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  1. Article: Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response

    Tallis, Michael / Morra, Rosa / Barkauskaite, Eva / Ahel, Ivan

    Chromosoma. 2014 Mar., v. 123, no. 1-2

    2014  

    Abstract: Poly(ADP-ribose) (PAR) is a post-translational modification of proteins and is synthesised by PAR polymerases (PARPs), which have long been associated with the coordination of the cellular response to DNA damage, amongst other processes. Binding of some ... ...

    Abstract Poly(ADP-ribose) (PAR) is a post-translational modification of proteins and is synthesised by PAR polymerases (PARPs), which have long been associated with the coordination of the cellular response to DNA damage, amongst other processes. Binding of some PARPs such as PARP1 to broken DNA induces a substantial wave of PARylation, which results in significant re-structuring of the chromatin microenvironment through modification of chromatin-associated proteins and recruitment of chromatin-modifying proteins. Similarly, other DNA damage response proteins are recruited to the damaged sites via PAR-specific binding modules, and in this way, PAR mediates not only local chromatin architecture but also DNA repair. Here, we discuss the expanding role of PAR in the DNA damage response, with particular focus on chromatin regulation.
    Keywords DNA ; DNA damage ; DNA repair ; chromatin ; photosynthetically active radiation ; post-translational modification
    Language English
    Dates of publication 2014-03
    Size p. 79-90.
    Publishing place Springer-Verlag
    Document type Article
    ZDB-ID 203083-4
    ISSN 1432-0886 ; 0009-5915
    ISSN (online) 1432-0886
    ISSN 0009-5915
    DOI 10.1007/s00412-013-0442-9
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 46/355: Show issues

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  2. Article ; Online: Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response.

    Tallis, Michael / Morra, Rosa / Barkauskaite, Eva / Ahel, Ivan

    Chromosoma

    2013  Volume 123, Issue 1-2, Page(s) 79–90

    Abstract: Poly(ADP-ribose) (PAR) is a post-translational modification of proteins and is synthesised by PAR polymerases (PARPs), which have long been associated with the coordination of the cellular response to DNA damage, amongst other processes. Binding of some ... ...

    Abstract Poly(ADP-ribose) (PAR) is a post-translational modification of proteins and is synthesised by PAR polymerases (PARPs), which have long been associated with the coordination of the cellular response to DNA damage, amongst other processes. Binding of some PARPs such as PARP1 to broken DNA induces a substantial wave of PARylation, which results in significant re-structuring of the chromatin microenvironment through modification of chromatin-associated proteins and recruitment of chromatin-modifying proteins. Similarly, other DNA damage response proteins are recruited to the damaged sites via PAR-specific binding modules, and in this way, PAR mediates not only local chromatin architecture but also DNA repair. Here, we discuss the expanding role of PAR in the DNA damage response, with particular focus on chromatin regulation.
    MeSH term(s) Animals ; Apoptosis/genetics ; Chromatin/chemistry ; Chromatin/metabolism ; DNA Damage/genetics ; DNA Repair/genetics ; Humans ; Poly Adenosine Diphosphate Ribose/metabolism ; Poly(ADP-ribose) Polymerases/metabolism
    Chemical Substances Chromatin ; Poly Adenosine Diphosphate Ribose (26656-46-2) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
    Language English
    Publishing date 2013-10-27
    Publishing country Austria
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 203083-4
    ISSN 1432-0886 ; 0009-5915
    ISSN (online) 1432-0886
    ISSN 0009-5915
    DOI 10.1007/s00412-013-0442-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ub I Zs.94/5: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease.

    Sharifi, Reza / Morra, Rosa / Appel, C Denise / Tallis, Michael / Chioza, Barry / Jankevicius, Gytis / Simpson, Michael A / Matic, Ivan / Ozkan, Ege / Golia, Barbara / Schellenberg, Matthew J / Weston, Ria / Williams, Jason G / Rossi, Marianna N / Galehdari, Hamid / Krahn, Juno / Wan, Alexander / Trembath, Richard C / Crosby, Andrew H /
    Ahel, Dragana / Hay, Ron / Ladurner, Andreas G / Timinszky, Gyula / Williams, R Scott / Ahel, Ivan

    The EMBO journal

    2013  Volume 32, Issue 9, Page(s) 1225–1237

    Abstract: Adenosine diphosphate (ADP)-ribosylation is a post-translational protein modification implicated in the regulation of a range of cellular processes. A family of proteins that catalyse ADP-ribosylation reactions are the poly(ADP-ribose) (PAR) polymerases ( ...

