Results 51 to 60 of about 353,107 (313)

A Ubiquitin-like Protein Unleashes Ubiquitin Ligases [PDF]

Cell, 2008
Modification of cullin-RING ubiquitin ligases by the ubiquitin-like molecule Nedd8 promotes substrate ubiquitination. A crystal structure of a cullin modified by Nedd8 recently reported in Cell (Duda et al., 2008) and a biochemical study in Molecular Cell (Saha and Deshaies, 2008) reveal the dramatic impact on the ligase machinery by conjugation of ...
Saifee, Nabiha Huq, Zheng, Ning
openaire   +2 more sources

Ubiquitin and ubiquitin-like conjugation systems in trypanosomatids

Current Opinion in Microbiology, 2022
In eukaryotic cells, reversible attachment of ubiquitin and ubiquitin-like modifiers (Ubls) to specific target proteins is conducted by multicomponent systems whose collective actions control protein fate and cell behaviour in precise but complex ways.
Burge, Rebecca, Mottram, Jeremy Charles, Wilkinson, Anthony J   +2 more
openaire   +3 more sources

Small ubiquitin-like modifier protein SUMO enables plants to control growth independently of the phytohormone gibberellin [PDF]

, 2014
Plants survive adverse conditions by modulating their growth in response to a changing environment. Gibberellins (GAs) play a key role in these adaptive responses by stimulating the degradation of growth-repressing DELLA proteins.
Bennett, M., Galbiati, Massimo, Hedden, Peter, Woodcock, A., S. Nelis, Hedden, P., A. Sadanandom, A. Woodcock, Woodcock, Ailidh, R. Swarup, Swarup, Ranjan, Tonelli, Chiara, Bennett, Malcolm J., Bennett, Malcolm, Zhang, Cunjin, C. Tonelli, Sadanandom, Ari, M. Galbiati, Nelis, S., Conti, L., L. Conti, Napier, Richard, Zhang, C., Conti, Lucio, Galbiati, M., Nelis, Stuart, R. Napier, P. Hedden, Sadanandom, A., C. Zhang, Napier, R., Swarup, R., M. Bennett, Tonelli, C.   +33 more
core   +1 more source

Sharpin prevents skin inflammation by inhibiting TNFR1-induced keratinocyte apoptosis

eLife, 2014
Linear Ubiquitin chain Assembly Complex (LUBAC) is an E3 ligase complex that generates linear ubiquitin chains and is important for tumour necrosis factor (TNF) signaling activation.
Snehlata Kumari, Younes Redouane, Jaime Lopez-Mosqueda, Ryoko Shiraishi, Malgorzata Romanowska, Stefan Lutzmayer, Jan Kuiper, Conception Martinez, Ivan Dikic, Manolis Pasparakis, Fumiyo Ikeda   +10 more
doaj   +1 more source

Structure and Ubiquitin Binding of the Ubiquitin-interacting Motif [PDF]

Journal of Biological Chemistry, 2003
Ubiquitylation is used to target proteins into a large number of different biological processes including proteasomal degradation, endocytosis, virus budding, and vacuolar protein sorting (Vps). Ubiquitylated proteins are typically recognized using one of several different conserved ubiquitin binding modules.
Robert D, Fisher, Bin, Wang, Steven L, Alam, Daniel S, Higginson, Howard, Robinson, Wesley I, Sundquist, Christopher P, Hill   +6 more
openaire   +2 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

Contributions of ubiquitin- and PCNA-binding domains to the activity of Polymerase η in Saccharomyces cerevisiae

, 2007
Bypassing of DNA lesions by damage-tolerant DNA polymerases depends on the interaction of these enzymes with the monoubiquitylated form of the replicative clamp protein, PCNA.
Bielen, Aleksandra B., Ulrich, Helle D., Parker, Joanne L., Đikić, Ivan   +3 more
core   +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.
Dias, David M, Carles Galdeano (1305135), Galdeano, Carles, Dias, David M., David M. Dias (1340694), Van Molle, Inge, Gadd, Morgan Stuart, Ciulli, Alessio, Sarah Hewitt (1340700), Soares, Pedro, Galdeano , Carles, Pedro Soares (393566), Gadd, Morgan S., Salvatore Scaffidi (1340703), Inge Van Molle (1284120), Morgan S. Gadd (149371), Scaffidi, Salvatore, Ipek Birced (1340697), Alessio Ciulli (762789), Hewitt, Sarah, Birced, Ipek   +20 more
core   +1 more source

DNA polymerase α/primase extraction from chromatin by VCP/p97 restricts ATR activation during unperturbed DNA replication

Nature Communications
The replication stress response is an essential pathway that deals with the obstacles that halt the progression of DNA replication forks even during an unperturbed S phase.
Sara Rodríguez-Acebes, Rodrigo Martín-Rufo, Alicia Gómez-Moya, Scott B. Churcher, Alejandro Fernández-Llorente, Guillermo de la Vega-Barranco, Alejandra Perona, Pilar Oroz, Elena Martín-Doncel, Luis Ignacio Toledo, Juan Méndez, Emilio Lecona   +11 more
doaj   +1 more source

Branched ubiquitin chain binding and deubiquitination by UCH37 facilitate proteasome clearance of stress-induced inclusions

eLife, 2021
UCH37, also known as UCHL5, is a highly conserved deubiquitinating enzyme (DUB) that associates with the 26S proteasome. Recently, it was reported that UCH37 activity is stimulated by branched ubiquitin (Ub) chain architectures.
Aixin Song, Zachary Hazlett, Dulith Abeykoon, Jeremy Dortch, Andrew Dillon, Justin Curtiss, Sarah Bollinger Martinez, Christopher P Hill, Clinton Yu, Lan Huang, David Fushman, Robert E Cohen, Tingting Yao   +12 more
doaj   +1 more source