Results 61 to 70 of about 327,531 (416)

G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase [PDF]

Journal of Biological Chemistry, 2009
Emerging evidence suggests that ubiquitination serves as a protein trafficking signal in addition to its well characterized role in promoting protein degradation. The yeast G protein α subunit Gpa1 represents a rare example of a protein that undergoes both mono- and poly-ubiquitination.
Brian Kuhlman, Michael J. Lee, Carrie Purbeck, Nikolay V. Dokholyan, Matthew P. Torres, Henrik G. Dohlman, Feng Ding   +6 more
openaire   +3 more sources

Regulation of the CRL4Cdt2 Ubiquitin Ligase and Cell-Cycle Exit by the SCFFbxo11 Ubiquitin Ligase [PDF]

Molecular Cell, 2013
F-box proteins and DCAF proteins are the substrate binding subunits of the Skp1-Cul1-F-box protein (SCF) and Cul4-RING protein ligase (CRL4) ubiquitin ligase complexes, respectively. Using affinity purification and mass spectrometry, we determined that the F-box protein FBXO11 interacts with CDT2, a DCAF protein that controls cell-cycle progression ...
Moritz Horn, Shanshan Duan, Shanshan Duan, Adam Antebi, Michele Pagano, Michele Pagano, Anita Saraf, Michael P. Washburn, Michael P. Washburn, Mario Rossi, Laurence Florens, Yeon-Tae Jeong   +11 more
openaire   +5 more sources

PepMLM: Target Sequence-Conditioned Generation of Therapeutic Peptide Binders via Span Masked Language Modeling [PDF]

arXiv, 2023
Target proteins that lack accessible binding pockets and conformational stability have posed increasing challenges for drug development. Induced proximity strategies, such as PROTACs and molecular glues, have thus gained attention as pharmacological alternatives, but still require small molecule docking at binding pockets for targeted protein ...
arxiv  

Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation [PDF]

, 2018
The E3 ligase parkin ubiquitinates outer mitochondrial membrane proteins during oxidative stress and is linked to early-onset Parkinson’s disease. Parkin is autoinhibited but is activated by the kinase PINK1 that phosphorylates ubiquitin leading to ...
Aguirre, Jacob D., Barber, Kathryn R., Chaugule, Viduth K., Condos, Tara E.C., Dunkerley, Karen M., Freeman, E Aisha, Konermann, Lars, Shaw, Gary S., Walden, Helen, Xiao, Yiming   +9 more
core   +1 more source

The E3 ubiquitin ligase RNF185 facilitates the cGAS-mediated innate immune response

PLoS Pathogens, 2017
The cyclic GMP-AMP synthase (cGAS), upon cytosolic DNA stimulation, catalyzes the formation of the second messenger 2′3′-cGAMP, which then binds to stimulator of interferon genes (STING) and activates downstream signaling. It remains to be elucidated how
Qiang Wang, Liyuan Huang, Ze Hong, Zhongshi Lv, Zhaomin Mao, Yijun Tang, X. Kong, Senlin Li, Ye Cui, Heng Liu, Lele Zhang, Xiaojie Zhang, Lindi Jiang, Chen Wang, Qin Zhou   +14 more
semanticscholar   +1 more source

RING Domain E3 Ubiquitin Ligases [PDF]

Annual Review of Biochemistry, 2009
E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of most E3s is specified by a RING domain, which binds to an E2∼ubiquitin thioester and activates discharge of its ubiquitin cargo.
Deshaies, Raymond J., Joazeiro, Claudio A. P.   +1 more
openaire   +4 more sources

Homo-PROTACs: bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation

Nature Communications, 2017
E3 ubiquitin ligases are key enzymes within the ubiquitin proteasome system which catalyze the ubiquitination of proteins, targeting them for proteasomal degradation.
Chiara Maniaci, S. Hughes, Andrea Testa, Wenzhang Chen, D. Lamont, S. Rocha, D. Alessi, R. Romeo, A. Ciulli   +8 more
semanticscholar   +1 more source

Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin [PDF]

Biophysical Journal, 92, 547-561 (2007), 2006
The refolding from stretched initial conformations of ubiquitin (PDB ID: 1ubq) under the quenched force is studied using the Go model and the Langevin dynamics. It is shown that the refolding decouples the collapse and folding kinetics. The force quench refolding times scale as tau_F ~ exp(f_q*x_F/k_B*T), where f_q is the quench force and x_F = 0.96 nm
arxiv   +1 more source

WWP2 ubiquitin ligase and its isoforms: New biological insight and promising disease targets [PDF]

, 2011
A number of recent papers on the WWP2 E3 ubiquitin ligase and two novel WWP2 isoforms have revealed important biological insight and disease-specific functions, and also impacted on our understanding of ubiquitin ligases in cell cycle regulation ...
Chantry, A
core   +1 more source

PEX2 is the E3 ubiquitin ligase required for pexophagy during starvation

Journal of Cell Biology, 2016
Sargent et al. identify the E3 ubiquitin ligase PEX2 as the causative agent of mammalian pexophagy. During amino acid starvation, PEX2 expression increases to ubiquitinate peroxisomal membrane proteins and signal peroxisome degradation by autophagy.
Graeme Sargent, T. van Zutphen, T. Shatseva, Ling Zhang, Valeria E. Di Giovanni, Robert H. J. Bandsma, P. Kim   +6 more
semanticscholar   +1 more source