Results 261 to 270 of about 171,834 (303)

Structural basis for L-isoaspartyl-containing protein recognition by the human PCMTD1 cullin-RING E3 ubiquitin ligase. [PDF]

J Biol Chem
Pang EZ, Zhao B, Flowers C, Oroudjeva E, Winter JB, Pandey V, Sawaya MR, Wohlschlegel J, Loo JA, Rodriguez JA, Clarke SG.   +10 more
europepmc   +1 more source

Beyond destruction: emerging roles of the E3 ubiquitin ligase Hakai. [PDF]

Cell Mol Biol Lett
Escuder-Rodríguez JJ, Rodríguez-Alonso A, Jove L, Quiroga M, Alfonsín G, Figueroa A.   +5 more
europepmc   +1 more source

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E3 ubiquitin ligases

Essays in Biochemistry, 2005
The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
openaire   +2 more sources

RBR E3 ubiquitin ligases in tumorigenesis

Seminars in Cancer Biology, 2020
RING-in-between-RING (RBR) E3 ligases are one class of E3 ligases that is characterized by the unique RING-HECT hybrid mechanism to function with E2s to transfer ubiquitin to target proteins for degradation. Emerging evidence has demonstrated that RBR E3 ligases play essential roles in neurodegenerative diseases, infection, inflammation and cancer ...
Peter, Wang, Xiaoming, Dai, Wenxiao, Jiang, Yuyun, Li, Wenyi, Wei   +4 more
openaire   +2 more sources

E3 ubiquitin ligases for MHC molecules

Current Opinion in Immunology, 2009
Recently, novel E3 ubiquitin ligases that target MHC molecules for lysosomal degradation have been discovered by several groups. All these E3s are membrane-bound and possess a variant type RING domain, termed the RING-CH or RING variant (RINGv) domain. They belong to a new E3 family designated Modulator of Immune Recognition (MIR), based on the name of
Satoshi, Ishido, Eiji, Goto, Yohei, Matsuki, Mari, Ohmura-Hoshino   +3 more
openaire   +2 more sources

HECT-Type E3 Ubiquitin Ligases in Cancer

Trends in Biochemical Sciences, 2019
Ubiquitination, a post-translational modification that involves a covalent attachment of ubiquitin to a protein substrate, is essential for cellular homeostatic maintenance. At the end of a three-enzyme cascade, E3 ubiquitin ligases (E3s) recruit substrates and promote or directly catalyze ubiquitin transfer to targets.
Francesca Bernassola, Giovanni Chillemi, Gerry Melino   +2 more
openaire   +4 more sources

Pseudophosphatase as E3 ubiquitin ligase inhibitor

Science Signaling, 2017
The pseudophosphatase STYX prevents the substrate recognition subunit FBXW7 from binding the catalytic E3 ubiquitin ligase complex.
openaire   +2 more sources

E3-Ubiquitin Ligase

2011
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E3 Ubiquitin Ligases

2012
Uwe Proske, David L. Morgan, Tamara Hew-Butler, Kevin G. Keenan, Roger M. Enoka, Sebastian Sixt, Josef Niebauer, John A. Hawley, Martin J. Gibala, Kathryn H. Myburgh, C. Capelli, P. Zamparo, Jie Kang, Herbert Löllgen, Ruth Löllgen, Wolfgang Jelkmann, Christopher B. Scott, Ioannis Smyrnias, Martin D. Bootman, H. Llewelyn Roderick, Jonathan N. Myers, Peter H. Brubaker, Kai-Håkon Carlsen, Michael Kjær, Marc Sim, Peter Peeling, Brian Dawson, Debbie Trinder   +27 more
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Systemwide disassembly and assembly of SCF ubiquitin ligase complexes

Cell, 2023
Kheewoong Baek, Daniel C Scott, Moeko King   +2 more
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