The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions
about
Envisioning the dynamics and flexibility of Mre11-Rad50-Nbs1 complex to decipher its roles in DNA replication and repairDestabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylaseBase excision repair: a critical player in many gamesPrereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins.New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.Regulation of NEIL1 protein abundance by RAD9 is important for efficient base excision repairThe C-terminal Domain (CTD) of Human DNA Glycosylase NEIL1 Is Required for Forming BERosome Repair Complex with DNA Replication Proteins at the Replicating Genome: DOMINANT NEGATIVE FUNCTION OF THE CTD.Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase.Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair.Regulation of limited N-terminal proteolysis of APE1 in tumor via acetylation and its role in cell proliferation.Dynamic structures in DNA damage responses & cancer.Distinct functional consequences of MUTYH variants associated with colorectal cancer: Damaged DNA affinity, glycosylase activity and interaction with PCNA and Hus1.Human Apurinic/Apyrimidinic Endonuclease (APE1) Is Acetylated at DNA Damage Sites in Chromatin, and Acetylation Modulates Its DNA Repair Activity.Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013)Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition.Crystal structure of mimivirus uracil-DNA glycosylase.Characterization of substrate binding and enzymatic removal of a 3-methyladenine lesion from genomic DNA with TAG of MDR A. baumannii.Pre-Replicative Repair of Oxidized Bases Maintains Fidelity in Mammalian Genomes: The Cowcatcher Role of NEIL1 DNA Glycosylase.What Combined Measurements From Structures and Imaging Tell Us About DNA Damage Responses.A role of disordered domains in regulating protein oligomerization and stability.Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes.The C-terminal tail of the NEIL1 DNA glycosylase interacts with the human mitochondrial single-stranded DNA binding protein.
P2860
Q28085622-DE8ADA8C-0B65-4864-B5FF-C0ED7DE784C2Q33558133-A6039B5C-B914-4621-93FE-93F39810CFC1Q33908163-4A57E1CA-A064-41E5-85B8-A6E33F92B027Q34360665-3F3356B9-C025-4AA0-A9E7-B970DB6A0CC6Q35395549-DF9F6034-9EFF-4CF6-B68E-B78E49F3A203Q35786136-9F2B6249-6542-42D6-9F2D-903D6A728D3BQ35978248-78012F4A-BB93-4859-A6F8-36403D76ABC0Q36102804-DBD8EE2E-A6B0-4053-868D-4B90ED57480EQ37102321-E4760FA2-74C3-4194-900F-BA51EC8A1F5FQ37225608-74FFEF95-2F05-4A93-9CA6-22BD29E2DB77Q37367852-F65A6F59-FB4D-4ADA-A628-70EF135C28B8Q37397651-EEA8D302-C8F0-40CC-883B-72DEB55B3179Q38725408-B69EE1F3-5D70-4781-98B9-6C96875A2BF4Q39148653-919B9D60-D5BB-4E73-9EE7-AE5D38D5E26AQ39848487-B26B00B3-9CCF-416C-890E-328AFA534967Q40099585-1AEC2F09-67FE-4151-9C7D-E816E8FB089AQ40502759-2EB84119-378E-46B0-B97E-46A94098C912Q41225003-AF5084D0-B618-4AF4-A2B8-A47829F2DA83Q41319392-6C2A82AD-69D6-4493-9198-E82FF15DE863Q42204359-630E6BF4-F707-4EAE-A7B6-8E1CCE73B9F1Q48340987-67CFD2D8-7642-47A3-B1D5-314510F94507Q52361367-82B8B959-6BCA-4651-8FB9-44D9F9AC62D9
P2860
The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 27 March 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The disordered C-terminal doma ...... ia intramolecular interactions
@en
The disordered C-terminal doma ...... a intramolecular interactions.
@nl
type
label
The disordered C-terminal doma ...... ia intramolecular interactions
@en
The disordered C-terminal doma ...... a intramolecular interactions.
@nl
prefLabel
The disordered C-terminal doma ...... ia intramolecular interactions
@en
The disordered C-terminal doma ...... a intramolecular interactions.
@nl
P2093
P2860
P1476
The disordered C-terminal doma ...... ia intramolecular interactions
@en
P2093
Luis Marcelo F Holthauzen
Muralidhar L Hegde
Pavana M Hegde
Sankar Mitra
Susan E Tsutakawa
Vincent J Hilser
P2860
P304
P356
10.1016/J.JMB.2013.03.030
P407
P577
2013-03-27T00:00:00Z