The FHA domain of aprataxin interacts with the C-terminal region of XRCC1
- 10 November 2004
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 325 (4) , 1279-1285
- https://doi.org/10.1016/j.bbrc.2004.10.162
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair proteinAnnals of Neurology, 2004
- Mutation of TDP1, encoding a topoisomerase I–dependent DNA damage repair enzyme, in spinocerebellar ataxia with axonal neuropathyNature Genetics, 2002
- The FHA domainFEBS Letters, 2001
- The Molecular Basis of FHA Domain:Phosphopeptide Binding Specificity and Implications for Phospho-Dependent Signaling MechanismsMolecular Cell, 2000
- Molecular Cloning of the Human Gene, PNKP, Encoding a Polynucleotide Kinase 3′-Phosphatase and Evidence for Its Role in Repair of DNA Strand Breaks Caused by Oxidative DamageJournal of Biological Chemistry, 1999
- Structure of an XRCC1 BRCT domain: a new protein-protein interaction moduleThe EMBO Journal, 1998
- Role of a BRCT domain in the interaction of DNA ligase III-α with the DNA repair protein XRCC1Current Biology, 1998
- XRCC1 Polypeptide Interacts with DNA Polymerase and Possibly Poly (ADP-Ribose) Polymerase, and DNA Ligase III Is a Novel Molecular 'Nick-Sensor' In VitroNucleic Acids Research, 1996
- Hereditary motor and sensory neuropathy associated with cerebellar atrophy (HMSNCA): a new diseaseJournal of the Neurological Sciences, 1995
- Ataxia—ocular motor aprilaxia: A syndrome mimicking ataxia‐telangiectasiaAnnals of Neurology, 1988