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  1. Article: Structural Requirements of HDAC Inhibitors: SAHA Analogues Modified at the C2 Position Display HDAC6/8 Selectivity.

    Negmeldin, Ahmed T / Padige, Geetha / Bieliauskas, Anton V / Pflum, Mary Kay H

    ACS medicinal chemistry letters

    2017  Volume 8, Issue 3, Page(s) 281–286

    Abstract: Histone deacetylase (HDAC) proteins are epigenetic regulators that deacetylate protein substrates, leading to subsequent changes in cell function. HDAC proteins are implicated in cancers, and several HDAC inhibitors have been approved by the FDA as ... ...

    Abstract Histone deacetylase (HDAC) proteins are epigenetic regulators that deacetylate protein substrates, leading to subsequent changes in cell function. HDAC proteins are implicated in cancers, and several HDAC inhibitors have been approved by the FDA as anticancer drugs, including SAHA (suberoylanilide hydroxamic acid; Vorinostat and Zolinza). Unfortunately, SAHA inhibits most HDAC isoforms, which limits its use as a pharmacological tool and may lead to side effects in the clinic. In this work SAHA analogues substituted at the C2 position were synthesized and screened for HDAC isoform selectivity
    Language English
    Publishing date 2017-02-07
    Publishing country United States
    Document type Journal Article
    ISSN 1948-5875
    ISSN 1948-5875
    DOI 10.1021/acsmedchemlett.6b00124
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Structural Requirements of Histone Deacetylase Inhibitors: SAHA Analogs Modified on the Hydroxamic Acid.

    Bieliauskas, Anton V / Weerasinghe, Sujith V W / Negmeldin, Ahmed T / Pflum, Mary Kay H

    Archiv der Pharmazie

    2016  Volume 349, Issue 5, Page(s) 373–382

    Abstract: Histone deacetylase (HDAC) proteins have emerged as targets for anti-cancer therapeutics, with several inhibitors used in the clinic, including suberoylanilide hydroxamic acid (SAHA, vorinostat). Because SAHA and many other inhibitors target all or most ... ...

    Abstract Histone deacetylase (HDAC) proteins have emerged as targets for anti-cancer therapeutics, with several inhibitors used in the clinic, including suberoylanilide hydroxamic acid (SAHA, vorinostat). Because SAHA and many other inhibitors target all or most of the 11 human HDAC proteins, the creation of selective inhibitors has been studied intensely. Recently, inhibitors selective for HDAC1 and HDAC2 were reported where selectivity was attributed to interactions between substituents on the metal binding moiety of the inhibitor and residues in the 14-Å internal cavity of the HDAC enzyme structure. Based on this earlier work, we synthesized and tested SAHA analogs with substituents on the hydroxamic acid metal binding moiety. The N-substituted SAHA analogs displayed reduced potency and solubility, but greater selectivity, compared to SAHA. Docking studies suggested that the N-substituent accesses the 14-Å internal cavity to impart preferential inhibition of HDAC1. These studies with N-substituted SAHA analogs are consistent with the strategy exploiting the 14-Å internal cavity of HDAC proteins to create HDAC1/2 selective inhibitors.
    MeSH term(s) Dose-Response Relationship, Drug ; Histone Deacetylase 1/antagonists & inhibitors ; Histone Deacetylase 6 ; Histone Deacetylase Inhibitors/chemical synthesis ; Histone Deacetylase Inhibitors/chemistry ; Histone Deacetylase Inhibitors/pharmacology ; Histone Deacetylases/metabolism ; Humans ; Hydroxamic Acids/chemistry ; Hydroxamic Acids/pharmacology ; Molecular Docking Simulation ; Structure-Activity Relationship ; Vorinostat
    Chemical Substances Histone Deacetylase Inhibitors ; Hydroxamic Acids ; Vorinostat (58IFB293JI) ; HDAC1 protein, human (EC 3.5.1.98) ; HDAC6 protein, human (EC 3.5.1.98) ; Histone Deacetylase 1 (EC 3.5.1.98) ; Histone Deacetylase 6 (EC 3.5.1.98) ; Histone Deacetylases (EC 3.5.1.98) ; histone deacetylase 3 (EC 3.5.1.98)
    Language English
    Publishing date 2016-04-09
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 6381-2
    ISSN 1521-4184 ; 0365-6233 ; 1437-1014
    ISSN (online) 1521-4184
    ISSN 0365-6233 ; 1437-1014
    DOI 10.1002/ardp.201500472
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uf I Zs.4: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Article: Isoform-selective histone deacetylase inhibitors.

