Results 11 to 20 of about 519,123 (352)

To Be or Not to Be...Ubiquitinated? [PDF]

Cell Cycle, 2004
Levels of p21, a cyclin-dependent kinase (CDK) inhibitor, are controlled in part at the post-translational level by protein degradation. Although the signaling pathways leading to p21 degradation have not yet been fully elucidated, it is evident that p21 ubiquitination is an essential factor in its degradation.
Joanna, Bloom, Michele, Pagano
openaire   +2 more sources

Cracking the Ubiquitin Code: The Ubiquitin Toolbox [PDF]

Current Issues in Molecular Biology, 2019
Ubiquitination, a post-translational modification, regulates a vast array of fundamental biological processes with dysregulation of the dedicated enzymes giving rise to pathologies such as cancer and neurodegenerative diseases. Assembly and its ensuing removal of this post-translational modification, determining a large variety of biological functions,
Mulder, M.P.C., Witting, K.F., Ovaa, H.
openaire   +3 more sources

Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination [PDF]

Cell, 2016
Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate NAD-dependent and ATP-independent ubiquitin transfer to host proteins.
Bhogaraju, S., Kalayil, S., Liu, Y., Bonn, F., Colby, T., Matić, I., Dikic, I.   +6 more
openaire   +3 more sources

Assembly and disassembly of branched ubiquitin chains

Frontiers in Molecular Biosciences, 2023
Protein ubiquitylation is an essential post-translational modification that regulates nearly all aspects of eukaryotic cell biology. A diverse collection of ubiquitylation signals, including an extensive repertoire of polymeric ubiquitin chains, leads to
Justin B. Gregor, Dantong Xu, Michael E. French, Michael E. French   +3 more
doaj   +1 more source

A Conditional Yeast E1 Mutant Blocks the Ubiquitin–Proteasome Pathway and Reveals a Role for Ubiquitin Conjugates in Targeting Rad23 to the Proteasome [PDF]

, 2007
E1 ubiquitin activating enzyme catalyzes the initial step in all ubiquitin-dependent processes. We report the isolation of uba1-204, a temperature-sensitive allele of the essential Saccharomyces cerevisiae E1 gene, UBA1.
Amerik A. Y., Babbitt S. E., Bertolaet B. L., Bertolaet B. L., Biggins S., Chen L., Cheng I. H., Ciechanover A., Deshaies R. J., Deveraux Q., Elsasser S., Elsasser S., Elsasser S., Finley D., Funakoshi M., Gandre S., Glickman M. H., Guthrie C., Haas A. L., Haracska L., Hicke L., Hofmann K., Johnson E. S., Kang Y., Kleijnen M. F., Kulka R. G., Lambertson D., Lambertson D., Lowe E. D., Madura K., McGrath J. P., Nazli Ghaboosi, Ortolan T. G., Peng J., Pickart C. M., Raasi S., Raasi S., Rao H., Raymond J. Deshaies, Richly H., Ryu K. S., Saeki Y., Saeki Y., Saeki Y., Salvat C., Schauber C., Schuberth C., Shimada K., Swanson R., Swanson R., van Nocker S., van Nocker S., Verma R., Verma R., Verma R., Walters K. J., Walters K. J., Watkins J. F., Wilkinson C.R.M., William Tansey   +59 more
core   +2 more sources

The Ubiquitination Machinery of the Ubiquitin System [PDF]

The Arabidopsis Book, 2014
The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as well as proteins that bind to ubiquitinated proteins leading them to their final fate.
openaire   +4 more sources

Generation and physiological roles of linear ubiquitin chains [PDF]

, 2012
Ubiquitination now ranks with phosphorylation as one of the best-studied post-translational modifications of proteins with broad regulatory roles across all of biology.
A Ciechanover, A Degterev, A Hershko, A Hershko, A Hershko, A Varshavsky, B Eisenhaber, B Gerlach, C Tokunaga, CK Ea, CM Pickart, CY Ni, DM Wenzel, DW Abbott, EW Doss-Pepe, F Ikeda, F Ikeda, F Ikeda, F Tokunaga, F Tokunaga, F Van Herreweghe, H HogenEsch, H Walczak, H Zhou, Henning Walczak, I Marin, I Marin, Ivan Dikic, J Peng, JN Dynek, JW Harper, Kazuhiro Iwai, KL Lim, M Karin, O Micheau, P Cohen, P de Bie, P Xu, S Hatakeyama, S Rahighi, T Hunter, T Kirisako, TL Haas, V Nagy, VK Chaugule, Y Sato, Y Ye, YC Lo   +47 more
core   +4 more sources

In the family with ubiquitin [PDF]

EMBO reports, 2011
The Cold Spring Harbor meeting on ‘The Ubiquitin family’, held in May 2011, brought together scientists from a wide range of fields, all under the common umbrella of ubiquitin and ubiquitin‐like protein structure, function and regulation.
Alexandru, Gabriela, Pariente, Nonia, Xirodimas, Dimitris   +2 more
openaire   +3 more sources

A novel synthetic chemistry approach to linkage-specific ubiquitin conjugation. [PDF]

, 2015
Ubiquitination is of great importance as the post-translational modification of proteins with ubiquitin, or ubiquitin chains, facilitates a number of vital cellular processes.
Caddick, S, Chudasama, V, Moody, P, Morgan, RE, Smith, ME   +4 more
core   +1 more source

Sugar-Recognizing Ubiquitin Ligases: Action Mechanisms and Physiology

Frontiers in Physiology, 2019
F-box proteins, the substrate recognition subunits of SKP1–CUL1–F-box protein (SCF) E3 ubiquitin ligase complexes, play crucial roles in various cellular events mediated by ubiquitination.
Yukiko Yoshida, Tsunehiro Mizushima, Keiji Tanaka   +2 more
doaj   +1 more source