Relevant bibliographies by topics / Ubiquitin ligase

Academic literature on the topic 'Ubiquitin ligase'

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Published: 4 June 2021
Last updated: 21 February 2023

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Journal articles on the topic "Ubiquitin ligase"

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Yoshida, Yukiko, Yasushi Saeki, Arisa Murakami, Junko Kawawaki, Hikaru Tsuchiya, Hidehito Yoshihara, Mayumi Shindo, and Keiji Tanaka. "A comprehensive method for detecting ubiquitinated substrates using TR-TUBE." Proceedings of the National Academy of Sciences 112, no. 15 (March 31, 2015): 4630–35. http://dx.doi.org/10.1073/pnas.1422313112.

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The identification of substrates for ubiquitin ligases has remained challenging, because most substrates are either immediately degraded by the proteasome or processed by deubiquitinating enzymes (DUBs) to remove polyubiquitin. Although a methodology that enables detection of ubiquitinated proteins using ubiquitin Lys-ε-Gly-Gly (diGly) remnant antibodies and MS has been developed, it is still insufficient for identification and characterization of the ubiquitin-modified proteome in cells overexpressing a particular ubiquitin ligase. Here, we show that exogenously expressed trypsin-resistant tandem ubiquitin-binding entity(ies) (TR-TUBE) protect polyubiquitin chains on substrates from DUBs and circumvent proteasome-mediated degradation in cells. TR-TUBE effectively associated with substrates ubiquitinated by an exogenously overexpressed ubiquitin ligase, allowing detection of the specific activity of the ubiquitin ligase and isolation of its substrates. Although the diGly antibody enabled effective identification of ubiquitinated proteins in cells, overexpression of an ubiquitin ligase and treatment with a proteasome inhibitor did not increase the level of diGly peptides specific for the ligase relative to the background level of diGly peptides, probably due to deubiquitination. By contrast, in TR-TUBE–expressing cells, the level of substrate-derived diGly peptides produced by the overexpressed ubiquitin ligase was significantly elevated. We developed a method for identifying the substrates of specific ubiquitin ligases using two enrichment strategies, TR-TUBE and diGly remnant antibodies, coupled with MS. Using this method, we identified target substrates of FBXO21, an uncharacterized F-box protein.
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Lee, Jaeseok, Youngjun Lee, Young Mee Jung, Ju Hyun Park, Hyuk Sang Yoo, and Jongmin Park. "Discovery of E3 Ligase Ligands for Target Protein Degradation." Molecules 27, no. 19 (October 2, 2022): 6515. http://dx.doi.org/10.3390/molecules27196515.

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Target protein degradation has emerged as a promising strategy for the discovery of novel therapeutics during the last decade. Proteolysis-targeting chimera (PROTAC) harnesses a cellular ubiquitin-dependent proteolysis system for the efficient degradation of a protein of interest. PROTAC consists of a target protein ligand and an E3 ligase ligand so that it enables the target protein degradation owing to the induced proximity with ubiquitin ligases. Although a great number of PROTACs has been developed so far using previously reported ligands of proteins for their degradation, E3 ligase ligands have been mostly limited to either CRBN or VHL ligands. Those PROTACs showed their limitation due to the cell type specific expression of E3 ligases and recently reported resistance toward PROTACs with CRBN ligands or VHL ligands. To overcome these hurdles, the discovery of various E3 ligase ligands has been spotlighted to improve the current PROTAC technology. This review focuses on currently reported E3 ligase ligands and their application in the development of PROTACs.
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Kilroy, Gail, Heather Kirk-Ballard, Lauren E. Carter, and Z. Elizabeth Floyd. "The Ubiquitin Ligase Siah2 Regulates PPARγ Activity in Adipocytes." Endocrinology 153, no. 3 (March 1, 2012): 1206–18. http://dx.doi.org/10.1210/en.2011-1725.

