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  1. AU="Debarnot, Cecilé"
  2. AU="Thomas, Sophie"
  3. AU=Steyer Terence E AU=Steyer Terence E
  4. AU="Retrouvey, Jean-Marc"
  5. AU="Crecchio, Carmine"
  6. AU=Moll Philip J. W.
  7. AU="Coombs, Catherine C"
  8. AU="Safaei, Naser"
  9. AU="Bachouche, Imene"
  10. AU="Roignant, Jean-Yves"
  11. AU="Thabet, Nagwa"
  12. AU="Asor, Eyal"
  13. AU="Rahaman, Md Hasibur"
  14. AU="Angela Di Capua"
  15. AU=De Vitis R
  16. AU="Young, Kaelin C"

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  1. Artikel ; Online: The catalytic domain of free or ligand bound histone deacetylase 4 occurs in solution predominantly in closed conformation.

    Schweipert, Markus / Nehls, Thomas / Frühauf, Anton / Debarnot, Cecilé / Kumar, Adarsh / Knapp, Stefan / Lermyte, Frederik / Meyer-Almes, Franz-Josef

    Protein science : a publication of the Protein Society

    2024  Band 33, Heft 3, Seite(n) e4917

    Abstract: Human histone deacetylase 4 (HDAC4) is a key epigenetic regulator involved in a number of important cellular processes. This makes HDAC4 a promising target for the treatment of several cancers and neurodegenerative diseases, in particular Huntington's ... ...

    Abstract Human histone deacetylase 4 (HDAC4) is a key epigenetic regulator involved in a number of important cellular processes. This makes HDAC4 a promising target for the treatment of several cancers and neurodegenerative diseases, in particular Huntington's disease. HDAC4 is highly regulated by phosphorylation and oxidation, which determine its nuclear or cytosolic localization, and exerts its function through multiple interactions with other proteins, forming multiprotein complexes of varying composition. The catalytic domain of HDAC4 is known to interact with the SMRT/NCOR corepressor complex when the structural zinc-binding domain (sZBD) is intact and forms a closed conformation. Crystal structures of the HDAC4 catalytic domain have been reported showing an open conformation of HDAC4 when bound to certain ligands. Here, we investigated the relevance of this HDAC4 conformation under physiological conditions in solution. We show that proper zinc chelation in the sZBD is essential for enzyme function. Loss of the structural zinc ion not only leads to a massive decrease in enzyme activity, but it also has serious consequences for the overall structural integrity and stability of the protein. However, the Zn
    Mesh-Begriff(e) Humans ; Catalytic Domain ; Ligands ; Phosphorylation ; Histone Deacetylases/chemistry ; Zinc
    Chemische Substanzen Ligands ; Histone Deacetylases (EC 3.5.1.98) ; Zinc (J41CSQ7QDS)
    Sprache Englisch
    Erscheinungsdatum 2024-02-12
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.4917
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Design, Synthesis, and Biological Evaluation of Novel Quinazolin-4(3H)-One-Based Histone Deacetylase 6 (HDAC6) Inhibitors for Anticancer Activity.

    Khetmalis, Yogesh Mahadu / Fathima, Ashna / Schweipert, Markus / Debarnot, Cécile / Bandaru, Naga Venkata Madhusudhan Rao / Murugesan, Sankaranarayanan / Jamma, Trinath / Meyer-Almes, Franz-Josef / Sekhar, Kondapalli Venkata Gowri Chandra

    International journal of molecular sciences

    2023  Band 24, Heft 13

    Abstract: A series of novel quinazoline-4-(3H)-one derivatives were designed and synthesized as histone deacetylase 6 (HDAC6) inhibitors based on novel quinazoline-4-(3H)-one as the cap group and benzhydroxamic acid as the linker and metal-binding group. A total ... ...