    Bieliauskas, Anton V / Pflum, Mary Kay H

    Chemical Society reviews

    2008  Volume 37, Issue 7, Page(s) 1402–1413

    Abstract: Histone deacetylase (HDAC) proteins are transcription regulators linked to cancer. As a result, multiple small molecule HDAC inhibitors are in various phases of clinical trials as anti-cancer drugs. The majority of HDAC inhibitors non-selectively ... ...

    Abstract Histone deacetylase (HDAC) proteins are transcription regulators linked to cancer. As a result, multiple small molecule HDAC inhibitors are in various phases of clinical trials as anti-cancer drugs. The majority of HDAC inhibitors non-selectively influence the activities of eleven human HDAC isoforms, which are divided into distinct classes. This tutorial review focuses on the recent progress toward the identification of class-selective and isoform-selective HDAC inhibitors. The emerging trends suggest that subtle differences in the active sites of the HDAC isoforms can be exploited to dictate selectivity.
    MeSH term(s) Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Binding Sites ; Cell Proliferation/drug effects ; Drug Design ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Histone Deacetylase Inhibitors ; Histone Deacetylases/chemistry ; Humans ; Hydroxamic Acids/pharmacology ; Protein Isoforms/antagonists & inhibitors ; Protein Isoforms/chemistry ; Tumor Cells, Cultured ; Vorinostat
    Chemical Substances Antineoplastic Agents ; Enzyme Inhibitors ; Histone Deacetylase Inhibitors ; Hydroxamic Acids ; Protein Isoforms ; trichostatin A (3X2S926L3Z) ; Vorinostat (58IFB293JI) ; Histone Deacetylases (EC 3.5.1.98)
    Language English
    Publishing date 2008-05-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1472875-8
    ISSN 1460-4744 ; 0306-0012
    ISSN (online) 1460-4744
    ISSN 0306-0012
    DOI 10.1039/b703830p
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Isoform-selective histone deacetylase inhibitors

    Bieliauskas, Anton V / Pflum, Mary Kay H

    Chemical Society reviews. 2008 June 23, v. 37, no. 7

    2008  

    Abstract: Histone deacetylase (HDAC) proteins are transcription regulators linked to cancer. As a result, multiple small molecule HDAC inhibitors are in various phases of clinical trials as anti-cancer drugs. The majority of HDAC inhibitors non-selectively ... ...

    Abstract Histone deacetylase (HDAC) proteins are transcription regulators linked to cancer. As a result, multiple small molecule HDAC inhibitors are in various phases of clinical trials as anti-cancer drugs. The majority of HDAC inhibitors non-selectively influence the activities of eleven human HDAC isoforms, which are divided into distinct classes. This tutorial review focuses on the recent progress toward the identification of class-selective and isoform-selective HDAC inhibitors. The emerging trends suggest that subtle differences in the active sites of the HDAC isoforms can be exploited to dictate selectivity.
    Keywords active sites ; antineoplastic agents ; clinical trials ; enzyme inhibitors ; histone deacetylase ; humans ; neoplasms ; transcription factors
    Language English
    Dates of publication 2008-0623
    Size p. 1402-1413.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472875-8
    ISSN 1460-4744 ; 0306-0012
    ISSN (online) 1460-4744
    ISSN 0306-0012
    DOI 10.1039/b703830p
    Database NAL-Catalogue (AGRICOLA)

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  5. Article: Structural requirements of HDAC inhibitors: SAHA analogs functionalized adjacent to the hydroxamic acid.

    Bieliauskas, Anton V / Weerasinghe, Sujith V W / Pflum, Mary Kay H

    Bioorganic & medicinal chemistry letters

    2007  Volume 17, Issue 8, Page(s) 2216–2219

    Abstract: Inhibitors of histone deacetylase (HDAC) proteins such as suberoylanilide hydroxamic acid (SAHA) have emerged as effective therapeutic anti-cancer agents. To better understand the structural requirements of HDAC inhibitors, a small molecule library with ... ...

