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  1. Book ; Online ; Thesis: Charakterisierung der physiologischen Funktion von Parkin im Zellkultur- und Maus-Modell

    Schlierf, Anita

    2010  

    Author's details Anita Schlierf
    Language German
    Size Online-Ressource
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss.--München, 2010
    Database Special collection on veterinary medicine and general parasitology

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  2. Book ; Online ; Thesis: Charakterisierung der physiologischen Funktion von Parkin im Zellkultur- und Maus-Modell

    Schlierf, Anita

    2010  

    Author's details Anita Schlierf
    Language German
    Size Online-Ressource
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss.--München, 2010
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  3. Book ; Online ; Thesis: Charakterisierung der physiologischen Funktion von Parkin im Zellkultur- und Maus-Modell

    Schlierf, Anita [Verfasser]

    2010  

    Author's details Anita Schlierf
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  4. Article ; Online: The

    Meschede, Jens / Šadić, Maria / Furthmann, Nikolas / Miedema, Tim / Sehr, Dominik A / Müller-Rischart, A Kathrin / Bader, Verian / Berlemann, Lena A / Pilsl, Anna / Schlierf, Anita / Barkovits, Katalin / Kachholz, Barbara / Rittinger, Katrin / Ikeda, Fumiyo / Marcus, Katrin / Schaefer, Liliana / Tatzelt, Jörg / Winklhofer, Konstanze F

    Science signaling

    2020  Volume 13, Issue 617

    Abstract: ... ...

    Abstract The
    MeSH term(s) Animals ; Cell Line, Tumor ; Cells, Cultured ; HEK293 Cells ; HeLa Cells ; Humans ; Mice, Knockout ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Mitophagy/genetics ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; NF-kappa B/metabolism ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Signal Transduction ; Tumor Necrosis Factor-alpha/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances Microfilament Proteins ; Molecular Chaperones ; NF-kappa B ; Nerve Tissue Proteins ; PACRG protein, human ; Tumor Necrosis Factor-alpha ; sharpin ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2020-02-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2417226-1
    ISSN 1937-9145 ; 1945-0877
    ISSN (online) 1937-9145
    ISSN 1945-0877
    DOI 10.1126/scisignal.aav1256
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: A CARD10-Dependent Tonic Signalosome Activates MALT1 Paracaspase and Regulates IL-17/TNF-α-Driven Keratinocyte Inflammation.

    Israël, Laura / Bardet, Maureen / Huppertz, Antje / Mercado, Nicolas / Ginster, Stefanie / Unterreiner, Adeline / Schlierf, Anita / Goetschy, Jean François / Zerwes, Hans-Günter / Roth, Lukas / Kolbinger, Frank / Bornancin, Frédéric

    The Journal of investigative dermatology

    2018  Volume 138, Issue 9, Page(s) 2075–2079

    MeSH term(s) CARD Signaling Adaptor Proteins/biosynthesis ; CARD Signaling Adaptor Proteins/genetics ; Gene Expression Regulation ; Humans ; Inflammation/genetics ; Inflammation/metabolism ; Inflammation/pathology ; Interleukin-17/biosynthesis ; Interleukin-17/genetics ; Keratinocytes/metabolism ; Keratinocytes/pathology ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein/biosynthesis ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein/genetics ; RNA/genetics ; Tumor Necrosis Factor-alpha/biosynthesis ; Tumor Necrosis Factor-alpha/genetics
    Chemical Substances CARD Signaling Adaptor Proteins ; CARD10 protein, human ; Interleukin-17 ; Tumor Necrosis Factor-alpha ; RNA (63231-63-0) ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein (EC 3.4.22.-)
    Language English
    Publishing date 2018-03-20
    Publishing country United States
    Document type Letter
    ZDB-ID 80136-7
    ISSN 1523-1747 ; 0022-202X
    ISSN (online) 1523-1747
    ISSN 0022-202X
    DOI 10.1016/j.jid.2018.03.1503
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Targeted inhibition of the COP9 signalosome for treatment of cancer.

