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  1. Article ; Online: Bi-allelic variants in RNF170 are associated with hereditary spastic paraplegia.

    Wagner, Matias / Osborn, Daniel P S / Gehweiler, Ina / Nagel, Maike / Ulmer, Ulrike / Bakhtiari, Somayeh / Amouri, Rim / Boostani, Reza / Hentati, Faycal / Hockley, Maryam M / Hölbling, Benedikt / Schwarzmayr, Thomas / Karimiani, Ehsan Ghayoor / Kernstock, Christoph / Maroofian, Reza / Müller-Felber, Wolfgang / Ozkan, Ege / Padilla-Lopez, Sergio / Reich, Selina /
    Reichbauer, Jennifer / Darvish, Hossein / Shahmohammadibeni, Neda / Tafakhori, Abbas / Vill, Katharina / Zuchner, Stephan / Kruer, Michael C / Winkelmann, Juliane / Jamshidi, Yalda / Schüle, Rebecca

    Nature communications

    2019  Volume 10, Issue 1, Page(s) 4790

    Abstract: Alterations of ... ...

    Abstract Alterations of Ca
    MeSH term(s) Adolescent ; Adult ; Animals ; Calcium/metabolism ; Cell Line, Tumor ; Child ; Child, Preschool ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum-Associated Degradation/genetics ; Female ; Fibroblasts/metabolism ; Gene Knockdown Techniques ; High-Throughput Nucleotide Sequencing ; Humans ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Male ; Middle Aged ; Neurons/metabolism ; Primary Cell Culture ; Signal Transduction ; Skin/cytology ; Spastic Paraplegia, Hereditary/genetics ; Spastic Paraplegia, Hereditary/metabolism ; Ubiquitin-Protein Ligases/genetics ; Zebrafish
    Chemical Substances Inositol 1,4,5-Trisphosphate Receptors ; Inositol 1,4,5-Trisphosphate (85166-31-0) ; RNF170 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2019-10-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-019-12620-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. 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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