    Abstract A series of novel quinazoline-4-(3H)-one derivatives were designed and synthesized as histone deacetylase 6 (HDAC6) inhibitors based on novel quinazoline-4-(3H)-one as the cap group and benzhydroxamic acid as the linker and metal-binding group. A total of 19 novel quinazoline-4-(3H)-one analogues (
    Mesh-Begriff(e) Histone Deacetylase 6/metabolism ; Structure-Activity Relationship ; Antineoplastic Agents/chemistry ; Cell Line, Tumor ; Quinazolines/pharmacology ; Quinazolines/chemistry ; Histone Deacetylase Inhibitors/chemistry ; Cell Proliferation ; Molecular Structure ; Histone Deacetylase 1/metabolism
    Chemische Substanzen Histone Deacetylase 6 (EC 3.5.1.98) ; Antineoplastic Agents ; Quinazolines ; Histone Deacetylase Inhibitors ; Histone Deacetylase 1 (EC 3.5.1.98)
    Sprache Englisch
    Erscheinungsdatum 2023-07-03
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241311044
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: 3-Chloro-5-Substituted-1,2,4-Thiadiazoles (TDZs) as Selective and Efficient Protein Thiol Modifiers.

    Jänsch, Niklas / Frühauf, Anton / Schweipert, Markus / Debarnot, Cécile / Erhardt, Miriam / Brenner-Weiss, Gerald / Kirschhöfer, Frank / Jasionis, Tomas / Čapkauskaitė, Edita / Zubrienė, Asta / Matulis, Daumantas / Meyer-Almes, Franz-Josef

    Chembiochem : a European journal of chemical biology

    2022  Band 23, Heft 21, Seite(n) e202200417

    Abstract: The study of cysteine modifications has gained much attention in recent years. This includes detailed investigations in the field of redox biology with focus on numerous redox derivatives like nitrosothiols, sulfenic acids, sulfinic acids and sulfonic ... ...

    Abstract The study of cysteine modifications has gained much attention in recent years. This includes detailed investigations in the field of redox biology with focus on numerous redox derivatives like nitrosothiols, sulfenic acids, sulfinic acids and sulfonic acids resulting from increasing oxidation, S-lipidation, and perthiols. For these studies selective and rapid blocking of free protein thiols is required to prevent disulfide rearrangement. In our attempt to find new inhibitors of human histone deacetylase 8 (HDAC8) we discovered 5-sulfonyl and 5-sulfinyl substituted 1,2,4-thiadiazoles (TDZ), which surprisingly show an outstanding reactivity against thiols in aqueous solution. Encouraged by these observations we investigated the mechanism of action in detail and show that these compounds react more specifically and faster than commonly used N-ethyl maleimide, making them superior alternatives for efficient blocking of free thiols in proteins. We show that 5-sulfonyl-TDZ can be readily applied in commonly used biotin switch assays. Using the example of human HDAC8, we demonstrate that cysteine modification by a 5-sulfonyl-TDZ is easily measurable using quantitative HPLC/ESI-QTOF-MS/MS, and allows for the simultaneous measurement of the modification kinetics of seven solvent-accessible cysteines in HDAC8.
    Mesh-Begriff(e) Humans ; Sulfhydryl Compounds ; Cysteine/metabolism ; Thiadiazoles/pharmacology ; Tandem Mass Spectrometry ; Sulfenic Acids ; Oxidation-Reduction ; Histone Deacetylases/metabolism ; Repressor Proteins/metabolism
    Chemische Substanzen Sulfhydryl Compounds ; Cysteine (K848JZ4886) ; Thiadiazoles ; Sulfenic Acids ; HDAC8 protein, human (EC 3.5.1.98) ; Histone Deacetylases (EC 3.5.1.98) ; Repressor Proteins
    Sprache Englisch
    Erscheinungsdatum 2022-09-27
    Erscheinungsland Germany
    Dokumenttyp Journal Article
    ZDB-ID 2020469-3
    ISSN 1439-7633 ; 1439-4227
    ISSN (online) 1439-7633
    ISSN 1439-4227
    DOI 10.1002/cbic.202200417
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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