Cdk1
- Known as:
- Cdk1
- Catalog number:
- 11-115-C100
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Exbio
- Gene target:
- Cdk1
Related genes to: Cdk1
- Gene:
- CDK1 NIH gene
- Name:
- cyclin dependent kinase 1
- Previous symbol:
- CDC2
- Synonyms:
- CDC28A
- Chromosome:
- 10q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-06-08
Related products to: Cdk1
Related articles to: Cdk1
- Understanding the complex connections between cellular mechanisms is crucial for developing effective cancer treatments. In this study, new Schiff base derivative triazine compounds (5-8) were synthesized and structurally characterized using various spectroscopic techniques to investigate their cellular and gene-protein-level effects in lung cancer and to develop anticancer activity strategies. The cytotoxic activities of compounds were evaluated against A549 and MRC-5 cell lines using the WST-8 assay. Moreover, cellular death mechanisms in lung cancer were investigated using methods such as qRT-PCR, ELISA, membrane array, and Flow cytometry. In lung cancer cells, compounds 5 (58.24%) and 6 (59.08%) were mildly effective in terms of cell viability, and these two compounds exhibited cytotoxic activity at a dose of 50 µM. Also, while an increase in the expressions of the p21, p27, and p53 genes was observed across all compounds in A549 cells, a decrease in the expressions of the GRP78, GRP94, AKT, RIPK1, CDK1, CDK2, HSP27, HSP40, HSP60, and HSP90 genes was observed. Besides, GRP78 and Caspase-3 were considerably increased by compounds 5 and 6. While Caspase-3, CHK1, P38, P53, and TRAILR-2 pro-apoptotic protein expressions increased, BCL-2, BCL-W, IGF-II, and NFB anti-apoptotic protein expressions decreased for all compounds. The G0/G1 phase was increased by compounds 5 and 6. Although these compounds attenuated both the S and G2/M phases. Overall, the new triazines target dysregulated cell-cycle, ER stress, and apoptotic pathways, demonstrating strong therapeutic potential in lung cancer. Notably, compounds 5 and 6 exhibited cytotoxic and pathway-modulating activities, highlighting their promise as clinically relevant lead candidates. - Source: PubMed
Mesci SedaDavarcı DeryaYazgan BurakArıman Bekir SabriYıldırım TubaŞenkuytu Elif - Insect wing polyphenism enables a single genome to produce distinct wing morphs in response to environmental cues, yet its underlying cellular determinants remain elusive. Here, we perform single-cell RNA sequencing of long-winged- and short-winged-destined wing buds of Pyrrhocoris apterus and Nilaparvata lugens, identifying six conserved cell types with comparable proportions between the two morphs. RNA interference-mediated silencing of 51 marker genes indicates that wing-patterning genes En (epithelial-like cells) and bs (tracheal cells), and cell-cycle genes Anln, CycB3, and cdk1 (neuron cells), are essential for long-winged development, among which En exhibits a specific temporal requirement. Flow cytometry analysis shows that long-winged formation mainly relies on an extended duration of cell proliferation. Cross-species comparisons indicate shared wing cell identities. Our findings indicate that hemipteran short-winged morphs may evolve from ancestral long-winged forms via precise regulation of wing-patterning and cell-cycle gene expression in epithelial‑like, tracheal, and neuron cells. This provides insights into the developmental plasticity of insect tissues at single‑cell resolution. - Source: PubMed
Publication date: 2026/07/02
Wan YiWu Hui-JieHuang Heng-GuangLiu Zhuo-QiSun Zhao-XiangYang Zhang-NvXu Hai-Jun - Skeletal muscle differentiation depends on precise temporal regulation of protein modifications. To define how phosphorylation and lysine acetylation change during this process, we applied tandem mass tag (TMT)-based quantitative proteomics to human myoblasts sampled at six stages spanning proliferation, induction of differentiation, and early myotube formation. Using sequential enrichment of phosphorylated and acetylated peptides, high-pH fractionation, and high-resolution mass spectrometry, we identified more than 22,000 modified peptides and quantified their temporal behavior after correction for protein abundance. Phosphorylation exhibited extensive site-specific remodeling throughout the time course, whereas acetylation showed a pronounced relative increase during late differentiation. Integration of corrected