    Abstract Adenosine diphosphate (ADP)-ribosylation is a post-translational protein modification implicated in the regulation of a range of cellular processes. A family of proteins that catalyse ADP-ribosylation reactions are the poly(ADP-ribose) (PAR) polymerases (PARPs). PARPs covalently attach an ADP-ribose nucleotide to target proteins and some PARP family members can subsequently add additional ADP-ribose units to generate a PAR chain. The hydrolysis of PAR chains is catalysed by PAR glycohydrolase (PARG). PARG is unable to cleave the mono(ADP-ribose) unit directly linked to the protein and although the enzymatic activity that catalyses this reaction has been detected in mammalian cell extracts, the protein(s) responsible remain unknown. Here, we report the homozygous mutation of the c6orf130 gene in patients with severe neurodegeneration, and identify C6orf130 as a PARP-interacting protein that removes mono(ADP-ribosyl)ation on glutamate amino acid residues in PARP-modified proteins. X-ray structures and biochemical analysis of C6orf130 suggest a mechanism of catalytic reversal involving a transient C6orf130 lysyl-(ADP-ribose) intermediate. Furthermore, depletion of C6orf130 protein in cells leads to proliferation and DNA repair defects. Collectively, our data suggest that C6orf130 enzymatic activity has a role in the turnover and recycling of protein ADP-ribosylation, and we have implicated the importance of this protein in supporting normal cellular function in humans.
    MeSH term(s) Amino Acid Sequence ; Base Sequence ; Cells, Cultured ; Child ; Child, Preschool ; Family ; Female ; Glycoside Hydrolases/genetics ; Glycoside Hydrolases/physiology ; HEK293 Cells ; HeLa Cells ; Humans ; Male ; Models, Molecular ; Molecular Sequence Data ; Neurodegenerative Diseases/enzymology ; Neurodegenerative Diseases/genetics ; Pedigree ; Poly Adenosine Diphosphate Ribose/genetics ; Poly Adenosine Diphosphate Ribose/physiology ; Protein Processing, Post-Translational/genetics ; Sequence Homology, Amino Acid ; Thiolester Hydrolases/genetics ; Thiolester Hydrolases/physiology
    Chemical Substances Poly Adenosine Diphosphate Ribose (26656-46-2) ; OARD1 protein, human (EC 3.1.2.-) ; Thiolester Hydrolases (EC 3.1.2.-) ; Glycoside Hydrolases (EC 3.2.1.-)
    Language English
    Publishing date 2013-03-12
    Publishing country England
    Document type Case Reports ; Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/emboj.2013.51
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 100: Show issues

    Order via subito

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  4. Article: Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response

    Tallis, Michael / Morra, Rosa / Barkauskaite, Eva / Ahel, Ivan

    Chromosoma

    Volume v. 123,, Issue no. 1

    Abstract: Poly(ADP-ribose) (PAR) is a post-translational modification of proteins and is synthesised by PAR polymerases (PARPs), which have long been associated with the coordination of the cellular response to DNA damage, amongst other processes. Binding of some ... ...

    Abstract Poly(ADP-ribose) (PAR) is a post-translational modification of proteins and is synthesised by PAR polymerases (PARPs), which have long been associated with the coordination of the cellular response to DNA damage, amongst other processes. Binding of some PARPs such as PARP1 to broken DNA induces a substantial wave of PARylation, which results in significant re-structuring of the chromatin microenvironment through modification of chromatin-associated proteins and recruitment of chromatin-modifying proteins. Similarly, other DNA damage response proteins are recruited to the damaged sites via PAR-specific binding modules, and in this way, PAR mediates not only local chromatin architecture but also DNA repair. Here, we discuss the expanding role of PAR in the DNA damage response, with particular focus on chromatin regulation.
    Keywords DNA damage ; DNA ; post-translational modification ; photosynthetically active radiation ; DNA repair ; chromatin
    Language English
    Document type Article
    ISSN 0009-5915
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

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