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  • 1
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    HDACs link the DNA damage response, processing of double-strand breaks and autophagy (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-03-04
    Description: Protein acetylation is mediated by histone acetyltransferases (HATs) and deacetylases (HDACs), which influence chromatin dynamics, protein turnover and the DNA damage response. ATM and ATR mediate DNA damage checkpoints by sensing double-strand breaks and single-strand-DNA-RFA nucleofilaments, respectively. However, it is unclear how acetylation modulates the DNA damage response. Here we show that HDAC inhibition/ablation specifically counteracts yeast Mec1 (orthologue of human ATR) activation, double-strand-break processing and single-strand-DNA-RFA nucleofilament formation. Moreover, the recombination protein Sae2 (human CtIP) is acetylated and degraded after HDAC inhibition. Two HDACs, Hda1 and Rpd3, and one HAT, Gcn5, have key roles in these processes. We also find that HDAC inhibition triggers Sae2 degradation by promoting autophagy that affects the DNA damage sensitivity of hda1 and rpd3 mutants. Rapamycin, which stimulates autophagy by inhibiting Tor, also causes Sae2 degradation. We propose that Rpd3, Hda1 and Gcn5 control chromosome stability by coordinating the ATR checkpoint and double-strand-break processing with autophagy.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3935290/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3935290/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robert, Thomas -- Vanoli, Fabio -- Chiolo, Irene -- Shubassi, Ghadeer -- Bernstein, Kara A -- Rothstein, Rodney -- Botrugno, Oronza A -- Parazzoli, Dario -- Oldani, Amanda -- Minucci, Saverio -- Foiani, Marco -- GGP08066/Telethon/Italy -- GM088413/GM/NIGMS NIH HHS/ -- GM50237/GM/NIGMS NIH HHS/ -- GM67055/GM/NIGMS NIH HHS/ -- K99 GM088413/GM/NIGMS NIH HHS/ -- R00 GM088413/GM/NIGMS NIH HHS/ -- R01 GM050237/GM/NIGMS NIH HHS/ -- R01 GM067055/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Mar 3;471(7336):74-9. doi: 10.1038/nature09803.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fondazione IFOM (Istituto FIRC di Oncologia Molecolare), IFOM-IEO Campus, via Adamello 16, Milan 20139, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21368826" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation/drug effects ; Aminopeptidases/metabolism ; *Autophagy/drug effects ; Chromosomal Instability ; *DNA Breaks, Double-Stranded/drug effects ; DNA Repair/drug effects ; Endodeoxyribonucleases/metabolism ; Endonucleases/chemistry/metabolism ; Exodeoxyribonucleases/metabolism ; Histone Acetyltransferases/metabolism ; Histone Deacetylase Inhibitors/pharmacology ; Histone Deacetylases/genetics/*metabolism ; Intracellular Signaling Peptides and Proteins/antagonists & inhibitors/metabolism ; Microtubule-Associated Proteins/metabolism ; Protein Kinases/genetics ; Protein Processing, Post-Translational/drug effects ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; *Saccharomyces cerevisiae/cytology/enzymology/genetics ; Saccharomyces cerevisiae Proteins/antagonists & ; inhibitors/chemistry/genetics/metabolism ; Signal Transduction/drug effects ; Valproic Acid/pharmacology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    A gut-vascular barrier controls the systemic dissemination of bacteria (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-11-14
    Description: In healthy individuals, the intestinal microbiota cannot access the liver, spleen, or other peripheral tissues. Some pathogenic bacteria can reach these sites, however, and can induce a systemic immune response. How such compartmentalization is achieved is unknown. We identify a gut-vascular barrier (GVB) in mice and humans that controls the translocation of antigens into the blood stream and prohibits entry of the microbiota. Salmonella typhimurium can penetrate the GVB in a manner dependent on its pathogenicity island (Spi) 2-encoded type III secretion system and on decreased beta-catenin-dependent signaling in gut endothelial cells. The GVB is modified in celiac disease patients with elevated serum transaminases, which indicates that GVB dismantling may be responsible for liver damage in these patients. Understanding the GVB may provide new insights into the regulation of the gut-liver axis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spadoni, Ilaria -- Zagato, Elena -- Bertocchi, Alice -- Paolinelli, Roberta -- Hot, Edina -- Di Sabatino, Antonio -- Caprioli, Flavio -- Bottiglieri, Luca -- Oldani, Amanda -- Viale, Giuseppe -- Penna, Giuseppe -- Dejana, Elisabetta -- Rescigno, Maria -- New York, N.Y. -- Science. 