AbstractUbiquitination targets proteins for degradation and is a potent regulator of cellular protein function. Recent results implicate the RING finger domain in specific ubiquitination events; it is possible that all RING proteins act as E3 ubiquitin protein ligases, with implications for a variety of biological areas
Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates governs n...
The activity of RING ubiquitin ligases (E3s) depends on an interaction between the RING domain and u...
Proteins of the ring between ring fingers (RBR)-domain family are characterized by three groups of s...
AbstractRING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, con...
Thesis (Ph.D.)--University of Washington, 2016-12Ubiquitination is a posttranslational modification ...
Protein ubiquitination plays an important role in regulating the abundance and conformation of a bro...
Protein ubiquitination is a post-translational modification that controls essential biological proce...
Funder: Boehringer Ingelheim Fonds (Stiftung für medizinische Grundlagenforschung); doi: https://doi...
textabstractUbiquitination is an important posttranslational modification that plays a role in virtu...
© 2019 by the authors. Licensee MDPI, Basel, Switzerland. There is growing evidence highlighting the...
AbstractUbiquitin modification is a well established way of regulating protein levels and activities...
Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology, where a cas...
AbstractSNURF/RNF4 has been implicated in transcriptional regulation and growth inhibition in a RING...
Recent studies point to a diverse assemblage of prokaryotic cognates of the eukaryotic ubiquitin (Ub...
AbstractSCF ubiquitin ligases contain an E3 core composed of Skp1, Cul1, a member of the Rbx1/Roc1 f...
Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates governs n...
The activity of RING ubiquitin ligases (E3s) depends on an interaction between the RING domain and u...
Proteins of the ring between ring fingers (RBR)-domain family are characterized by three groups of s...
AbstractRING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, con...
Thesis (Ph.D.)--University of Washington, 2016-12Ubiquitination is a posttranslational modification ...
Protein ubiquitination plays an important role in regulating the abundance and conformation of a bro...
Protein ubiquitination is a post-translational modification that controls essential biological proce...
Funder: Boehringer Ingelheim Fonds (Stiftung für medizinische Grundlagenforschung); doi: https://doi...
textabstractUbiquitination is an important posttranslational modification that plays a role in virtu...
© 2019 by the authors. Licensee MDPI, Basel, Switzerland. There is growing evidence highlighting the...
AbstractUbiquitin modification is a well established way of regulating protein levels and activities...
Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology, where a cas...
AbstractSNURF/RNF4 has been implicated in transcriptional regulation and growth inhibition in a RING...
Recent studies point to a diverse assemblage of prokaryotic cognates of the eukaryotic ubiquitin (Ub...
AbstractSCF ubiquitin ligases contain an E3 core composed of Skp1, Cul1, a member of the Rbx1/Roc1 f...
Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates governs n...
The activity of RING ubiquitin ligases (E3s) depends on an interaction between the RING domain and u...
Proteins of the ring between ring fingers (RBR)-domain family are characterized by three groups of s...
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