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Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants
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| Zeitschriftentitel: | Bioengineering & Translational Medicine |
|---|---|
| Personen und Körperschaften: | , |
| In: | Bioengineering & Translational Medicine, 2, 2017, 1, S. 31-42 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Gorelik, Maryna Sidhu, Sachdev S. Gorelik, Maryna Sidhu, Sachdev S. |
|---|---|
| author |
Gorelik, Maryna Sidhu, Sachdev S. |
| spellingShingle |
Gorelik, Maryna Sidhu, Sachdev S. Bioengineering & Translational Medicine Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants Pharmaceutical Science Biomedical Engineering Biotechnology |
| author_sort |
gorelik, maryna |
| spelling |
Gorelik, Maryna Sidhu, Sachdev S. 2380-6761 2380-6761 Wiley Pharmaceutical Science Biomedical Engineering Biotechnology http://dx.doi.org/10.1002/btm2.10044 <jats:title>Abstract</jats:title><jats:p>The ubiquitin proteasome system (UPS) has garnered much attention due to its potential for the development of therapeutics. Following a successful clinical application of general proteasome inhibitors much effort has been devoted to targeting individual UPS components including E3 enzymes and deubiquitinases that control specificity of ubiquitination. Our group has developed a novel approach for targeting the UPS proteins using engineered ubiquitin variants (Ubvs). These drug‐like proteins can serve as valuable tools to study biological function of UPS components and assist in the development of small molecules for clinical use. In this review, we summarize studies of Ubvs targeting members of three major families, including deubiquitinases, HECT E3 ligases, and CRL E3 ligases. In particular, we focus on Ubv binding mechanisms, structural studies, and effects on enzyme function. Furthermore, new insights gained from the Ubvs are discussed in the context of small molecule studies.</jats:p> Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants Bioengineering & Translational Medicine |
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| title |
Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_unstemmed |
Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_full |
Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_fullStr |
Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_full_unstemmed |
Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_short |
Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_sort |
specific targeting of the deubiquitinase and e3 ligase families with engineered ubiquitin variants |
| topic |
Pharmaceutical Science Biomedical Engineering Biotechnology |
| url |
http://dx.doi.org/10.1002/btm2.10044 |
| publishDate |
2017 |
| physical |
31-42 |
| description |
<jats:title>Abstract</jats:title><jats:p>The ubiquitin proteasome system (UPS) has garnered much attention due to its potential for the development of therapeutics. Following a successful clinical application of general proteasome inhibitors much effort has been devoted to targeting individual UPS components including E3 enzymes and deubiquitinases that control specificity of ubiquitination. Our group has developed a novel approach for targeting the UPS proteins using engineered ubiquitin variants (Ubvs). These drug‐like proteins can serve as valuable tools to study biological function of UPS components and assist in the development of small molecules for clinical use. In this review, we summarize studies of Ubvs targeting members of three major families, including deubiquitinases, HECT E3 ligases, and CRL E3 ligases. In particular, we focus on Ubv binding mechanisms, structural studies, and effects on enzyme function. Furthermore, new insights gained from the Ubvs are discussed in the context of small molecule studies.</jats:p> |
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| author | Gorelik, Maryna, Sidhu, Sachdev S. |
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| description | <jats:title>Abstract</jats:title><jats:p>The ubiquitin proteasome system (UPS) has garnered much attention due to its potential for the development of therapeutics. Following a successful clinical application of general proteasome inhibitors much effort has been devoted to targeting individual UPS components including E3 enzymes and deubiquitinases that control specificity of ubiquitination. Our group has developed a novel approach for targeting the UPS proteins using engineered ubiquitin variants (Ubvs). These drug‐like proteins can serve as valuable tools to study biological function of UPS components and assist in the development of small molecules for clinical use. In this review, we summarize studies of Ubvs targeting members of three major families, including deubiquitinases, HECT E3 ligases, and CRL E3 ligases. In particular, we focus on Ubv binding mechanisms, structural studies, and effects on enzyme function. Furthermore, new insights gained from the Ubvs are discussed in the context of small molecule studies.</jats:p> |
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| source_id | 49 |
| spelling | Gorelik, Maryna Sidhu, Sachdev S. 2380-6761 2380-6761 Wiley Pharmaceutical Science Biomedical Engineering Biotechnology http://dx.doi.org/10.1002/btm2.10044 <jats:title>Abstract</jats:title><jats:p>The ubiquitin proteasome system (UPS) has garnered much attention due to its potential for the development of therapeutics. Following a successful clinical application of general proteasome inhibitors much effort has been devoted to targeting individual UPS components including E3 enzymes and deubiquitinases that control specificity of ubiquitination. Our group has developed a novel approach for targeting the UPS proteins using engineered ubiquitin variants (Ubvs). These drug‐like proteins can serve as valuable tools to study biological function of UPS components and assist in the development of small molecules for clinical use. In this review, we summarize studies of Ubvs targeting members of three major families, including deubiquitinases, HECT E3 ligases, and CRL E3 ligases. In particular, we focus on Ubv binding mechanisms, structural studies, and effects on enzyme function. Furthermore, new insights gained from the Ubvs are discussed in the context of small molecule studies.</jats:p> Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants Bioengineering & Translational Medicine |
| spellingShingle | Gorelik, Maryna, Sidhu, Sachdev S., Bioengineering & Translational Medicine, Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants, Pharmaceutical Science, Biomedical Engineering, Biotechnology |
| title | Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_full | Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_fullStr | Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_full_unstemmed | Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_short | Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| title_sort | specific targeting of the deubiquitinase and e3 ligase families with engineered ubiquitin variants |
| title_unstemmed | Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants |
| topic | Pharmaceutical Science, Biomedical Engineering, Biotechnology |
| url | http://dx.doi.org/10.1002/btm2.10044 |