Results 11 to 20 of about 383,830 (310)

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
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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.
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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, Sagar, Kalayil, Sissy, Liu, Yaobin, Bonn, Florian, Colby, Thomas, Matic, Ivan, Dikic, Ivan   +6 more
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Using Ubiquitin Binders to Decipher the Ubiquitin Code [PDF]

Trends in Biochemical Sciences, 2019
Post-translational modifications (PTMs) by ubiquitin (Ub) are versatile, highly dynamic, and involved in nearly all aspects of eukaryote biological function. The reversibility and heterogeneity of Ub chains attached to protein substrates have complicated their isolation, quantification, and characterization.
Mattern M, Sutherland JD, Kadimisetty K, Barrio R, Rodriguez M   +4 more
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Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G., Hay, Ronald T., Larsen, Ida B., Kragelund, Birthe B., Tatham, Michael H, Rösner, Heike I, Kragelund, Birthe Brandt, Hay, Ronald T, Kragelund, Birthe B, Kriegenburg, Franziska, Tatham, Michael H., Rösner, Heike Ilona, Paraskevopoulos, Konstantinos, Brandstrup, Rikke, Larsen, Ida B, Medina, Bethan; id_orcid, Hartmann-Petersen, Rasmus, Gordon, Colin, Rösner, Heike I., Hardwick, Kevin G, Medina, Bethan   +20 more
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Ubiquitin in Motion: Structural Studies of the Ubiquitin-Conjugating Enzyme∼Ubiquitin Conjugate [PDF]

Biochemistry, 2011
Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functional ubiquitin ligase (E3) complex poised for Ub transfer
Jonathan N, Pruneda, Kate E, Stoll, Laura J, Bolton, Peter S, Brzovic, Rachel E, Klevit   +4 more
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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.
Iwai Kazuhiro, Walczak, H, Walczak, Henning, Kazuhiro Iwai, Walczak Henning, Đikić, Ivan, Ivan Dikic, Iwai, Kazuhiro, Iwai, K, Dikic, I, Dikic Ivan, Henning Walczak   +11 more
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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.
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Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation [PDF]

, 2012
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately ...
Amanda Denuc, Marfany Gemma, Denuc Isern, Amanda, Burr, A. A., Gemma Marfany, Blount Jessica R., Sokol V Todi, Todi Sokol V., Marfany i Nadal, Gemma, Jessica R Blount, Denuc Amanda, Blount, J. R., Aaron A Burr, Burr Aaron A., Todi, Sokol V.   +14 more
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Ubiquitin-dependent and -independent proteasomal protein degradation.

, 2023
A. UPS protein degradation resulting from (1) ubiquitin system targeting followed by (2) proteasomal protein degradation. B. Proteins with ubiquitin-independent degrons are directly bound and degraded by the proteasome without ubiquitin system targeting.
Frank W. Albert (7879037), Randi Avery (15383490), Mahlon A. Collins (15383487)   +2 more
core   +1 more source