Literature DB >> 30743180

Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases.

Nicholas J Porter1, David W Christianson2.   

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Year:  2019        PMID： 30743180      PMCID： PMC6687579          DOI： 10.1016/j.sbi.2019.01.004

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN： 0959-440X            Impact factor:   6.809


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  71 in total

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6.  Molecular Basis for the Selective Inhibition of Histone Deacetylase 6 by a Mercaptoacetamide Inhibitor.

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Authors:  A Lahm; C Paolini; M Pallaoro; M C Nardi; P Jones; P Neddermann; S Sambucini; M J Bottomley; P Lo Surdo; A Carfí; U Koch; R De Francesco; C Steinkühler; P Gallinari
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Review 9.  The growing landscape of lysine acetylation links metabolism and cell signalling.

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2.  Binding of inhibitors to active-site mutants of CD1, the enigmatic catalytic domain of histone deacetylase 6.

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5.  Analyzing the Effects of HDAC Inhibitors on DNA Damage and Associated Cytotoxicity in Primary Hepatocytes.

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Review 6.  Structural determinants of affinity and selectivity in the binding of inhibitors to histone deacetylase 6.

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7.  Exploring Structural Determinants of Inhibitor Affinity and Selectivity in Complexes with Histone Deacetylase 6.

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8.  Structural Basis of Catalysis and Inhibition of HDAC6 CD1, the Enigmatic Catalytic Domain of Histone Deacetylase 6.

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9.  OleD Loki as a Catalyst for Hydroxamate Glycosylation.

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10.  Unique Molecular Interaction with the Histone Deacetylase 6 Catalytic Tunnel: Crystallographic and Biological Characterization of a Model Chemotype.

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Journal:  J Med Chem       Date:  2021-02-12       Impact factor: 7.446
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