Results 221 to 230 of about 129,362 (255)
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AJP - Renal Physiology, 2011
The E3 ubiquitin (Ub)-protein ligases (E3s) play a role as regulators of protein trafficking and degradation. We aimed to integrate the profile of E3s in rat kidney and examine the changes in protein abundance of the selected E3s in response to 1-deamino-
Yu-Jung Lee+8 more
semanticscholar +1 more source
The E3 ubiquitin (Ub)-protein ligases (E3s) play a role as regulators of protein trafficking and degradation. We aimed to integrate the profile of E3s in rat kidney and examine the changes in protein abundance of the selected E3s in response to 1-deamino-
Yu-Jung Lee+8 more
semanticscholar +1 more source
Identification of the ubiquitin–protein ligase that recognizes oxidized IRP2
Nature Cell Biology, 2003The ubiquitin system is involved in several basic cellular functions. Ubiquitination is carried out by a cascade of three reactions catalysed by the E1, E2 and E3 enzymes. Among these, the E3 ubiquitin-protein ligases have a pivotal role in determining the specificity of the system by recognizing the target substrates through defined targeting motifs ...
Nagahiro Minato+11 more
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Role of Ubiquitin Protein Ligases in the Pathogenesis of Polyglutamine Diseases
Neurochemical Research, 2007The accumulation of intracellular protein deposits as inclusion bodies is the common pathological hallmark of most age related neurodegenerative disorders including polyglutamine diseases. Appearances of aggregates of the misfolded mutant disease proteins suggest that the cells are unable to efficiently degrade them, and failure of clearance leads to ...
Priyanka Dikshit, Nihar Ranjan Jana
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Progress in regulation of activity and stability of ubiquitin protein ligase MDM2
Hereditas (Beijing), 2009The ubiquitin protein ligase (E3) MDM2 (Murine double minute 2) possesses oncogenic activities. Overexpression of this protein enhances degradation and inactivation of the tumor suppressor p53. At least 7% of all human tumors exhibit inappropriate amplification of mdm2, whereas p53 gene remains in its wild-type configuration.
Jing NIE+2 more
openaire +3 more sources
Ring finger ubiquitin protein ligases and their implication to the pathogenesis of human diseases.
Current pharmaceutical design, 2009The ubiquitin proteasome system (UPS) plays a fundamental role in maintaining the correct balance of protein levels inside all living cells. Degradation of proteins by this pathway is essential for most cellular processes including cell signalling, DNA ...
H. Ardley
semanticscholar +1 more source
An Altered-specificity Ubiquitin-conjugating Enzyme/Ubiquitin–Protein Ligase Pair
Journal of Molecular Biology, 2004The human CCR4-NOT complex is a global regulator of RNA polymerase II transcription. Recently, we showed that the RING domain CNOT4 subunit contains intrinsic ubiquitin-protein ligase (E3) activity. Here we show that binding of the CNOT4 RING finger to the ubiquitin-conjugating enzyme (E2) UbcH5B is highly selective.
Winkler, GS+5 more
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RING domain E3 ubiquitin ligases.
Annual Review of Biochemistry, 2009E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate.
R. Deshaies, C. Joazeiro
semanticscholar +1 more source
Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors
Nature Immunology, 2004Activation of Toll-like receptors (TLRs) results in a proinflammatory response needed to combat infection. Thus, limiting TLR signaling is essential for preventing a protective response from causing injury to the host. Here we describe how a RING finger protein, Triad3A, acts as an E3 ubiquitin-protein ligase and enhances ubiquitination and proteolytic
Richard J. Ulevitch, Tsung-Hsien Chuang
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Challenges in the use of sortase and other peptide ligases for site-specific protein modification
Chemical Society Reviews, 2022Holly E Morgan+2 more
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