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Moderate reductions in peroxisome proliferator-activated receptor (PPAR)γ levels control insulin sensitivity as effectively as activation of PPARγ in adipocytes by the thiazolidinediones. That observation suggests that PPARγ activity can be regulated by modulating the amount of PPARγ protein in adipocytes. Activation of PPARγ in adipocytes is linked to changes in PPARγ protein levels via increased degradation of PPARγ proteins by the ubiquitin proteasome system. Identification of the ubiquitin ligase or ligases that recognize ligand bound PPARγ is an essential step in determining the physiological significance of the relationship between activation and ubiquitin-dependent degradation of PPARγ. Using an RNA interference-based screen, we identified five RING (really interesting new gene)-type ubiquitin ligases that alter PPARγ protein levels in adipocytes. Here, we demonstrate that Drosophila seven-in-absentia homolog 2 (Siah2), a mammalian homolog of Drosophila seven-in-absentia, regulates PPARγ ubiquitylation and ligand-dependent activation of PPARγ in adipocytes. We also demonstrate that Siah2 expression is up-regulated during adipogenesis and that PPARγ interacts with Siah2 during adipogenesis. In addition, Siah2 is required for adipogenesis. These data suggest that modulation of PPARγ protein levels by the ubiquitin ligase Siah2 is essential in determining the physiological effects of PPARγ activation in adipocytes.
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Fang, Nancy N., and Thibault Mayor. "Hul5 ubiquitin ligase." Prion 6, no. 3 (July 2012): 240–44. http://dx.doi.org/10.4161/pri.19929.

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Qian, Hao, Ying Zhang, Boquan Wu, Shaojun Wu, Shilong You, Naijin Zhang, and Yingxian Sun. "Structure and function of HECT E3 ubiquitin ligases and their role in oxidative stress." Journal of Translational Internal Medicine 8, no. 2 (June 30, 2020): 71–79. http://dx.doi.org/10.2478/jtim-2020-0012.

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AbstractUbiquitination is a modification after protein transcription that plays a vital role in maintaining the homeostasis of the cellular environment. The Homologous to E6AP C-terminus (HECT) family E3 ubiquitin ligases are a kind of E3 ubiquitin ligases with a C-terminal HECT domain that mediates the binding of ubiquitin to substrate proteins and a variable-length N-terminal extension. HECT-ubiquitinated ligases can be divided into three categories: NEDD4 superfamily, HERC superfamily, and other HECT superfamilies. HECT ubiquitin ligase plays an essential role in the development of many human diseases. In this review, we focus on the physiological and pathological processes involved in oxidative stress and the role of E3 ubiquitin ligase of the HECT family.
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Ibarra, Rebeca, Heather R. Borror, Bryce Hart, Richard G. Gardner, and Gary Kleiger. "The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites." Biomolecules 11, no. 11 (November 2, 2021): 1619. http://dx.doi.org/10.3390/biom11111619.

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Cellular homeostasis depends on robust protein quality control (PQC) pathways that discern misfolded proteins from functional ones in the cell. One major branch of PQC involves the controlled degradation of misfolded proteins by the ubiquitin-proteasome system. Here ubiquitin ligases must recognize and bind to misfolded proteins with sufficient energy to form a complex and with an adequate half-life to achieve poly-ubiquitin chain formation, the signal for protein degradation, prior to its dissociation from the ligase. It is not well understood how PQC ubiquitin ligases accomplish these tasks. Employing a fully reconstituted enzyme and substrate system to perform quantitative biochemical experiments, we demonstrate that the yeast PQC ubiquitin ligase San1 contains multiple substrate binding sites along its polypeptide chain that appear to display specificity for unique misfolded proteins. The results are consistent with a model where these substrate binding sites enable San1 to bind to misfolded substrates avidly, resulting in high affinity ubiquitin ligase-substrate complexes.
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Kelsall, Ian R., Jiazhen Zhang, Axel Knebel, J. Simon C. Arthur, and Philip Cohen. "The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells." Proceedings of the National Academy of Sciences 116, no. 27 (June 17, 2019): 13293–98. http://dx.doi.org/10.1073/pnas.1905873116.

