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  1. Article: Length Matters: MINDY Is a New Deubiquitinase Family that Preferentially Cleaves Long Polyubiquitin Chains

    Maurer, Till / Ingrid E. Wertz

    Molecular cell. 2016 July 07, v. 63, no. 1

    2016  

    Abstract: Abdul Rehman and colleagues identify a sixth family of deubiquitinase enzymes that are highly conserved throughout eukaryotes and show a remarkable selectivity for cleaving extended Lys-48-linked polyubiquitin chains. ...

    Abstract Abdul Rehman and colleagues identify a sixth family of deubiquitinase enzymes that are highly conserved throughout eukaryotes and show a remarkable selectivity for cleaving extended Lys-48-linked polyubiquitin chains.
    Keywords enzymes ; eukaryotic cells ; ubiquitin
    Language English
    Dates of publication 2016-0707
    Size p. 4-6.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2016.06.027
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2005/501: Show issues

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  2. Article: Activity‐based probes for the multicatalytic proteasome

    Hewings, David S / Ingrid E. Wertz / John A. Flygare / Matthew Bogyo

    FEBS journal. 2017 May, v. 284, no. 10

    2017  

    Abstract: Proteasomes are multisubunit protease complexes responsible for degrading most intracellular proteins. In addition to removing damaged proteins, they regulate many important cellular processes through the controlled degradation of transcription factors, ... ...

    Abstract Proteasomes are multisubunit protease complexes responsible for degrading most intracellular proteins. In addition to removing damaged proteins, they regulate many important cellular processes through the controlled degradation of transcription factors, cell cycle regulators, and enzymes. Eukaryotic proteasomes have three catalytic subunits, β1, β2, and β5, that each has different substrate specificities. Additionally, although we know that diverse cell types express proteasome variants with distinct activity and specificity profiles, the functions of these different pools of proteasomes are not fully understood. Covalent inhibitors of the protease activity of the proteasome have been developed as drugs for hematological malignancies and are currently under investigation for other diseases. Therefore, there is a need for tools that allow direct monitoring of proteasome activity in live cells and tissues. Activity‐based probes have proven valuable for biochemical and cell biological studies of the role of individual proteasome subunits, and for evaluating the efficacy and selectivity of proteasome inhibitors. These probes react covalently with the protease active sites, and contain a reporter tag to identify the probe‐labeled proteasome subunits. This review will describe the development of broad‐spectrum and subunit‐specific proteasome activity‐based probes, and discuss how these probes have contributed to our understanding of proteasome biology, and to the development of proteasome inhibitors.
    Keywords active sites ; cell cycle ; chemical bonding ; drugs ; enzyme activity ; monitoring ; proteasome endopeptidase complex ; proteasome inhibitors ; protein subunits ; proteinases ; substrate specificity ; tissues ; transcription factors
    Language English
    Dates of publication 2017-05
    Size p. 1540-1554.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note REVIEW
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.14016
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2006/704: Show issues

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  3. 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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  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 Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. 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)

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    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.

  6. Article ; Online: Correction

    James D Joseph / Beatrice Darimont / Wei Zhou / Alfonso Arrazate / Amy Young / Ellen Ingalla / Kimberly Walter / Robert A Blake / Jim Nonomiya / Zhengyu Guan / Lorna Kategaya / Steven P Govek / Andiliy G Lai / Mehmet Kahraman / Dan Brigham / John Sensintaffar / Nhin Lu / Gang Shao / Jing Qian /
    Kate Grillot / Michael Moon / Rene Prudente / Eric Bischoff / Kyoung-Jin Lee / Celine Bonnefous / Karensa L Douglas / Jackaline D Julien / Johnny Y Nagasawa / Anna Aparicio / Josh Kaufman / Benjamin Haley / Jennifer M Giltnane / Ingrid E Wertz / Mark R Lackner / Michelle A Nannini / Deepak Sampath / Luis Schwarz / Henry Charles Manning / Mohammed Noor Tantawy / Carlos L Arteaga / Richard A Heyman / Peter J Rix / Lori Friedman / Nicholas D Smith / Ciara Metcalfe / Jeffrey H Hager

    eLife, Vol

    The selective estrogen receptor downregulator GDC-0810 is efficacious in diverse models of ER+ breast cancer

    2019  Volume 8

    Keywords Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2019-01-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: The selective estrogen receptor downregulator GDC-0810 is efficacious in diverse models of ER+ breast cancer

    James D Joseph / Beatrice Darimont / Wei Zhou / Alfonso Arrazate / Amy Young / Ellen Ingalla / Kimberly Walter / Robert A Blake / Jim Nonomiya / Zhengyu Guan / Lorna Kategaya / Steven P Govek / Andiliy G Lai / Mehmet Kahraman / Dan Brigham / John Sensintaffar / Nhin Lu / Gang Shao / Jing Qian /
    Kate Grillot / Michael Moon / Rene Prudente / Eric Bischoff / Kyoung-Jin Lee / Celine Bonnefous / Karensa L Douglas / Jackaline D Julien / Johnny Y Nagasawa / Anna Aparicio / Josh Kaufman / Benjamin Haley / Jennifer M Giltnane / Ingrid E Wertz / Mark R Lackner / Michelle A Nannini / Deepak Sampath / Luis Schwarz / Henry Charles Manning / Mohammed Noor Tantawy / Carlos L Arteaga / Richard A Heyman / Peter J Rix / Lori Friedman / Nicholas D Smith / Ciara Metcalfe / Jeffrey H Hager

    eLife, Vol

    2016  Volume 5

    Abstract: ER-targeted therapeutics provide valuable treatment options for patients with ER+ breast cancer, however, current relapse and mortality rates emphasize the need for improved therapeutic strategies. The recent discovery of prevalent ESR1 mutations in ... ...

    Abstract ER-targeted therapeutics provide valuable treatment options for patients with ER+ breast cancer, however, current relapse and mortality rates emphasize the need for improved therapeutic strategies. The recent discovery of prevalent ESR1 mutations in relapsed tumors underscores a sustained reliance of advanced tumors on ERα signaling, and provides a strong rationale for continued targeting of ERα. Here we describe GDC-0810, a novel, non-steroidal, orally bioavailable selective ER downregulator (SERD), which was identified by prospectively optimizing ERα degradation, antagonism and pharmacokinetic properties. GDC-0810 induces a distinct ERα conformation, relative to that induced by currently approved therapeutics, suggesting a unique mechanism of action. GDC-0810 has robust in vitro and in vivo activity against a variety of human breast cancer cell lines and patient derived xenografts, including a tamoxifen-resistant model and those that harbor ERα mutations. GDC-0810 is currently being evaluated in Phase II clinical studies in women with ER+ breast cancer.
    Keywords breast cancer ; estrogen receptor ; SERD ; GDC-0810 ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 616
    Language English
    Publishing date 2016-07-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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