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The protein encoded by TDP1 is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. Additionally we are shipping TDP1 Antibodies (96) and TDP1 Proteins (11) and many more products for this protein.
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AtTDP plays a clear role in the repair of topoisomerase I (show TOP1 ELISA Kits)-DNA complexes.
We show that two genes, TDP1, a tyrosyl-DNA-phosphdiesterase, and TAF12 (show TAF12 ELISA Kits), an RNA polymerase II TATA-box binding factor, cause CIN (show PDXP ELISA Kits) when overexpressed in human cells. Using SDL screens in yeast, we identified a set of genes that when deleted specifically kill cells with high levels of Tdp1
TDP1 participation in human non-homologous end joining (NHEJ) is mediated by interaction with XLF (show NHEJ1 ELISA Kits), and that TDP1-XLF (show NHEJ1 ELISA Kits) interactions and subsequent NHEJ events are regulated by phosphorylation of TDP1-S81.
Mutations in TDP1 and APTX have been linked to Spinocerebellar ataxia with axonal neuropathy (SCAN1) and Ataxia-ocular motor apraxia 1 (AOA1), respectively, while mutations in PNKP are considered to be responsible for Microcephaly with seizures (MCSZ) and Ataxia-ocular motor apraxia 4 (AOA4).
The data obtained suggest that PARP1 (show PARP1 ELISA Kits) and TDP1 bind in an antiparallel orientation; the N-terminus of the former protein interacts with the C-terminal domain of the latter.
Tyrosyl-DNA-phosphodiesterase I (TDP1) participates in the removal and repair of stabilized-Top2alpha cleavage complexes in human cells.
varying expression levels of TOP1 (show TOP1 ELISA Kits) and TDP1 polypeptides in multiple colorectal cancer cell lines and in clinical colorectal cancer samples, are reported.
both TOP1 (show TOP1 ELISA Kits) and TDP1 were upregulated in the tumor tissue compared to the adjacent non-tumor tissue in non-small cell lung cancer tissue
Density functional theory computations are used to acquire thermodynamic and kinetic data along the catalytic pathway, including the phosphoryl transfers of Tdp1 and subsequent hydrolysis.
TDP1 plays a role during the early stages of mammalian NHEJ. TPD1 stimulated DNA binding by XLF. TDP1 also promoted DNA binding by Ku70/80 and stimulated DNA-PK activity.
These findings suggest that the flexibility of Tdp1 active site residues may impair the resolution of mutant Tdp1 covalent phosphohistidyl intermediates
These findings provide evidence for TDP1 as a novel mitochondrial enzyme.
The interaction with Lig3alpha is promoted by serine 81 that is located within a putative S/TQ site in the N-terminus domain of TDP1.
Data indicate that TDP1 is required for neural homeostasis and reveal a widespread requisite for TDP1 function in response to acutely elevated levels of DNA topoisomerase I (Top1 (show TOP1 ELISA Kits))-associated DNA strand breaks.
This study provides a direct demonstration that Tdp1 repairs Topo I (show TOP1 ELISA Kits) covalent lesions in vivo and suggests that spinocerebellar ataxia with axonal neuropathy (SCAN1 (show CANT1 ELISA Kits)) arises from the recessive neomorphic mutation H493R.
Tdp1(-/-) fibroblasts exhibited deficiencies in processing 3'-phosphotyrosyl single-strand breaks and 3'-phosphoglycolate double-strand breaks, but not 3 (show CNOT3 ELISA Kits)'-phosphoglycolate single-strand breaks.
The protein encoded by this gene is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. This protein may also remove glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks. This gene is a member of the phospholipase D family and contains two PLD phosphodiesterase domains. Mutations in this gene are associated with the disease spinocerebellar ataxia with axonal neuropathy (SCAN1). While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same isoform.
tyrosyl-DNA Phosphodiesterase (Tdp1)
, tyrosyl-DNA phosphodiesterase (Tdp1)
, tyrosyl-DNA phosphodiesterase 1
, tyrosyl-DNA phosphodiesterase 1-like
, tyr-DNA phosphodiesterase 1
, protein expressed in male leptotene and zygotene spermatocytes 501
, tyrosyl-DNA phodphodiesterase 1