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The linear ubiquitin assembly complex (LUBAC) comprises 3 components: HOIP, HOIL-1, and Sharpin, of which HOIP and HOIL-1 are both members of the RBR subfamily of E3 ubiquitin ligases. HOIP catalyses the formation of Met1-linked ubiquitin oligomers (also called linear ubiquitin), but the function of the E3 ligase activity of HOIL-1 is unknown. Here, we report that HOIL-1 is an atypical E3 ligase that forms oxyester bonds between the C terminus of ubiquitin and serine and threonine residues in its substrates. Exploiting the sensitivity of HOIL-1–generated oxyester bonds to cleavage by hydroxylamine, and macrophages from knock-in mice expressing the E3 ligase-inactive HOIL-1[C458S] mutant, we identify IRAK1, IRAK2, and MyD88 as physiological substrates of the HOIL-1 E3 ligase during Toll-like receptor signaling. HOIL-1 is a monoubiquitylating E3 ubiquitin ligase that initiates the de novo synthesis of polyubiquitin chains that are attached to these proteins in macrophages. HOIL-1 also catalyses its own monoubiquitylation in cells and most probably the monoubiquitylation of Sharpin, in which ubiquitin is also attached by an oxyester bond. Our study establishes that oxyester-linked ubiquitylation is used as an intracellular signaling mechanism.
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Marblestone, Jeffrey G., K. G. Suresh Kumar, Michael J. Eddins, Craig A. Leach, David E. Sterner, Michael R. Mattern, and Benjamin Nicholson. "Novel Approach for Characterizing Ubiquitin E3 Ligase Function." Journal of Biomolecular Screening 15, no. 10 (September 23, 2010): 1220–28. http://dx.doi.org/10.1177/1087057110380456.

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The ubiquitin-proteasome system is central to the regulation of numerous cellular events, and dysregulation may lead to disease pathogenesis. E3 ubiquitin ligases typically function in concert with E1 and E2 enzymes to recruit specific substrates, thereby coordinating their ubiquitylation and subsequent proteasomal degradation or cellular activity. E3 ligases have been implicated in a wide range of pathologies, and monitoring their activity in a rapid and cost-effective manner would be advantageous in drug discovery. The relative lack of high-throughput screening (HTS)–compliant E3 ligase assays has significantly hindered the discovery of E3 inhibitors. Herein, the authors describe a novel HTS-compliant E3 ligase assay platform that takes advantage of a ubiquitin binding domain’s inherent affinity for polyubiquitin chains, permitting the analysis of ubiquitin chain formation in an E3 ligase-dependent manner. This assay has been used successfully with members of both the RING and HECT families, demonstrating the platform’s broad utility for analyzing a wide range of E3 ligases. The utility of the assay platform is demonstrated by the identification of inhibitors of the E3 ligase CARP2. As the number of E3 ligases associated with various disease states increases, the ability to quantitate the activity of these enzymes in an expeditious manner becomes imperative in drug discovery.
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Toma-Fukai, Sachiko, and Toshiyuki Shimizu. "Structural Diversity of Ubiquitin E3 Ligase." Molecules 26, no. 21 (November 4, 2021): 6682. http://dx.doi.org/10.3390/molecules26216682.

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The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure of PCAF_N, a newly categorized E3 ligase, was reported. We present a review of the recent progress toward the structural understanding of E3 ligases.
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Kelley, Dior R. "E3 Ubiquitin Ligases: Key Regulators of Hormone Signaling in Plants." Molecular & Cellular Proteomics 17, no. 6 (March 7, 2018): 1047–54. http://dx.doi.org/10.1074/mcp.mr117.000476.

