Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions. - Test2 - elhamkhani - TriplyDB

Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions.

Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions.

http://www.wikidata.org/entity/Q30497640

about

Molecules that target nucleophosmin for cancer treatment: an update Protective effects and mechanisms of sirtuins in the nervous system Human AP endonuclease 1: a potential marker for the prediction of environmental carcinogenesis risk Emerging roles of the nucleolus in regulating the DNA damage response: the noncanonical DNA repair enzyme APE1/Ref-1 as a paradigmatical example Base Excision Repair, a Pathway Regulated by Posttranslational Modifications Nucleolar accumulation of APE1 depends on charged lysine residues that undergo acetylation upon genotoxic stress and modulate its BER activity in cells Ubiquitination of human AP-endonuclease 1 (APE1) enhanced by T233E substitution and by CDK5.Nucleophosmin modulates stability, activity, and nucleolar accumulation of base excision repair proteins.APE1/Ref-1 as an emerging therapeutic target for various human diseases: phytochemical modulation of its functions Nucleolin and nucleophosmin: nucleolar proteins with multiple functions in DNA repair.Knock-in reconstitution studies reveal an unexpected role of Cys-65 in regulating APE1/Ref-1 subcellular trafficking and function Identification of inhibitors of biological interactions involving intrinsically disordered proteins.Inhibitors of the apurinic/apyrimidinic endonuclease 1 (APE1)/nucleophosmin (NPM1) interaction that display anti-tumor properties Monoclonal antibodies against pools of mono- and polyacetylated peptides selectively recognize acetylated lysines within the context of the original antigen Molecular cloning and 3D structure modeling of APEX1, DNA base excision repair enzyme from the Camel, Camelus dromedarius Regulation of limited N-terminal proteolysis of APE1 in tumor via acetylation and its role in cell proliferation.APE1 polymorphic variants cause persistent genomic stress and affect cancer cell proliferation.Coordination of MYH DNA glycosylase and APE1 endonuclease activities via physical interactions.Human apurinic/apyrimidinic endonuclease 1.SIRT1 gene expression upon genotoxic damage is regulated by APE1 through nCaRE-promoter elements.Oxidized base damage and single-strand break repair in mammalian genomes: role of disordered regions and posttranslational modifications in early enzymes.A review on protein-protein interaction network of APE1/Ref-1 and its associated biological functions.BERing the burden of damage: Pathway crosstalk and posttranslational modification of base excision repair proteins regulate DNA damage management.Sirt1 in cerebral ischemia.Human Apurinic/Apyrimidinic Endonuclease (APE1) Is Acetylated at DNA Damage Sites in Chromatin, and Acetylation Modulates Its DNA Repair Activity.The prion protein is critical for DNA repair and cell survival after genotoxic stress.Crosstalk between the nucleolus and the DNA damage response.Functional regulation of the apurinic/apyrimidinic endonuclease 1 by nucleophosmin: impact on tumor biology.Structural investigation of nucleophosmin interaction with the tumor suppressor Fbw7γ.Mammalian APE1 controls miRNA processing and its interactome is linked to cancer RNA metabolism.Role of the unstructured N-terminal domain of the hAPE1 (human apurinic/apyrimidinic endonuclease 1) in the modulation of its interaction with nucleic acids and NPM1 (nucleophosmin).Nol12 is a multifunctional RNA binding protein at the nexus of RNA and DNA metabolism.Abasic and oxidized ribonucleotides embedded in DNA are processed by human APE1 and not by RNase H2.CREBBP and p300 lysine acetyl transferases in the DNA damage response.Polyubiquitination of apurinic/apyrimidinic endonuclease 1 by Parkin.Effect of estrogens on base excision repair in brain and liver mitochondria of aged female rats.

P2860

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P2860

Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions.

http://www.wikidata.org/entity/Q30497640

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Critical lysine residues withi ...... late its biological functions.

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Critical lysine residues withi ...... late its biological functions.

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type

label

Critical lysine residues withi ...... late its biological functions.

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Critical lysine residues withi ...... late its biological functions.

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Critical lysine residues withi ...... late its biological functions.

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Critical lysine residues withi ...... late its biological functions.

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Nucleic Acids Research

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Critical lysine residues withi ...... ulate its biological functions

@en

P2093

Carlo Pedone

http://www.w3.org/2001/XMLSchema#string

Damiano Fantini

http://www.w3.org/2001/XMLSchema#string

Daniela Marasco

http://www.w3.org/2001/XMLSchema#string

Franco Quadrifoglio

http://www.w3.org/2001/XMLSchema#string

Laura Cesaratto

http://www.w3.org/2001/XMLSchema#string

Luigi Vitagliano

http://www.w3.org/2001/XMLSchema#string

Mattia Poletto

http://www.w3.org/2001/XMLSchema#string

Milena Romanello

http://www.w3.org/2001/XMLSchema#string

P2860

Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter

Nucleophosmin regulates the stability and transcriptional activity of p53

Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1).

Identification of Apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA

SIRT1 deacetylates APE1 and regulates cellular base excision repair

APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process.

The interaction between Ku antigen and REF1 protein mediates negative gene regulation by extracellular calcium

Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A

XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions

Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene

P304

8239-8256

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scholarly article

P356

10.1093/NAR/GKQ691

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P407

P433

22

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P478

38

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Chiara D'Ambrosio

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2010-08-10T00:00:00Z

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45603316

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20699270

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3001066

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