Maria M. Simile, Gianpaolo Vidili, Giovanni M. Pes, Maria P. Dore, Francesco Urigo, Eleonora Cossu, Li Che, Claudio Feo, Sara M. Steinmann, Silvia Ribback, Rosa M. Pascale, Matthias Evert, Xin Chen, and Diego F. Calvisi. Fatty acid synthase promotes hepatocellular carcinoma growth via s-phase kinase-associated protein 2/p27kip1 regulation. Jul 2024. URL: https://doi.org/10.3390/medicina60071160, doi:10.3390/medicina60071160. This article has 12 citations.
(jin2024extrachromosomalcirculardna pages 18-20): Wei Jin, Zhenqun Xu, Yan Song, and Fangjie Chen. Extrachromosomal circular dna promotes prostate cancer progression through the fam84b/cdkn1b/myc/wwp1 axis. Cellular & Molecular Biology Letters, Jul 2024. URL: https://doi.org/10.1186/s11658-024-00616-3, doi:10.1186/s11658-024-00616-3. This article has 15 citations and is from a peer-reviewed journal.
(horestani2024functionalcircuitsof pages 1-3): Mehdi Heidari Horestani, Katrin Schindler, and Aria Baniahmad. Functional circuits of lyl1 controlled by supraphysiological androgen in prostate cancer cells to regulate cell senescence. Cell Communication and Signaling : CCS, Dec 2024. URL: https://doi.org/10.1186/s12964-024-01970-7, doi:10.1186/s12964-024-01970-7. This article has 8 citations.