    Abstract Inhibitors of histone deacetylase (HDAC) proteins such as suberoylanilide hydroxamic acid (SAHA) have emerged as effective therapeutic anti-cancer agents. To better understand the structural requirements of HDAC inhibitors, a small molecule library with a variety of substituents attached adjacent to the metal binding hydroxamic acid of SAHA was synthesized. The presence of a substituent adjacent to the hydroxamic acid led to an 800- to 5000-fold decrease in inhibition compared to SAHA. The observed results have implications for drug design, suggesting that HDAC inhibitors with substituents near the metal binding moiety will have inhibitory activities in the micromolar rather than nanomolar range.
    MeSH term(s) Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Combinatorial Chemistry Techniques ; Dose-Response Relationship, Drug ; Drug Design ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Histone Deacetylase Inhibitors ; Humans ; Hydroxamic Acids/chemical synthesis ; Hydroxamic Acids/chemistry ; Hydroxamic Acids/pharmacology ; Inhibitory Concentration 50 ; Structure-Activity Relationship
    Chemical Substances Antineoplastic Agents ; Enzyme Inhibitors ; Histone Deacetylase Inhibitors ; Hydroxamic Acids ; vorinostat (58IFB293JI)
    Language English
    Publishing date 2007-04-15
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1063195-1
    ISSN 1464-3405 ; 0960-894X
    ISSN (online) 1464-3405
    ISSN 0960-894X
    DOI 10.1016/j.bmcl.2007.01.117
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3203: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article: A community-built calibration system: The case study of quantification of metabolites in grape juice by qNMR spectroscopy

    Musio, Biagia / Acquotti, Domenico / Airoldi, Cristina / Assfalg, Michael / Barge, Alessandro / Bateman, Lorraine / Benevelli, Francesca / Bertelli, Davide / Bertocchi, Fabio / Bieliauskas, Aurimas / Borioni, Anna / Caligiani, Augusta / Callone, Emanuela / Čamra, Ales / Cesare Marincola, Flaminia / Chalasani, Dinesh / Consonni, Roberto / Dambruoso, Paolo / Davalli, Silvia /
    David, Taylor / Di Noia, Tommaso / Diehl, Bernd / Donarski, James / Gallo, Vito / Gil, Ana M / Gobetto, Roberto / Goldoni, Luca / Hamon, Erwann / Harwood, John S / Intini, Nicola / Kobrlová, Andrea / Latronico, Mario / Longobardi, Francesco / Luisi, Renzo / Mallamace, Domenico / Mammi, Stefano / Martin-Biran, Magali / Mastrorilli, Piero / Mazzei, Pierluigi / Mele, Andrea / Milone, Salvatore / Molero Vilchez, Dolores / Mulder, Roger J / Napoli, Claudia / Pontrelli, Stefania / Ragno, Daniele / Ragone, Rosa / Randazzo, Antonio / Rizzuti, Antonino / Rossi, Maria Cecilia / Rotondo, Archimede / Šačkus, Algirdas / Sáez Barajas, Elena / Scapicchio, Pasquale / Schievano, Elisabetta / Sitaram, Bhavaraju / Stevanato, Livio / Takis, Panteleimon G / Teipel, Jan / Thomas, Freddy / Todisco, Stefano / Torregiani, Elisabetta / Triggiani, Maurizio / Valensin, Daniela / Veronesi, Marina / Warren, John / Wist, Julien / Zailer-Hafer, Elina / Zuccaccia, Cristiano

    Talanta. 2020 July 01, v. 214

    2020  

    Abstract: Nuclear Magnetic Resonance (NMR) is an analytical technique extensively used in almost every chemical laboratory for structural identification. This technique provides statistically equivalent signals in spite of using spectrometer with different ... ...

    Abstract Nuclear Magnetic Resonance (NMR) is an analytical technique extensively used in almost every chemical laboratory for structural identification. This technique provides statistically equivalent signals in spite of using spectrometer with different hardware features and is successfully used for the traceability and quantification of analytes in food samples. Nevertheless, to date only a few internationally agreed guidelines have been reported on the use of NMR for quantitative analysis. The main goal of the present study is to provide a methodological pipeline to assess the reproducibility of NMR data produced for a given matrix by spectrometers from different manufacturers, with different magnetic field strengths, age and hardware configurations. The results have been analyzed through a sequence of chemometric tests to generate a community-built calibration system which was used to verify the performance of the spectrometers and the reproducibility of the predicted sample concentrations.
    Keywords case studies ; chemical species ; chemometrics ; grape juice ; guidelines ; magnetic fields ; metabolites ; nuclear magnetic resonance spectroscopy ; quantitative analysis ; spectrometers ; traceability
    Language English
    Dates of publication 2020-0701
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 1500969-5
    ISSN 1873-3573 ; 0039-9140
    ISSN (online) 1873-3573
    ISSN 0039-9140
    DOI 10.1016/j.talanta.2020.120855
    Database NAL-Catalogue (AGRICOLA)

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