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to delineate the complete subunit architecture of the regulatory particle . Our studies reveal the spatial arrangement of ubiquitin receptors, deubiquitinating enzymes, and the protein unfolding machinery ...
The 26S proteasome contains a 19S regulatory particle that selects and unfolds ubiquitinated substrates for degradation in the 20S catalytic particle . To date there are no high-resolution structures ...
in mammalian cells (Wang et al., 1996). The distinct 19S regulatory particles are subunits of the multiple 26S proteasome complexes, which regulate the degradation of different proteins (McDonald and Byers, 1997 ...
26S proteasome regulatory subunit (by homology) RPT4 RPT4 orf19.482 2.6 26S proteasome regulatory subunit (by homology) RPN5.3f RPN5 orf19.4032 3.1 Subunit of the regulatory particle ...
E , Martin A . Complete subunit architecture of the proteasome regulatory particle . Nature 2012 , 482 : 186 – 191 . Google Scholar Crossref Search ADS PubMed 42 Luan B , Huang X , Wu J , Mei Z , Wang ...
( regulatory particle /PA700) [9–11]. This factor is an ATP-dependent activator that binds and unfolds ubiquitin-conjugated proteins to promote proteasomal degradation of its substrates [11]. The other three ...
Rpn4p transactivation domains. FEBS Lett 2008; 582: 3459– 64 Google Scholar CrossRef Search ADS PubMed Lander GC , Estrin E, Matyskiela MEet al. . Complete subunit architecture of the proteasome ...
, several Ub- proteasome pathway components were also confirmed as Ub targets upon PTI immune elicitation, including the E2 UBC13 and proteasome subunit REGULATORY PARTICLE NON-ATPASE SUBUNIT 8b (RPN8b). Taken ...
campestris pv vesicatoria, interacts with the proteasomal subunit Regulatory Particle AAA-ATPase6 (RPT6) in planta to suppress proteasome activity, resulting in the inhibition of salicylic acid-related immune ...
with ubiquitylation of the ubiquitin attached to the protein to produce polyubiquitinated proteins, which are recognized by ubiquitin receptors on the 19S regulatory particle of the proteasome and removed ...
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