    Schlierf, Anita / Altmann, Eva / Quancard, Jean / Jefferson, Anne B / Assenberg, René / Renatus, Martin / Jones, Matthew / Hassiepen, Ulrich / Schaefer, Michael / Kiffe, Michael / Weiss, Andreas / Wiesmann, Christian / Sedrani, Richard / Eder, Jörg / Martoglio, Bruno

    Nature communications

    2016  Volume 7, Page(s) 13166

    Abstract: The COP9 signalosome (CSN) is a central component of the activation and remodelling cycle of cullin-RING E3 ubiquitin ligases (CRLs), the largest enzyme family of the ubiquitin-proteasome system in humans. CRLs are implicated in the regulation of ... ...

    Abstract The COP9 signalosome (CSN) is a central component of the activation and remodelling cycle of cullin-RING E3 ubiquitin ligases (CRLs), the largest enzyme family of the ubiquitin-proteasome system in humans. CRLs are implicated in the regulation of numerous cellular processes, including cell cycle progression and apoptosis, and aberrant CRL activity is frequently associated with cancer. Remodelling of CRLs is initiated by CSN-catalysed cleavage of the ubiquitin-like activator NEDD8 from CRLs. Here we describe CSN5i-3, a potent, selective and orally available inhibitor of CSN5, the proteolytic subunit of CSN. The compound traps CRLs in the neddylated state, which leads to inactivation of a subset of CRLs by inducing degradation of their substrate recognition module. CSN5i-3 differentially affects the viability of tumour cell lines and suppresses growth of a human xenograft in mice. Our results provide insights into how CSN regulates CRLs and suggest that CSN5 inhibition has potential for anti-tumour therapy.
    MeSH term(s) Animals ; Antineoplastic Agents/chemical synthesis ; Antineoplastic Agents/pharmacology ; Azepines/chemical synthesis ; Azepines/pharmacology ; COP9 Signalosome Complex/antagonists & inhibitors ; COP9 Signalosome Complex/genetics ; COP9 Signalosome Complex/metabolism ; Female ; Gene Expression Regulation, Neoplastic ; HCT116 Cells ; Humans ; Intracellular Signaling Peptides and Proteins/antagonists & inhibitors ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Lymphoma, Large-Cell, Anaplastic/drug therapy ; Lymphoma, Large-Cell, Anaplastic/genetics ; Lymphoma, Large-Cell, Anaplastic/metabolism ; Lymphoma, Large-Cell, Anaplastic/pathology ; Mice ; Mice, SCID ; Molecular Targeted Therapy ; NEDD8 Protein/genetics ; NEDD8 Protein/metabolism ; Peptide Hydrolases/genetics ; Peptide Hydrolases/metabolism ; Protein Processing, Post-Translational ; Proteolysis/drug effects ; Pyrazoles/chemical synthesis ; Pyrazoles/pharmacology ; THP-1 Cells ; Tumor Burden/drug effects ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Xenograft Model Antitumor Assays
    Chemical Substances Antineoplastic Agents ; Azepines ; Intracellular Signaling Peptides and Proteins ; Isoenzymes ; NEDD8 Protein ; NEDD8 protein, human ; Pyrazoles ; CULL-RING ligase, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Peptide Hydrolases (EC 3.4.-) ; COPS5 protein, human (EC 3.4.-.-) ; COP9 Signalosome Complex (EC 3.4.19.12)
    Language English
    Publishing date 2016-10-24
    Publishing country England
    Document type Journal Article
    ISSN 2041-1723
    ISSN (online) 2041-1723
    DOI 10.1038/ncomms13166
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Targeted inhibition of the COP9 signalosome for treatment of cancer

    Anita Schlierf / Eva Altmann / Jean Quancard / Anne B. Jefferson / René Assenberg / Martin Renatus / Matthew Jones / Ulrich Hassiepen / Michael Schaefer / Michael Kiffe / Andreas Weiss / Christian Wiesmann / Richard Sedrani / Jörg Eder / Bruno Martoglio

    Nature Communications, Vol 7, Iss 1, Pp 1-

    2016  Volume 10

    Abstract: Dysregulation of protein degradation by the ubiquitin-proteasome system is a feature commonly associated with cancer. Here, the authors develop an orally available small molecule that inhibits CSN5, the proteolytic subunit of the COP9 signalosome, and ... ...

    Abstract Dysregulation of protein degradation by the ubiquitin-proteasome system is a feature commonly associated with cancer. Here, the authors develop an orally available small molecule that inhibits CSN5, the proteolytic subunit of the COP9 signalosome, and blocks tumour growth in a xenograft model.
    Keywords Science ; Q
    Language English
    Publishing date 2016-10-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Azaindoles as Zinc-Binding Small-Molecule Inhibitors of the JAMM Protease CSN5.

