Results 71 to 80 of about 383,830 (310)

Ubiquitin-proteasome system in eukaryotes and Pup-proteasome system in Mycobacterium.

, 2021
DUB, deubiquitinase; Pup, prokaryotic ubiquitin-like protein.
Gang Lin (824266), Hao Zhang (15339)
core   +1 more source

The Roles of Ubiquitin in Mediating Autophagy

Cells, 2020
Ubiquitination, the post-translational modification essential for various intracellular processes, is implicated in multiple aspects of autophagy, the major lysosome/vacuole-dependent degradation pathway.
Zhangyuan Yin, Hana Popelka, Yuchen Lei, Ying Yang, Daniel J. Klionsky   +4 more
doaj   +1 more source

The ubiquitin system in normal and infected germinal center B cells

FEBS Letters, EarlyView.
The ubiquitin system plays a central role in germinal center (GC) B cells, influencing differentiation to long‐lived memory B cells. Oncogenic gammaherpesviruses gain access to memory B cells by establishing latency in GC B cells. Mapping ubiquitin mechanisms in normal and infected GC B cells will define specific molecular circuits in B cells germane ...
Destiny Davis, Lesly Mejia, Emily K Moser   +2 more
wiley   +1 more source

Structure of the Human FANCL RING-Ube2T Complex Reveals Determinants of Cognate E3-E2 Selection [PDF]

, 2014
The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for ubiquitin modification of a substrate. Moreover, the pairing dictates both the substrate choice and the modification type. The molecular details of generic
Miles, Jennifer Anne, Hodson, Charlotte, Purkiss, Andrew, Walden, Helen   +3 more
core   +1 more source

Selective ubiquitination of drug-like small molecules by the ubiquitin ligase HUWE1

Nature Communications
The ubiquitin system regulates eukaryotic physiology by modifying myriad substrate proteins. Substrate specificity and the assembly of ubiquitin signals are determined by ubiquitin ligases, some of which also modify non-protein biomolecules.
Barbara Orth, Pavel Pohl, Florian Aust, Yanlong Ji, Ayshwarya Seenivasan, Olexandr Dybkov, Xiaojun Julia Liang, Lars Bock, Florian Leidner, Sophie Levantovsky, Patrick Schardey, Pascal Sander, Nathanael J. Disch, Masanja L. Trautz, Athanasia Mizi, Argyris Papantonis, Christof Lenz, Helmut Grubmüller, Wieland Steinchen, Christian Behrends, Henning Urlaub, Matthias Gehringer, Sonja Lorenz   +22 more
doaj   +1 more source

The natural history of ubiquitin and ubiquitin-related domains [PDF]

Frontiers in Bioscience, 2012
The ubiquitin (Ub) system is centered on conjugation and deconjugation of Ub and Ub-like (Ubls) proteins by a system of ligases and peptidases, respectively. Ub/Ubls contain the beta-grasp fold, also found in numerous proteins with biochemically distinct roles unrelated to the conventional Ub-system. The beta-GF underwent an early radiation spawning at
Alexander Maxwell, Burroughs, Lakshminarayan M, Iyer, L, Aravind   +2 more
openaire   +2 more sources

Smaller is better: nanobodies meet NMR

FEBS Letters, EarlyView.
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley   +1 more source

Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains [PDF]

, 2015
This work was supported by grants from Cancer Research UK (C434/A13067), the Wellcome Trust (098391/Z/12/Z) and Biotechnology and Biological Sciences Research Council (BB/J016004/1).The RING E3 ligase catalysed formation of lysine 63 linked ubiquitin ...
Naismith, Jim, Emma Branigan, Branigan, Emma, Hay, Ronald T., Ellis G Jaffray, Plechanovová, Anna, Jaffray, Ellis, Jaffray, Ellis G., Naismith, James H., James H Naismith, Hay, Ronald Thomas, Anna Plechanovová, Ronald T Hay   +12 more
core   +1 more source

Engineering ubiquitin to modulate the ubiquitin proteosome system [PDF]

Cell Cycle, 2013
(2013). Engineering ubiquitin to modulate the ubiquitin proteosome system. Cell Cycle: Vol. 12, No. 11, pp. 1651-1652.
Andreas, Ernst, Sachdev S, Sidhu
openaire   +2 more sources

Inhibition of dipeptidyl peptidase 7 impairs lysophagy in LLOMe‐treated HepG2 cells

FEBS Letters, EarlyView.
DPP7 inhibition delays ubiquitin‐dependent lysophagy by attenuating ubiquitin accumulation and the recruitment of SQSTM1 and LC3 to damaged lysosomes, resulting in delayed clearance of damaged lysosomes and impaired restoration of lysosomal homeostasis. Created using FigureLabs (Certificate ID: FL‐PUB‐20260922‐Z99XNX).
Na Yeon Park, Inho Kwon, Yong Hwan Kim, Ji‐Eun Bae, Joon Bum Kim, Seong Hyun Kim, Sungho Maeng, Doo Sin Jo, Dong‐Hyung Cho   +8 more
wiley   +1 more source