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  1. Article ; Online: Chaperone mediated detection of small molecule target binding in cells

    Kelvin F. Cho / Taylur P. Ma / Christopher M. Rose / Donald S. Kirkpatrick / Kebing Yu / Robert A. Blake

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 11

    Abstract: Quantitative profiling of small molecule-protein binding in cells can aid basic biochemical research and drug discovery. Here, the authors develop the Heat Shock Protein Inhibition Protein Stability Assay (HIPStA) as a high-throughput method to assess ... ...

    Abstract Quantitative profiling of small molecule-protein binding in cells can aid basic biochemical research and drug discovery. Here, the authors develop the Heat Shock Protein Inhibition Protein Stability Assay (HIPStA) as a high-throughput method to assess cellular target engagement and identify new drug targets.
    Keywords Science ; Q
    Language English
    Publishing date 2020-01-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Chaperone mediated detection of small molecule target binding in cells

    Kelvin F. Cho / Taylur P. Ma / Christopher M. Rose / Donald S. Kirkpatrick / Kebing Yu / Robert A. Blake

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 11

    Abstract: Quantitative profiling of small molecule-protein binding in cells can aid basic biochemical research and drug discovery. Here, the authors develop the Heat Shock Protein Inhibition Protein Stability Assay (HIPStA) as a high-throughput method to assess ... ...

    Abstract Quantitative profiling of small molecule-protein binding in cells can aid basic biochemical research and drug discovery. Here, the authors develop the Heat Shock Protein Inhibition Protein Stability Assay (HIPStA) as a high-throughput method to assess cellular target engagement and identify new drug targets.
    Keywords Science ; Q
    Language English
    Publishing date 2020-01-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    More links

    Kategorien

  3. Article ; Online: Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes

    David S. Hewings / Johanna Heideker / Taylur P. Ma / Andrew P. AhYoung / Farid El Oualid / Alessia Amore / Gregory T. Costakes / Daniel Kirchhofer / Bradley Brasher / Thomas Pillow / Nataliya Popovych / Till Maurer / Carsten Schwerdtfeger / William F. Forrest / Kebing Yu / John Flygare / Matthew Bogyo / Ingrid E. Wertz

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 17

    Abstract: Deubiquitinases are proteases that cleave after the C-terminus of ubiquitin to hydrolyze ubiquitin chains and cleave ubiquitin from substrates. Here the authors describe a reactive-site-centric chemoproteomics approach to studying deubiquitinase activity, ...

    Abstract Deubiquitinases are proteases that cleave after the C-terminus of ubiquitin to hydrolyze ubiquitin chains and cleave ubiquitin from substrates. Here the authors describe a reactive-site-centric chemoproteomics approach to studying deubiquitinase activity, and expand the repertoire of known deubiquitinases.
    Keywords Science ; Q
    Language English
    Publishing date 2018-03-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    More links

    Kategorien

  4. Article ; Online: Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes

    David S. Hewings / Johanna Heideker / Taylur P. Ma / Andrew P. AhYoung / Farid El Oualid / Alessia Amore / Gregory T. Costakes / Daniel Kirchhofer / Bradley Brasher / Thomas Pillow / Nataliya Popovych / Till Maurer / Carsten Schwerdtfeger / William F. Forrest / Kebing Yu / John Flygare / Matthew Bogyo / Ingrid E. Wertz

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 17

    Abstract: Deubiquitinases are proteases that cleave after the C-terminus of ubiquitin to hydrolyze ubiquitin chains and cleave ubiquitin from substrates. Here the authors describe a reactive-site-centric chemoproteomics approach to studying deubiquitinase activity, ...

    Abstract Deubiquitinases are proteases that cleave after the C-terminus of ubiquitin to hydrolyze ubiquitin chains and cleave ubiquitin from substrates. Here the authors describe a reactive-site-centric chemoproteomics approach to studying deubiquitinase activity, and expand the repertoire of known deubiquitinases.
    Keywords Science ; Q
    Language English
    Publishing date 2018-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    More links

    Kategorien

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