    Altmann, Eva / Erbel, Paul / Renatus, Martin / Schaefer, Michael / Schlierf, Anita / Druet, Adelaide / Kieffer, Laurence / Sorge, Mickael / Pfister, Keith / Hassiepen, Ulrich / Jones, Matthew / Ruedisser, Simon / Ostermeier, Daniela / Martoglio, Bruno / Jefferson, Anne B / Quancard, Jean

    Angewandte Chemie (International ed. in English)

    2016  Volume 56, Issue 5, Page(s) 1294–1297

    Abstract: CSN5 is the zinc metalloprotease subunit of the COP9 signalosome (CSN), which is an important regulator of cullin-RING E3 ubiquitin ligases (CRLs). CSN5 is responsible for the cleavage of NEDD8 from CRLs, and blocking deconjugation of NEDD8 traps the ... ...

    Abstract CSN5 is the zinc metalloprotease subunit of the COP9 signalosome (CSN), which is an important regulator of cullin-RING E3 ubiquitin ligases (CRLs). CSN5 is responsible for the cleavage of NEDD8 from CRLs, and blocking deconjugation of NEDD8 traps the CRLs in a hyperactive state, thereby leading to auto-ubiquitination and ultimately degradation of the substrate recognition subunits. Herein, we describe the discovery of azaindoles as a new class of CSN5 inhibitors, which interact with the active-site zinc ion of CSN5 through an unprecedented binding mode. The best compounds inhibited CSN5 with nanomolar potency, led to degradation of the substrate recognition subunit Skp2 in cells, and reduced the viability of HCT116 cells.
    MeSH term(s) Binding Sites ; COP9 Signalosome Complex/antagonists & inhibitors ; COP9 Signalosome Complex/genetics ; COP9 Signalosome Complex/metabolism ; Catalytic Domain ; Cell Proliferation/drug effects ; Crystallography, X-Ray ; Fluorescence Resonance Energy Transfer ; HCT116 Cells ; Humans ; Indoles/chemistry ; Indoles/metabolism ; Indoles/pharmacology ; Molecular Docking Simulation ; NEDD8 Protein/chemistry ; NEDD8 Protein/metabolism ; Protein Subunits/antagonists & inhibitors ; Protein Subunits/genetics ; Protein Subunits/metabolism ; RNA Interference ; RNA, Small Interfering/metabolism ; S-Phase Kinase-Associated Proteins/chemistry ; S-Phase Kinase-Associated Proteins/metabolism ; Zinc/chemistry ; Zinc/metabolism
    Chemical Substances Indoles ; NEDD8 Protein ; NEDD8 protein, human ; Protein Subunits ; RNA, Small Interfering ; S-Phase Kinase-Associated Proteins ; SKP2 protein, human ; COP9 Signalosome Complex (EC 3.4.19.12) ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2016-12-16
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.201608672
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  9. Article ; Online: Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling.

    Henn, Iris H / Bouman, Lena / Schlehe, Julia S / Schlierf, Anita / Schramm, Julia E / Wegener, Elmar / Nakaso, Kazuhiro / Culmsee, Carsten / Berninger, Benedikt / Krappmann, Daniel / Tatzelt, Jörg / Winklhofer, Konstanze F

    The Journal of neuroscience : the official journal of the Society for Neuroscience

    2006  Volume 27, Issue 8, Page(s) 1868–1878

    Abstract: Mutations in the parkin gene are a major cause of autosomal recessive Parkinson's disease. Here we show that the E3 ubiquitin ligase parkin activates signaling through the IkappaB kinase (IKK)/nuclear factor kappaB (NF-kappaB) pathway. Our analysis ... ...