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Ubiquitin-mediated control of protein stability is central to most aspects of plant hormone signaling. Attachment of ubiquitin to target proteins occurs via an enzymatic cascade with the final step being catalyzed by a family of enzymes known as E3 ubiquitin ligases, which have been classified based on their protein domains and structures. Although E3 ubiquitin ligases are conserved among eukaryotes, in plants they are well-known to fulfill unique roles as central regulators of phytohormone signaling, including hormone perception and regulation of hormone biosynthesis. This review will highlight up-to-date findings that have refined well-known E3 ligase-substrate interactions and defined novel E3 ligase substrates that mediate numerous hormone signaling pathways. Additionally, examples of how particular E3 ligases may mediate hormone crosstalk will be discussed as an emerging theme. Looking forward, promising experimental approaches and methods that will provide deeper mechanistic insight into the roles of E3 ubiquitin ligases in plants will be considered.
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Dissertations / Theses on the topic "Ubiquitin ligase"

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Fan, Jun. "Investigating the crosstalk between Nedd4 ubiquitin ligases and PIAS3 SUMO ligase." Thesis, Queen Mary, University of London, 2017. http://qmro.qmul.ac.uk/xmlui/handle/123456789/31791.

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Previously it has been shown that Rsp5p, a member of Nedd4 ubiquitin ligases in yeast, is modified by the ubiquitin-like protein SUMO and that this modification is performed by Siz1p, a member of PIAS SUMO ligases that are in turn substrates of Rsp5p-dependent ubiquitylation, thus defining a previously unidentified system of crosstalk between the ubiquitin and SUMO systems in yeast. This project aims to identify whether similar crosstalk pattern exists in human cells. In vitro ubiquitylation assays showed that some of the human Nedd4 family members (Nedd4.1, Nedd4.2, WWP1) are capable of ubiquitylating the human SUMO ligase PIAS3, while in contrast, Smurf2 does not appear to be able to modify this protein. This modification is partially WW-PY-motif-dependent as ubiquitylation level of PIAS3 mutants with altered PY motifs conducted by Nedd4.1 or Nedd4.2 was reduced, but not completely disrupted. Interestingly, in vitro SUMOylation assay revealed that Nedd4.1 is SUMOylated even in the absence of SUMO E3 ligases and an apparent interaction between the SUMO E2 (Ubc9) and Nedd4.1 was observed both in vitro and in vivo. I show that auto- SUMOylation of Nedd4.1 is accompanied with the formation of thioester-linked conjugates between Nedd4.1 and SUMO, but these do not involve cysteine residues (C867, C778, and C627) within the HECT domain itself and is not occurring at a predicted SUMOylation consensus site (K357). Furthermore, I have shown that Nedd4.1 and SUMO1/2 colocalize in HeLa cells, and that overexpression of epitope tagged Nedd4 and SUMO1/2, followed by denaturing pull-downs demonstrates that both Nedd4.1 and Nedd4.2 can be SUMOylated in vivo. Meanwhile, I have generated a SUMO trap based on SUMO interacting motifs (SIMs) and confirmed its ability of capturing SUMOylated proteins both in vivo and in vitro. Its use reveals that Nedd4 SUMO conjugates could be captured by SUMO trap when Nedd4 and SUMO were co-expressed in HeLa cells, again confirming Nedd4.1 as a substrate for SUMO1 or SUMO2. In conclusion, I show that SUMOylation of Nedd4.1 does exist in HeLa cells, and on the other hand, some of Nedd4 family members are responsible for PIAS3 ubiquitylation in vitro, providing evidence of a crosstalk between Nedd4 family of ubiquitin ligases and PIAS family of SUMO ligases in mammals.
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Nathan, James Alexander. "The RING-CH ubiquitin E3 ligase MARCH7." Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612286.

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Depaux, Arnaud. "Régulation des complexes d'ubiquitinylation et de sumoylation par la ligase E3 hSIAH2." Paris 7, 2006. http://www.theses.fr/2006PA077094.

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Les modifications post-traductionnelles des protéines (phosphorylation, l'acétylation ou l'ubiquitinylation) permettent de réguler leur activité, stabilité, localisation ou interactions avec d'autres facteurs. Les complexes permettant la modification par l'ubiquitine ou Sumo bien que d'organisation similaire sont composés de protéines différentes : une ligase El qui active le résidu, une ligase E2 permettant le transfert de l'ubiquitine sur le substrat et une ligase E3 qui assure la spécificité de reconnaissance du substrat. Plusieurs familles de ligases E3 ont été décrites mais seule la famille de protéines à domaine RING Finger présente des membres impliqués dans les complexes de la sumoylation et de l'ubiquitinylation. Afin de caractériser de nouveaux partenaires des ligases à domaine RING Finger hSIAHl et hSIAH2 (human Seven In Absentia homolog), nous avons développé une expérience de double-hybride chez la levure en utilisant hSIAH2 pour appât. La caractérisation des partenaires ainsi isolés a fait l'objet de mon projet de thèse. J'ai mis en évidence des protéines impliquées dans l'ubiquitinylation (Ubiquitine, Ubc5 ou hSIAH) et la sumoylation (PIAS, SUMO et Ubc9). J'ai ainsi démontré que hSIAH2 est capable de former des homodimères et des hétérodimères avec hSIAH et que cette dimérisation permet de réguler la propre stabilité des deux protéines. D'autre part, j'ai montré que hSIAH2 catalyse l'ubiquitinylation de PIAS et sa dégradation par le protéasome. L'ensemble de ce travail a mis en évidence le rôle spécifique de hSIAH2 dans la régulation de la stabilité d'intermédiaires essentiels, à la fois, aux complexes d'ubiquitinylation et de sumoylation
After synthesis, proteins are targeted to post-translational modifications such as acetylation, phosphorylation or ubiquitination. These mechanisms regulate their function, stability, localization or interaction with partners. Modification process by ubiquitin or sumo named ubiquitination or sumoylation respectively involve complexes with similar organization but compose of different enzymes. Their organization relies on Sumo or ubiquitin activating El enzyme, transferring E2-ligase and E3-ligase or sub-complex conferring the substrate specific récognition. El-ligase is unique for each complex, whereas E2 and E3-ligases are multiple. Among E3-ligase families, RING Finger protein family only has been involved in both modifications complexes. Two human homologs of Drosophila Seven In Absentia (hSIAHl et hSIAH2), belong to RING Finger E3-ligase family. In a yeast two hybrid assay, we have identified new SIAH interacting proteins. Their characterization has been the purpose of my PhD project. We have characterized partners implicated in both ubiquitination (ubiquitin, Ubc5 or hSIAH) and sumoylation (Sumo, Ubc9 and PIAS) pathways. In a first attempt, I have demonstrated that hSIAH proteins can form homo- or hetero-dimers. Dimerization régulates their stability via a proteasome dependent degradation. I have also demonstrated that hSIAH2 catalyzes the proteasome dependent degradation of PIAS1, a sumo E3-ligase. Altogether this study evidences an important rôle for hSIAH2 in the regulation of the stability of ubiquitination and sumolation complexes
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Bazirgan, Omar Al-Kasim. "Functional analysis of the ubiquitin ligase Hrd1p with the ubiquitin-conjugating enzyme Ubc7p." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2007. http://wwwlib.umi.com/cr/ucsd/fullcit?p3246079.

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Thesis (Ph. D.)--University of California, San Diego, 2007.
Title from first page of PDF file (viewed March 9, 2007). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references.
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Wertz, Ingrid E. "Identification and characterization of novel ubiquitin ligase enzymes /." For electronic version search Digital dissertations database. Restricted to UC campuses. Access is free to UC campus dissertations, 2004. http://uclibs.org/PID/11984.

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Harvey, Kieran F. "Functional characterisation of the ubiquitin-protein ligase, Nedd4." Title page, contents and abstract only, 2000. http://web4.library.adelaide.edu.au/theses/09PH/09phh3411.pdf.

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Addenda pasted into back end-paper. Bibliography: leaves 107-147. The studies presented in this thesis have identified Nedd4 as a key protein involved in Na+-dependent downregulation of the epithelial Na+ channel (ENaC). These studies have aided in the molecular understanding of the familial hypertensive disorder, