β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency. [PDF]
, 2010 ObjectiveThe islet in type 2 diabetes is characterized by β-cell apoptosis, β-cell endoplasmic reticulum stress, and islet amyloid deposits derived from islet amyloid polypeptide (IAPP).
Butler, Alexandra E +7 more
core +2 more sources
Intracellular Dynamics of the Ubiquitin-Proteasome-System [version 2; referees: 3 approved]
F1000Research, 2015 The ubiquitin-proteasome system is the major degradation pathway for short-lived proteins in eukaryotic cells. Targets of the ubiquitin-proteasome-system are proteins regulating a broad range of cellular processes including cell cycle progression, gene ...
Maisha Chowdhury, Cordula Enenkel
doaj +1 more source
Prion degradation pathways: Potential for therapeutic intervention [PDF]
, 2015 Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be
Goold, R, McKinnon, C, Tabrizi, SJ
core +1 more source
The ubiquitin proteasome system in neuropathology [PDF]
Acta Neuropathologica, 2009 The ubiquitin proteasome system (UPS) orchestrates the turnover of innumerable cellular proteins. In the process of ubiquitination the small protein ubiquitin is attached to a target protein by a peptide bond. The ubiquitinated target protein is subsequently shuttled to a protease complex known as the 26S proteasome and subjected to degradative ...
openaire +2 more sources
F1000Research, 2015 The ubiquitin-proteasome system is the major degradation pathway for short-lived proteins in eukaryotic cells. Targets of the ubiquitin-proteasome-system are proteins regulating a broad range of cellular processes including cell cycle progression, gene ...
Maisha Chowdhury, Cordula Enenkel
doaj +1 more source
Up-regulation of ubiquitin–proteasome activity upon loss of NatA-dependent N-terminal acetylation
Life Science Alliance, 2022 Inactivation of N-terminal acetyltransferase A is found to alter Rpn4 as well as E3 ligase abundance, causing up-regulation of Ubiquitin–proteasome activity.
Ilia Kats +6 more
doaj +1 more source
Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von hippel-lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities [PDF]
, 2014 E3 ubiquitin ligases are attractive targets in the ubiquitin-proteasome system, however, the development of small-molecule ligands has been rewarded with limited success.
Adams J. +31 more
core +5 more sources
Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins [PDF]
, 2008 Background: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step in the regulation of the ubiquitin-proteasome pathway, yet the mechanisms underlying this step are not understood in detail.
Deshaies, Raymond J. +6 more
core +6 more sources
Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]
, 2012 Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone +2 more
core +2 more sources
Poxvirus Exploitation of the Ubiquitin-Proteasome System
Viruses, 2010 Ubiquitination plays a critical role in many cellular processes. A growing number of viruses have evolved strategies to exploit the ubiquitin-proteasome system, including members of the Poxviridae family. Members of the poxvirus family have recently been
Alastair Teale +5 more
doaj +1 more source