    Abstract Mutations in the parkin gene are a major cause of autosomal recessive Parkinson's disease. Here we show that the E3 ubiquitin ligase parkin activates signaling through the IkappaB kinase (IKK)/nuclear factor kappaB (NF-kappaB) pathway. Our analysis revealed that activation of this signaling cascade is causally linked to the neuroprotective potential of parkin. Inhibition of NF-kappaB activation by an IkappaB super-repressor or a kinase-inactive IKKbeta interferes with the neuroprotective activity of parkin. Furthermore, pathogenic parkin mutants with an impaired neuroprotective capacity show a reduced ability to stimulate NF-kappaB-dependent transcription. Finally, we present evidence that parkin interacts with and promotes degradation-independent ubiquitylation of IKKgamma/NEMO (NF-kappaB essential modifier) and TRAF2 [TNF (tumor necrosis factor) receptor-associated factor 2], two critical components of the NF-kappaB pathway. Thus, our results support a direct link between the neuroprotective activity of parkin and ubiquitin signaling in the IKK/NF-kappaB pathway.
    MeSH term(s) Animals ; Cell Survival/physiology ; Cells, Cultured ; Cytoprotection/physiology ; Enzyme Activation/physiology ; Humans ; I-kappa B Kinase/metabolism ; Mutation ; NF-kappa B/metabolism ; Neurons/physiology ; Rats ; Signal Transduction/physiology ; Stress, Physiological/metabolism ; TNF Receptor-Associated Factor 2/metabolism ; Transcription, Genetic/drug effects ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/biosynthesis ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/pharmacology ; Ubiquitin-Protein Ligases/physiology
    Chemical Substances NF-kappa B ; TNF Receptor-Associated Factor 2 ; Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; parkin protein (EC 2.3.2.27) ; I-kappa B Kinase (EC 2.7.11.10)
    Language English
    Publishing date 2006-05-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 604637-x
    ISSN 1529-2401 ; 0270-6474
    ISSN (online) 1529-2401
    ISSN 0270-6474
    DOI 10.1523/JNEUROSCI.5537-06.2007
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    Zs.A 1668: Show issues Location:
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  10. Article: SoxD proteins influence multiple stages of oligodendrocyte development and modulate SoxE protein function.

    Stolt, C Claus / Schlierf, Anita / Lommes, Petra / Hillgärtner, Simone / Werner, Torsten / Kosian, Thomas / Sock, Elisabeth / Kessaris, Nicoletta / Richardson, William D / Lefebvre, Veronique / Wegner, Michael

    Developmental cell

    2006  Volume 11, Issue 5, Page(s) 697–709

    Abstract: The myelin-forming oligodendrocytes are an excellent model to study transcriptional regulation of specification events, lineage progression, and terminal differentiation in the central nervous system. Here, we show that the group D Sox transcription ... ...

    Abstract The myelin-forming oligodendrocytes are an excellent model to study transcriptional regulation of specification events, lineage progression, and terminal differentiation in the central nervous system. Here, we show that the group D Sox transcription factors Sox5 and Sox6 jointly and cell-autonomously regulate several stages of oligodendrocyte development in the mouse spinal cord. They repress specification and terminal differentiation and influence migration patterns. As a consequence, oligodendrocyte precursors and terminally differentiating oligodendrocytes appear precociously in spinal cords deficient for both Sox proteins. Sox5 and Sox6 have opposite functions than the group E Sox proteins Sox9 and Sox10, which promote oligodendrocyte specification and terminal differentiation. Both genetic as well as molecular evidence suggests that Sox5 and Sox6 directly interfere with the function of group E Sox proteins. Our studies reveal a complex regulatory network between different groups of Sox proteins that is essential for proper progression of oligodendrocyte development.
    MeSH term(s) Animals ; Cell Differentiation ; Cell Lineage ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/physiology ; Gene Expression Regulation, Developmental ; High Mobility Group Proteins/genetics ; High Mobility Group Proteins/physiology ; Mice ; Mice, Knockout ; Mutation ; Myelin Sheath/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/physiology ; Oligodendroglia/cytology ; Oligodendroglia/physiology ; SOX9 Transcription Factor ; SOXD Transcription Factors ; SOXE Transcription Factors ; Spinal Cord/cytology ; Spinal Cord/embryology ; Spinal Cord/metabolism ; Transcription Factors/genetics ; Transcription Factors/physiology
    Chemical Substances DNA-Binding Proteins ; High Mobility Group Proteins ; Nuclear Proteins ; SOX9 Transcription Factor ; SOXD Transcription Factors ; SOXE Transcription Factors ; Sox10 protein, mouse ; Sox5 protein, mouse ; Sox6 protein, mouse ; Sox9 protein, mouse ; Transcription Factors
    Language English
    Publishing date 2006-11-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2006.08.011
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