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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, S., Kalayil, S., Liu, Y., Bonn, F., Colby, T., Matić, I., Dikic, I.   +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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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 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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BRCA1 is a histone-H2A-specific ubiquitin ligase [PDF]

, 2014
The RING domain proteins BRCA1 and BARD1 comprise a heterodimeric ubiquitin (E3) ligase that is required for the accumulation of ubiquitin conjugates at sites of DNA damage and for silencing at DNA satellite repeat regions. Despite its links to chromatin,
Donna L. Mallery, Mallery, D., Conor Larkin, Huang, Jeffrey T.J., Kalb, R., Kevin Hiom, Kalb, Reinhard, Reinhard Kalb, Huang, Jeffrey T. J.; id_orcid, Hiom, Kevin, Hiom, K., Jeffrey T.J. Huang, Larkin, C., Mallery, Donna L., Larkin, Conor, Huang, J.   +15 more
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Distinct ubiquitin binding modes exhibited by SH3 domains: Molecular determinants and functional implications [PDF]

, 2013
SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation.
Jerónimo Bravo (22727), Jose L Ortega Roldan, Jerónimo Bravo, Ana I. Azuaga, Casares Atienza, Salvador, Ringkjøbing Jensen, M, van Nuland, Nico A. J., Azuaga, AI, Malene Ringkjøbing Jensen, Buday, Laszlo, Azuaga, Ana I., Ortega Roldan, Jose L., Martin Blackledge, van Nuland, Nico a J, Martin Blackledge (204261), Cárdenes, N, Nuland, Nico A. J. van, Blackledge, M, Ringkjøbing Jensen, Malene, Azuaga, Ana I, Casares, S, Salvador Casares (69741), Jensen, Malene Ringkjøbing, Ortega-Roldán, José Luis, Casares, Salvador, Nico A. J. van Nuland (116707), Bravo, J, Ortega Roldan, Jose L, Van Nuland, NAJ, Bravo, Jerónimo, Jose L. Ortega Roldan (457421), Azuaga Fortes, Ana Isabel, Ana I. Azuaga (121437), Ortega-Roldan, Jose L., Nico A J van Nuland, Jose L. Ortega Roldan, Malene Ringkjøbing Jensen (204257), Nayra Cárdenes (457422), Cárdenes, Nayra, Nico A. J. Van Nul, Ana I Azuaga, Salvador Casares, Ortega Roldan, JL, Nayra Cárdenes, Blackledge, Martin   +44 more
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