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A tri-serine cluster within the topoisomerase IIalpha-interaction domain of the BLM helicase is required for regulating chromosome breakage in human cells.
Steered molecular dynamics calculations suggests the Top2-catalyzed DNA passage may be achieved by a rocker-switch-type movement of the DNA-gate.
The highly proliferating C2A subtype of hepatoblastoma is characterized by topoisomerase 2-alpha gene up-regulation and Fanconi anemia pathway activation.
TOP2A protein showed a time dependent influence on prognosis in stage I-II luminal breast cancer, suggesting it might be a potential predictor of late recurrence for this group of patients.
Data indicate that tyrosyl-DNA phosphodiesterase 2 (TDP2) alone does not remove DNA topoisomerase II (TOP2)-DNA complexes from genomic DNA in vitro and that depletion of TDP2 in cells does not slow the removal of TOP2-DNA complexes.
High TOP2A expression and Gene Amplification is associated with Upper Tract Urothelial Carcinomas.
Ki-67 and TOPO 2A expression correlated with tumour size and tumour invasiveness in somatotropinomas.
RNF168 interacts with TOP2alpha to mediate its polyubiquitylation and RNF168 deficiency confers resistance to ICRF-193, a TOP2 catalytic inhibitor, and cytotoxic anti-cancer drug etoposide in cultured mouse cells.
we show that despite being more cytotoxic, F14512 is less efficient than etoposide at producing TOP2alpha cleavage-complex (TOP2alphacc) in cells
our data support further assessment of TOP2A and EZH2 as biomarkers for early identification of patients with increased metastatic potential that may benefit from adjuvant or neoadjuvant targeted therapy approaches
High mRNA levels of TOP2A is independent predictor of poor outcome in Renal Cell Carcinoma patients.
findings implicate TOP2A cleavage as a broad DNA damage mechanism in oncogenic translocations as well as a functional role of TOP2A cleavage in regulating transcription elongation and gene activation.
TOP2A acts as a co-activator of beta-catenin and activates Epithelial-mesenchymal transition process.
ProEx C is an immunohistochemical cocktail containing antibodies direct against topoisomerase IIalpha (TOP2A) and minichromosome maintenance 2 (MCM2) proteins. This brief review covers the effective utility of ProEx C as adjunct tool in assessing the urothelial lesions in urine cytology, also providing prognostic and therapeutic information to help in clinical decisions.
High TOP2A expression was significantly associated with longer time to progression after EDP-M. TOP2A and TS proteins assessed by immunohistochemistry significantly correlated with mRNA expression. Immunohistochemical TOP2A expression was associated with a non-significant better response and longer TTP after EDP-M.
Data show that comparing with Ki-67 and TOP2A, RacGAP1 allowed for a clearer prognostic statement.
These findings reveal a novel, p53-independent activity of Mdm2 and have important implications for the choice of chemotherapeutic agents in the treatment of Mdm2-overexpressing tumors. Herein is shown that tumor cells with MDM2 amplification are selectively resistant to treatment with topoisomerase II poisons but not other DNA damaging agents
The methodology is useful for a high-throughput analysis of drugs that poison Top2, allowing not just the discrimination of the Top2 isoform that is targeted but also to track its removal
TOP2A was identified in association with the progression and prognosis of pancreatic ductal adenocarcinoma probably by regulating cell cycle and p53 signaling pathway.
the relation between TOP2A levels and sensitivity for doxorubicin was examined, confirming reports that TOP2A mRNA levels were overexpressed in MPNST and showing that MPNST cell lines exhibited relatively high TOP2A protein levels and sensitivity to doxorubicin.
Topo IIalpha plays an important role in adipogenesis.
Polyamide functionalisation at the N1-position offers a design strategy to improve drug-like properties. Dicationic HxIP* 3 increased topo IIalpha expression and chemosensitivity to topo II-targeting agents.
TOP2 and BAF cooperate to recruit pluripotency factors, which explains some of the instructive roles of BAF complexes.
Deletion or deficiency of PTEN leads to down regulation of TOP2A, dysfunction of the decatenation checkpoint and incomplete DNA decatenation in G2 and M phases.
Inhibition of DNA topoisomerase II selectively reduces the threat of tumorigenicity
Cohesin removal is a prerequisite for the posterior topoisomerase IIalpha-mediated resolution of persisting catenations between segregating chromatids during anaphase II.
Data show that unfolded protein response (UPR)-induced changes in topoisomerase IIalpha (Topo IIalpha) protein levels are not responsible for resistance to etoposide, and that the PERK plays a Topo IIalpha-independent role in altered sensitivity to the drug.
Topoisomerase IIa not only contributes to stem-cell transcriptome regulation but also primes developmental genes for subsequent activation upon differentiation.
studies indicate that the ability of TOP2A to prevent DNA entanglement at mitosis requires BAF complexes and suggest that this activity contributes to the role of BAF subunits as tumour suppressors
our data reveal TDP2-mediated error-free NHEJ as an efficient and accurate mechanism to repair TOP2-induced DSBs
Top2alpha is suggested to be a universal target for cancer immunotherapy.
DNA topoisomerase II distribution in mouse preimplantation embryos
DNA topoisomerase II is essential for preimplantation mouse development
The role of topoisomerase II in the excision of DNA loop domains during apoptosis.
CCAAT binding factor (CBF) binding mediates cell cycle activation of this enzyme; conventional CBF activation domains are not required.
Gly881, which is located in the ATP binding site, was replaced by Arg in DNA topoisomerase IIalpha of NC-190-resistance tumor cells. These cells were also etoposide-resistant.
Results suggest that topo IIalpha-depleted cells with the droplet-like nuclear structure induce apoptosis, which is dependent on caspase and p53 activity during the G1 phase in mammalian cells.
The functional status of pRb protein may influence sensitivity to etoposide by facilitating the repair of trapped TOP2-DNA complexes.
Expression of the topoisomerase IIalpha gene in confluent NIH 3T3 cells was induced by treatment with f-PIP
Interacts with protein targets to mediate salicylic acid (SA)-dependent signaling necessary for the immune response to avirulent pathogens.
The absence of zygotic top2a is not fully compensated for by maternal, zygotic or ectopic top2b mRNA suggesting distinct functions of Top2a and Top2b in embryonic development.
Results confirm a conserved role for topoisomerase II alpha (TOP2A) in vertebrates as well as a dose-sensitive requirement for top2a in adults.
This gene encodes a DNA topoisomerase, an enzyme that controls and alters the topologic states of DNA during transcription. This nuclear enzyme is involved in processes such as chromosome condensation, chromatid separation, and the relief of torsional stress that occurs during DNA transcription and replication. It catalyzes the transient breaking and rejoining of two strands of duplex DNA which allows the strands to pass through one another, thus altering the topology of DNA. Two forms of this enzyme exist as likely products of a gene duplication event. The gene encoding this form, alpha, is localized to chromosome 17 and the beta gene is localized to chromosome 3. The gene encoding this enzyme functions as the target for several anticancer agents and a variety of mutations in this gene have been associated with the development of drug resistance. Reduced activity of this enzyme may also play a role in ataxia-telangiectasia.
, DNA topoisomerase (ATP-hydrolyzing)
, DNA topoisomerase 2-alpha
, DNA topoisomerase II, 170 kD
, DNA topoisomerase II, alpha isozyme
, DNA Topoisomerase II alpha
, topoisomerase (DNA) 2 alpha
, DNA topoisomeraseII_alpha
, topoisomerase (DNA) II alpha
, Thimet metalloendopeptidase 2
, Zincin-like metalloproteases family protein 2
, topoisomerase 2