Robuta

https://elifesciences.org/articles/13027v1 Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition |... atomic structure of the 26s proteasome https://www.rcsb.org/structure/5MPD RCSB PDB - 5MPD: 26S proteasome in presence of ATP (s1) 26S proteasome in presence of ATP (s1) rcsb pdb 26s proteasome presence atp s1 https://www.ncbi.nlm.nih.gov/protein/5VHQ_E Chain E, 26S proteasome regulatory subunit 10B - Protein - NCBI 26s proteasome chain regulatory subunit 10b https://www.wikidata.org/wiki/Q27931789 Identification of ubiquitin-like protein-binding subunits of the 26S proteasome - Wikidata ubiquitin like protein 26s proteasome identification https://www.ncbi.nlm.nih.gov/protein/2N3T_A Chain A, 26S proteasome regulatory subunit RPN1 - Protein - NCBI 26s proteasome chain regulatory subunit rpn1 https://elifesciences.org/articles/13027 Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition |... Within the isolated lid sub-complex of the proteasome, a finely tuned network of interactions maintains the deubiquitinase in an inhibited conformation;... atomic structure of the 26s proteasome https://elifesciences.org/articles/49806 Specific lid-base contacts in the 26s proteasome control the conformational switching required for... The 26S proteasome lid subcomplex acts as an external scaffold whose interactions with the ATPase motor stabilize the substrate-engagement-competent state, and... https://www.wikidata.org/wiki/Q27931597 Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase... https://pmc.ncbi.nlm.nih.gov/articles/PMC5127335/ p62- and ubiquitin-dependent stress-induced autophagy of the mammalian 26S proteasome - PMC Whereas the role of the ubiquitin system in protein degradation is well established, little is known regarding the regulation of its own components, including...