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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. Zusätzlich bieten wir Ihnen TDP1 Proteine (10) und TDP1 Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal TDP1 Primary Antibody für ELISA, WB - ABIN565920
Katyal, el-Khamisy, Russell, Li, Ju, Caldecott, McKinnon: TDP1 facilitates chromosomal single-strand break repair in neurons and is neuroprotective in vivo. in The EMBO journal 2007
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Human Polyclonal TDP1 Primary Antibody für IHC (p), IP - ABIN257087
Perego, Cossa, Tinelli, Corna, Carenini, Gatti, De Cesare, Ciusani, Zunino, Luison, Canevari, Zaffaroni, Beretta: Role of tyrosyl-DNA phosphodiesterase 1 and inter-players in regulation of tumor cell sensitivity to topoisomerase I inhibition. in Biochemical pharmacology 2011
Show all 2 Pubmed References
AtTDP plays a clear role in the repair of topoisomerase I (zeige TOP1 Antikörper)-DNA complexes.
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 (zeige PARP1 Antikörper) 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 (zeige TOP1 Antikörper) and TDP1 polypeptides in multiple colorectal cancer cell lines and in clinical colorectal cancer samples, are reported.
both TOP1 (zeige TOP1 Antikörper) 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
This article summarizes and compares the biochemistry, functions, and post-translational regulation of TDP1 and TDP2 (zeige TDP2 Antikörper), as well as the relevance of TDP1 and TDP2 (zeige TDP2 Antikörper) as determinants of response to anticancer agents
TDP1 and APTX (zeige APTX Antikörper) take part in the mitochondrial DNA repair and are apparently being transported from the cell nucleus. (Review)
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 (zeige TOP1 Antikörper))-associated DNA strand breaks.
This study provides a direct demonstration that Tdp1 repairs Topo I (zeige TOP1 Antikörper) covalent lesions in vivo and suggests that spinocerebellar ataxia with axonal neuropathy (SCAN1 (zeige CANT1 Antikörper)) 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 (zeige CNOT3 Antikörper)'-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