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  1. Article ; Online: Antibody toolkit reveals N-terminally ubiquitinated substrates of UBE2W

    Christopher W. Davies / Simon E. Vidal / Lilian Phu / Jawahar Sudhamsu / Trent B. Hinkle / Scott Chan Rosenberg / Frances-Rose Schumacher / Yi Jimmy Zeng / Carsten Schwerdtfeger / Andrew S. Peterson / Jennie R. Lill / Christopher M. Rose / Andrey S. Shaw / Ingrid E. Wertz / Donald S. Kirkpatrick / James T. Koerber

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Volume 19

    Abstract: UBE2W catalyzes the ubiquitination of protein N-termini but its substrate spectrum is largely unknown. Here, the authors discover mAbs selective for peptides derived from N-terminally ubiquitinated proteins, solve the structure of a peptide-bound mAb and ...

    Abstract UBE2W catalyzes the ubiquitination of protein N-termini but its substrate spectrum is largely unknown. Here, the authors discover mAbs selective for peptides derived from N-terminally ubiquitinated proteins, solve the structure of a peptide-bound mAb and apply the mAbs to map endogenous UBE2W substrates by proteomics.
    Keywords Science ; Q
    Language English
    Publishing date 2021-07-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. 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)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  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 Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

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