Results 11 to 20 of about 202,310 (299)

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.
Colby, T., Bonn, F., Dikic, I., Matić, I., Kalayil, S., Liu, Y., Bhogaraju, S.   +6 more
core   +5 more sources

Ubiquitination and De-Ubiquitination in the Synthesis of Cow Milk Fat: Reality and Prospects

Molecules
Ubiquitination modifications permit the degradation of labelled target proteins with the assistance of proteasomes and lysosomes, which is the main protein degradation pathway in eukaryotic cells.
Rui Gao, Yanni Wu, Yuhao Wang, Zhangping Yang, Yongjiang Mao, Yi Yang, Chunhua Yang, Zhi Chen   +7 more
doaj   +2 more sources

PKC-Dependent GlyT1 Ubiquitination Occurs Independent of Phosphorylation: Inespecificity in Lysine Selection for Ubiquitination. [PDF]

PLoS ONE, 2015
Neurotransmitter transporter ubiquitination is emerging as the main mechanism for endocytosis and sorting of cargo into lysosomes. In this study, we demonstrate PKC-dependent ubiquitination of three different isoforms of the glycine transporter 1 (GlyT1).
Susana P Barrera, Vicente Castrejon-Tellez, Margarita Trinidad, Elisa Robles-Escajeda, Javier Vargas-Medrano, Armando Varela-Ramirez, Manuel Miranda   +6 more
doaj   +2 more sources

Non-degradative Ubiquitination of Protein Kinases. [PDF]

PLoS Computational Biology, 2016
Growing evidence supports other regulatory roles for protein ubiquitination in addition to serving as a tag for proteasomal degradation. In contrast to other common post-translational modifications, such as phosphorylation, little is known about how non ...
K Aurelia Ball, Jeffrey R Johnson, Mary K Lewinski, John Guatelli, Erik Verschueren, Nevan J Krogan, Matthew P Jacobson   +6 more
doaj   +3 more sources

SCUD: Saccharomyces Cerevisiae Ubiquitination Database [PDF]

BMC Genomics, 2008
Background Ubiquitination is an important post-translational modification involved in diverse biological processes. Therefore, genomewide representation of the ubiquitination system for a species is important. Description SCUD is a web-based database for
Jung Jin Woo, Lee Minho, Lee Won-Chul, Kim Kwang Pyo, Kim Dongsup   +4 more
doaj   +2 more sources

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

TRAIP Mediates Alcohol-Induced Liver Injury through Regulating β-catenin Ubiquitin Degradation via Direct Interaction. [PDF]

Adv Sci (Weinh)
This study reveals that NF‐κB1‐driven TRAIP upregulation in ALD correlates with disease severity. Mechanistically, TRAIP directly binds β‐catenin via its CC domain and promotes its K48‐linked ubiquitination and degradation, which is independent of the GSK3β/β‐TrCP pathway.
Wu Z, Liu M, Liao L, Mo Z, Xu W, Mao L, Chen Y, Xie Q, Yao M, Chen S, Tomlinson S, Mueller S, He S, Yuan G.   +13 more
europepmc   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources