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Ubiquitin specific peptidase 5

isopeptidase T, Isot, USP5, UCHT
Ubiquitin (see MIM 191339)-dependent proteolysis is a complex pathway of protein metabolism implicated in such diverse cellular functions as maintenance of chromatin structure, receptor function, and degradation of abnormal proteins. A late step of the process involves disassembly of the polyubiquitin chains on degraded proteins into ubiquitin monomers. USP5 disassembles branched polyubiquitin chains by a sequential exo mechanism, starting at the proximal end of the chain (Wilkinson et al., 1995 [PubMed 7578059]).[supplied by OMIM, Mar 2010] (from NCBI)
Top mentioned proteins: Ubiquitin, CAN, Ubiquitin Thiolesterase, ZNF, V1a
Papers using isopeptidase T antibodies
The role of anthrolysin O in gut epithelial barrier disruption during Bacillus anthracis infection.
Ryffel Bernhard, In PLoS ONE, 2009
... Human recombinant N-terminal A20 (TNFAIP3 catalytic DUB domain) and Isopeptidase T were from Boston Biochem (Cambridge, MA) ...
Papers on isopeptidase T
Molecular dynamics of zinc-finger ubiquitin binding domains: a comparative study of histone deacetylase 6 and ubiquitin-specific protease 5.
Nurisso et al., Genève, Switzerland. In J Biomol Struct Dyn, Dec 2015
The behavior was then compared to the prototypical ZnF-UBP from ubiquitin-specific protease 5 (USP5) in order to spot relevant differences useful for selective drug design.
Structural insights into interactions between ubiquitin specific protease 5 and its polyubiquitin substrates by mass spectrometry and ion mobility spectrometry.
Oldham et al., Nottingham, United Kingdom. In Protein Sci, Aug 2015
Nanoelectrospray ionization-mass spectrometry and ion mobility-mass spectrometry have been used to study the interactions of the large, multidomain, and conformationally flexible deubiquitinating enzyme ubiquitin specific protease 5 (USP5) with mono- and poly-ubiquitin (Ub) substrates.
Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5.
Oldham et al., Nottingham, United Kingdom. In Proteomics, Aug 2015
We have applied IM-MS analysis to the multidomain deubiquitinating enzyme ubiquitin specific protease 5 (USP5), which is believed to exhibit significant conformational flexibility.
The de novo synthesis of ubiquitin: identification of deubiquitinases acting on ubiquitin precursors.
Azevedo et al., Porto, Portugal. In Sci Rep, 2014
Using an unbiased biochemical approach we found that UCHL3, USP9X, USP7, USP5 and Otulin/Gumby/FAM105b are by far the most active DUBs acting on these precursors.
Small organic molecule disruptors of Cav3.2 - USP5 interactions reverse inflammatory and neuropathic pain.
Zamponi et al., Calgary, Canada. In Mol Pain, 2014
We reported that this enhancement of Cav3.2 currents in afferent neurons is mediated by deubiquitination of the channels by the deubiquitinase USP5, and that disrupting USP5/Cav3.2
Activity-Based Proteomic Profiling of Deubiquitinating Enzymes in Salmonella-Infected Macrophages Leads to Identification of Putative Function of UCH-L5 in Inflammasome Regulation.
Edelmann et al., United States. In Plos One, 2014
Also, we detected down-regulation of UCH-L3, and USP4 as well as up-regulation of USP5 and UCH-L5 deubiquitinating enzymes in macrophages infected with Salmonella Typhimurium.
Stability and bioactivity of thrombin binding aptamers modified with D-/L-isothymidine in the loop regions.
Yang et al., Beijing, China. In Org Biomol Chem, 2014
Incorporation of L-isothymidine (L-isoT) at T3, T9, T12 positions and D-isoT at the T7 position in TBA's loop regions promoted the formation of G-quadruplex, resulting in enhanced affinity with thrombin and an increased anticoagulant effect.
Regulation of BCL-X splicing reveals a role for the polypyrimidine tract binding protein (PTBP1/hnRNP I) in alternative 5' splice site selection.
Sette et al., Roma, Italy. In Nucleic Acids Res, 2014
Notably, a similar function of PTBP1 in the selection of alternative 5' splice sites was confirmed using the USP5 gene as additional model.
The deubiquitinase Leon/USP5 regulates ubiquitin homeostasis during Drosophila development.
Chien et al., Taipei, Taiwan. In Biochem Biophys Res Commun, 2014
The Drosophila USP5 homolog Leon functions as other family members of unconventional deubiquitinases, disassembling free, substrate-unconjugated polyubiquitin chains to replenish the pool of mono-ubiquitin, and maintaining cellular ubiquitin homeostasis.
The deubiquitinating enzyme USP5 modulates neuropathic and inflammatory pain by enhancing Cav3.2 channel activity.
Zamponi et al., Calgary, Canada. In Neuron, 2014
A proteomic screen identified the deubiquitinating enzyme USP5 as a Cav3.2
Drosophila USP5 controls the activation of apoptosis and the Jun N-terminal kinase pathway during eye development.
Qu et al., Wenzhou, China. In Plos One, 2013
Here, for the first time, we report the phenotypes observed during eye development that are induced by deleting Drosophila USP5 gene, which encodes one of the USP subfamily of DUBs.
A ubiquitin shuttle DC-UbP/UBTD2 reconciles protein ubiquitination and deubiquitination via linking UbE1 and USP5 enzymes.
Hu et al., Shanghai, China. In Plos One, 2013
We identified two Ub-related enzymes, the deubiquitinating enzyme USP5 and the Ub-activating enzyme UbE1, as interacting partners of DC-UbP from HEK 293T cells.
Two ZnF-UBP domains in isopeptidase T (USP5).
Dhe-Paganon et al., Toronto, Canada. In Biochemistry, 2012
USP5 uses multiple zinc fluoride (ZnF)-ubiquitin binding protein (UBP) domains for substrate targeting and core catalytic function.
Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53.
Saville et al., Dundee, United Kingdom. In J Biol Chem, 2009
p53 is selectively stabilized because the unanchored polyubiquitin that accumulates after USP5 knockdown is able to compete with ubiquitinated p53 but not with Mdm2 for proteasomal recognition
The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin.
Wilkinson et al., Atlanta, United States. In Cell, 2006
We report the crystal structures of the zinc-finger ubiquitin binding domain (ZnF UBP) from the deubiquitinating enzyme isopeptidase T (IsoT, or USP5) alone and in complex with ubiquitin. This domain is required for optimal catalytic activation of IsoT.
Further characterization of the putative human isopeptidase T catalytic site.
Gabriel et al., Genève, Switzerland. In Febs Lett, 2002
identification of catalytic site
Selective upregulation of the ubiquitin-proteasome proteolytic pathway proteins, proteasome zeta chain and isopeptidase T in fetal Down syndrome.
Lubec et al., Vienna, Austria. In J Neural Transm Suppl, 2000
Selective upregulation of the ubiquitin-proteasome proteolytic pathway proteins, proteasome zeta chain and isopeptidase T in fetal Down syndrome.
Cross-linking of human T cell receptor proteins: association between the T cell idiotype beta subunit and the T3 glycoprotein heavy subunit.
Strominger et al., In Cell, 1985
The cross-linked cells were solubilized in Nonidet-P40, immunoprecipitated with anti-Ti (monoclonal antibody T40/25) or anti-T3 (monoclonal antibodies UCHT-1 or OKT3), and analyzed by SDS-PAGE.
Polymorphism in mitogenic effect of IgG1 monoclonal antibodies against T3 antigen on human T cells.
Koene et al., In Nature, 1983
We have now tested the mitogenic effect of these antibodies and compared it with the mitogenicity of three other anti-T3 monoclonal antibodies, OKT 3, UCHT 1 (ref.
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