Research Topic

E3 Ubiquitin Ligases: From Structure to Physiology, Volume II

About this Research Topic

This Research Topic is part of the E3 Ubiquitin Ligases: From Structure to Physiology series:
E3 Ubiquitin Ligases: From Structure to Physiology

Ubiquitin ligases refers to a family of proteins that are widely distributed in animals and plants and act as key regulators of cell metabolism and cell signaling. Recent reviews nicely describe our current understanding of the function of specific classes of ubiquitin ligases. However, a more holistic account of ubiquitin ligases in health and disease remain as an important pending assignment in the field.

This Research Topic addresses this gap in knowledge and aims to include contributions from leading scientists with a long-standing interest in ubiquitin ligases, ranging from the study of the function and structure of HECT-type, RNA-binding, SCF, E1, and E3 ubiquitin ligase; alternative Ubiquitin-modification Pathways; Cullin-RING ubiquitin ligase complex, to the discovery of inhibitors and activators of RING and U-box type E3 Ligases; and the role of ubiquitin ligases in autophagy and of ubiquitin-modifying enzymes in the regulation of the immune response.


Keywords: ubiquitin-modifying enzymes, ubiquitination, protein degradation, ligases, drug target


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

This Research Topic is part of the E3 Ubiquitin Ligases: From Structure to Physiology series:
E3 Ubiquitin Ligases: From Structure to Physiology

Ubiquitin ligases refers to a family of proteins that are widely distributed in animals and plants and act as key regulators of cell metabolism and cell signaling. Recent reviews nicely describe our current understanding of the function of specific classes of ubiquitin ligases. However, a more holistic account of ubiquitin ligases in health and disease remain as an important pending assignment in the field.

This Research Topic addresses this gap in knowledge and aims to include contributions from leading scientists with a long-standing interest in ubiquitin ligases, ranging from the study of the function and structure of HECT-type, RNA-binding, SCF, E1, and E3 ubiquitin ligase; alternative Ubiquitin-modification Pathways; Cullin-RING ubiquitin ligase complex, to the discovery of inhibitors and activators of RING and U-box type E3 Ligases; and the role of ubiquitin ligases in autophagy and of ubiquitin-modifying enzymes in the regulation of the immune response.


Keywords: ubiquitin-modifying enzymes, ubiquitination, protein degradation, ligases, drug target


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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Submission Deadlines

30 March 2021 Abstract
29 June 2021 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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Topic Editors

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Submission Deadlines

30 March 2021 Abstract
29 June 2021 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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