2015 Nov 13;350(6262):830-4. doi: 10.1126/science.aad0135.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Oncology, European Institute of Oncology, Milan, Italy. ; The Italian Foundation for Cancer Research (FIRC) Institute of Molecular Oncology (IFOM), Milan, Italy. ; First Department of Medicine, St. Matteo Hospital, University of Pavia, Pavia, Italy. ; Unita Operativa Gastroenterologia ed Endoscopia, Fondazione IRCCS Ca Granda, Ospedale Maggiore Policlinico di Milano, and Dipartimento di Fisiopatologia Medico-Chirurgica e dei Trapianti, Universita degli Studi di Milano, Milan, Italy. ; Department of Pathology and Laboratory Medicine, European Institute of Oncology, Milan, Italy. ; The Italian Foundation for Cancer Research (FIRC) Institute of Molecular Oncology (IFOM), Milan, Italy. Department of Biosciences, Universita degli Studi di Milano, Italy. Department of Genetics, Immunology and Pathology, Uppsala University, Uppsala, Sweden. ; Department of Experimental Oncology, European Institute of Oncology, Milan, Italy. Department of Biosciences, Universita degli Studi di Milano, Italy. maria.rescigno@ieo.eu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26564856" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Bacterial/blood/immunology ; Capillary Permeability/*immunology ; Celiac Disease/blood/immunology/microbiology ; Genomic Islands/genetics/immunology ; Humans ; Ileum/blood supply/immunology/microbiology ; Intestinal Mucosa/immunology/microbiology ; Intestines/blood supply/*immunology/*microbiology ; Liver/immunology ; Mice ; Mice, Inbred C57BL ; Microbiota/*immunology ; Salmonella Infections/*immunology ; Salmonella typhimurium/genetics/*immunology/pathogenicity ; Signal Transduction ; Spleen/immunology ; Transaminases/blood ; Type III Secretion Systems/genetics/immunology ; Wnt Signaling Pathway ; beta Catenin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Small GTPase Rab5 participates in chromosome congression and regulates localization of the centromere-associated protein CENP-F to kinetochores (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-10-10
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 4
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    Small GTPase Rab5 participates in chromosome congression and regulates localization of the centromere-associated protein CENP-F to kinetochores [Cell Biology] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-10-19
    Description: Rab5 is a small GTPase known to regulate vesicular trafficking during interphase. Here, we show that Rab5 also plays an unexpected role during mitotic progression. RNAi-mediated silencing of Rab5 caused defects in chromosome congression and extensive prometaphase delay, and it correlated with a severe reduction in the localization of the centromere-associated protein CENP-F to kinetochores. CENP-F is a component of the nuclear matrix required for chromosome congression that, at mitotic entry, localizes to the nuclear envelope and assembles on kinetochores, contributing to the establishment of kinetochore microtubule interactions. We found that Rab5 forms a complex with a subset of CENP-F in mitotic cells and regulates the kinetics of release of CENP-F from the nuclear envelope and its accumulation on kinetochores. Simultaneous depletion of both Rab5 and CENP-F recapitulated the mitotic defects caused by silencing of either Rab5 or CENP-F alone, indicating epistatic roles for these two proteins in the pathway that orchestrates chromosome congression. These results reveal the involvement of Rab5 in the proper execution of mitotic programs whose deregulation can undermine chromosomal stability.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 5
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    Excited state hydrogen transfer dynamics in substituted phenols and their complexes with ammonia: ππ∗-πσ∗ energy gap propensity and ortho-substitution effect (2010)
    American Institute of Physics
    Details
    Publication Date: 2010-09-28
    Print ISSN: 0021-9606
    Electronic ISSN: 1089-7690
    Topics: Chemistry and Pharmacology , Physics
    Published by American Institute of Physics
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