modification levels with protein abundances and temporal clustering revealed stage-specific regulation of processes linked to cell-cycle withdrawal, metabolic transitions, cytoskeletal reorganization, and chromatin-associated functions. Predicted temporal activity profiles of kinases, acetyltransferases, and deacetylases uncovered coordinated regulatory patterns, including activity relationships involving CK2A1-HDAC1/2, PRKAA1-HAT1, and CDK1/2-KAT7. Dual-modified proteins such as lamin A/C and glycolytic enzymes displayed densely regulated clusters of phosphorylation and acetylation sites that may contribute to nuclear remodeling and metabolic adaptation during myogenesis. Together, this work provides a high-resolution temporal phospho-acetylome atlas of human muscle cell differentiation, identifies candidate phosphorylation-acetylation coordination patterns, and establishes a systems-level resource for future mechanistic studies of post-translational regulation in skeletal muscle development. - Source: PubMed
Publication date: 2026/07/02
Smith Lauren EHagensen Christina ETsiamis Vasileiosvan Waardenberg Ashley JMamchaoui KamelJensen Ole NSchwämmle VeitRogowska-Wrzesinska Adelina - Cells entering mitosis with incompletely replicated DNA face catastrophic chromosome segregation failure. During interphase, the replisome-associated E3 ubiquitin ligase TRAIP ubiquitylates barriers in front of the fork to allow replisome progression. In mitosis, TRAIP is reprogrammed from a -acting to a -acting ligase that can ubiquitylate the replisome itself. This enables the processing of unreplicated DNA by promoting replisome disassembly, fork breakage, and joining of the broken chromosome arms. Here, we describe a mechanism for this reprogramming: the ATPase TTF2 is recruited to the replisome, where its noncatalytic N-terminal domain tethers Cyclin B-CDK1-phosphorylated TRAIP to the leading strand DNA polymerase ε in a geometry that allows replisome ubiquitylation. Thus, a phospho-regulated architectural switch alters replisome organization in mitosis to safeguard genome integrity before chromosome segregation. - Source: PubMed
Publication date: 2026/07/02
Can GeylaniShyian MaksymKrishnamoorthy ArchanaAhmed SamreenLim YangWu AlexPavani RaphaelZaher Manal SNussenzweig AndréRäschle MarkusWilson Thomas EGlover Thomas WWalter Johannes CPellman David - Emodin is a naturally occurring anthraquinone being investigated for its anticancer potential due to its ability to modulate the cell cycle and inhibit tumor progression. The cell cycle is composed of a series of events that dictate cell growth and cell division. The G0/G1 checkpoint is the resting stage before the first gap phase (G1), whereas the G2/M checkpoint is the working stage from the second gap phase (G2) before mitosis begins. Emodin exerts its effects by the following means: Cyclins, which propel the cells through the cell cycle stages; cyclin-dependent kinases (CDKs), which are energy sources that, along with cyclins, push the cell cycle further; and finally, CDK inhibitors, such as p21 and p27, which can inhibit CDK activity. G0/G1 arrest is mediated by the suppression of cyclin D/CDK4 and cyclin E/CDK2 activity, whereas G2/M arrest results from the inhibition of cyclin B/CDK1 and the disruption of mitotic progression. G2/M arrest is further reinforced by the activation of the checkpoint kinases, Chk1 and Chk2. These kinases operate downstream of DNA damage sensors and effectors to maintain cell cycle blockade. The present review discusses the mechanisms of emodin-induced cell cycle arrest. In preclinical settings, emodin has been shown to be capable of suppressing tumor cell proliferation in multiple cancer models, both by itself and in combination with standard chemotherapy or radiotherapy. However, suboptimal bioavailability and metabolic instability are obstacles that have hindered its clinical application, with results being inconsistent among cancer types. Future studies are required to develop more efficacious drug delivery systems, identify predictive biomarkers and conduct strong clinical trials. Addressing these issues may position emodin as a viable cancer therapeutic option, either alone or in combination with current therapies. - Source: PubMed
Publication date: 2026/06/19
Das ShreyaKompala JhansiLaney KylePathak SnehaNayar RaviKhurana SukantGhezzi AlfredoKarthik LakshminarayananBanerjee Abhijit G