Literature DB >> 20074048

The therapeutic potential of deubiquitinating enzyme inhibitors.

Frédéric Colland1.   

Abstract

Proteases play a key role in various pathological processes and several protease inhibitors are already available for treatment. DUBs (deubiquitinating enzymes) constitute one of the largest classes of human proteases and are key effectors of the ubiquitin-proteasome system. This pathway regulating cellular protein turnover has been implicated in the pathogenesis of many human diseases, including neurodegenerative disorders, viral diseases and cancer. The therapeutic efficacy of the proteasome inhibitor Velcade (bortezomib) for treating multiple myeloma and mantle cell lymphoma establishes this system as a valid target for cancer treatment. A promising alternative to targeting the proteasome itself would be to target the upstream, ubiquitin conjugation/deconjugation system, to generate more specific, less toxic anticancer agents. Advances in small molecule-based inhibitors specifically targeting DUBs are presented in this review.

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Year:  2010        PMID: 20074048     DOI: 10.1042/BST0380137

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  57 in total

1.  Ubiquitination: Added complexity in Ras and Rho family GTPase function.

Authors:  Michelle de la Vega; James F Burrows; James A Johnston
Journal:  Small GTPases       Date:  2011-07-01

2.  Deubiquitylase, deSUMOylase, and deISGylase activity microarrays for assay of substrate preference and functional modifiers.

Authors:  Christian M Loch; Charles L Cuccherini; Craig A Leach; James E Strickler
Journal:  Mol Cell Proteomics       Date:  2010-10-18       Impact factor: 5.911

3.  Characterization of Puma-dependent and Puma-independent neuronal cell death pathways following prolonged proteasomal inhibition.

Authors:  Liam P Tuffy; Caoimhín G Concannon; Beatrice D'Orsi; Matthew A King; Ina Woods; Heinrich J Huber; Manus W Ward; Jochen H M Prehn
Journal:  Mol Cell Biol       Date:  2010-10-04       Impact factor: 4.272

Review 4.  Protein quality control during erythropoiesis and hemoglobin synthesis.

Authors:  Eugene Khandros; Mitchell J Weiss
Journal:  Hematol Oncol Clin North Am       Date:  2010-12       Impact factor: 3.722

Review 5.  Regulation of AMPK by the ubiquitin proteasome system.

Authors:  Makhosazane Zungu; Jonathan C Schisler; M Faadiel Essop; Chris McCudden; Cam Patterson; Monte S Willis
Journal:  Am J Pathol       Date:  2010-12-23       Impact factor: 4.307

6.  Deubiquitinases Modulate Platelet Proteome Ubiquitination, Aggregation, and Thrombosis.

Authors:  Nilaksh Gupta; Wei Li; Thomas M McIntyre
Journal:  Arterioscler Thromb Vasc Biol       Date:  2015-10-15       Impact factor: 8.311

7.  The ubiquitin ligase RNF220 enhances canonical Wnt signaling through USP7-mediated deubiquitination of β-catenin.

Authors:  Pengcheng Ma; Xiangcai Yang; Qinghua Kong; Chaocui Li; Shuangjuan Yang; Yan Li; Bingyu Mao
Journal:  Mol Cell Biol       Date:  2014-09-29       Impact factor: 4.272

8.  Saturation scanning of ubiquitin variants reveals a common hot spot for binding to USP2 and USP21.

Authors:  Isabel Leung; Ayelet Dekel; Julia M Shifman; Sachdev S Sidhu
Journal:  Proc Natl Acad Sci U S A       Date:  2016-07-19       Impact factor: 11.205

Review 9.  Regulation of pluripotency and differentiation by deubiquitinating enzymes.

Authors:  B Suresh; J Lee; H Kim; S Ramakrishna
Journal:  Cell Death Differ       Date:  2016-06-10       Impact factor: 15.828

Review 10.  Targeting the ubiquitin pathway for cancer treatment.

Authors:  Jia Liu; Shavali Shaik; Xiangpeng Dai; Qiong Wu; Xiuxia Zhou; Zhiwei Wang; Wenyi Wei
Journal:  Biochim Biophys Acta       Date:  2014-12-04
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