Results 31 to 40 of about 176,319 (351)

How to Inactivate Human Ubiquitin E3 Ligases by Mutation

Frontiers in Cell and Developmental Biology, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Cristina Garcia-Barcena, Nerea Osinalde, Juanma Ramirez, Ugo Mayor, Ugo Mayor   +4 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., Alessio Ciulli, Bochevarov A. D., Buckley D. L., Buckley D. L., Buckley D. L., Bunnage M. E., Carles Galdeano, Ciechanover A., Cohen P., David M. Dias, Demo S. D., Dias D. M., Hon W. C., Inge Van Molle, Ipek Birced, Louie R. J., Manalo D. J., Morgan S. Gadd, Muchnik E., Nalepa G., Pedro Soares, Pellecchia M., Rabinowitz M. H., Rentsch A., Salvatore Scaffidi, Sarah Hewitt, Semenza G.L., Tetko I. V., Van Molle I., Wells J. A., Zhang W.   +31 more
core   +5 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, Rajalingam, Krishnaraj, Dikic, Ivan   +2 more
core   +2 more sources

A pathogen type III effector with a novel E3 ubiquitin ligase architecture.

PLoS Pathogens, 2013
Type III effectors are virulence factors of Gram-negative bacterial pathogens delivered directly into host cells by the type III secretion nanomachine where they manipulate host cell processes such as the innate immunity and gene expression.
Alexander U Singer, Sebastian Schulze, Tatiana Skarina, Xiaohui Xu, Hong Cui, Lennart Eschen-Lippold, Monique Egler, Tharan Srikumar, Brian Raught, Justin Lee, Dierk Scheel, Alexei Savchenko, Ulla Bonas   +12 more
doaj   +1 more source

Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity [PDF]

, 2018
Ubiquitination is initiated by transfer of ubiquitin (Ub) from a ubiquitin-activating enzyme (E1) to a ubiquitin-conjugating enzyme (E2), producing a covalently linked intermediate (E2-Ub)(1). Ubiquitin ligases (E3s) of the 'really interesting new gene' (
A Borodovsky, A Hershko, A Plechanovová, AA Yunus, AF Alpi, Axel Knebel, B Grill, B Stieglitz, B Stieglitz, B Yang, BC Lechtenberg, Daan M. F. van Aalten, DM Wenzel, DS Hewings, E Babetto, G Langer, GN Murshudov, H Dou, HI Wan, J You, JE Brownell, JM Huibregtse, JN Pruneda, K Cadwell, Karim Rafie, Kay Hofmann, KC Pao, KK Dove, Kuan-Chuan Pao, L Conforti, M Scheffner, M Stanley, M Zhen, Mathew Stanley, MJ Niphakis, N Zheng, Nicola T. Wood, P Emsley, Peter D. Mabbitt, PY Wu, R Byrne, Ramasubramanian Sundaramoorthy, RJ Deshaies, S Milde, Satpal Virdee, SC Lovell, SK Olsen, X Wang, X Xiong, Y Shimizu, YO Ali   +50 more
core   +2 more sources

Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation [PDF]

, 2015
This is the author accepted manuscript. The final version is available from EMBO Press via the DOI in this recordMutations in the mitochondrial protein kinase PINK1 are associated with autosomal recessive Parkinson disease (PD).
Alessi, Dario R, Gonzalez, Alba, Hope, Anthony G, Johnson, Clare, Kazlauskaite, Agne, Knebel, Axel, Kumar, Atul, Martínez-Torres, R Julio, Muqit, Miratul MK, Peggie, Mark, Peltier, Julien, Prescott, Alan R, Trost, Matthias, van Aalten, Daan Mf, Walden, Helen, Wilkie, Scott, Zhang, Jinwei   +16 more
core   +3 more sources

Selective targeting of activating and inhibitory Smads by distinct WWP2 ubiquitin ligase isoforms differentially modulates TGFβ signalling and EMT [PDF]

, 2011
Ubiquitin-dependent mechanisms have emerged as essential regulatory elements controlling cellular levels of Smads and TGFß-dependent biological outputs such as epithelial–mesenchymal transition (EMT). In this study, we identify a HECT E3 ubiquitin ligase
A Chantry, A Hata, CH Heldin, CS Lutz, D Javelaud, F Bernassola, F Murray-Zmijewski, FJ McDonald, G Pirozzi, H Li, H Xu, H Zhu, HM Xu, J Tazi, J Xu, J Zavadil, L Levy, M Flasza, NJ Foot, NS Raikwar, P Kavsak, P Lönn, PJ Lu, S Bonni, S Danckwardt, S Hong, S M Soond, S Wicks, S Wiesner, S Zhang, T Atsumi, T Mund, TW Nilsen, U Valcourt, V Ellenrieder, W Li   +35 more
core   +1 more source

The E3 ubiquitin ligase RNF135 regulates the tumorigenesis activity of tongue cancer SCC25 cells

Cancer Medicine, 2016
Several E3 ubiquitin ligases have been confirmed that they are related to the tumorigenesis. This study aims to find the tongue cancer‐related E3 ubiquitin ligase. The E3 ubiquitin ligase library was screened.
Jian Jin, liya Zhao, Zubing Li
doaj   +1 more source

Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity

Cells, 2021
Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite
Utsa Bhaduri, Giuseppe Merla
doaj   +1 more source

Viral hijacking of cellular ubiquitination pathways as an anti-innate immunity strategy. [PDF]

, 2006
International audienceViruses are obligate parasites of host cells. Virus-host coevolution has selected virus for growth despite antiviral defenses set up by hosting cells and organisms. Ubiquitin conjugation onto proteins, through a cascade of reactions
Chen, Mingzhou, Gerlier, Denis
core   +3 more sources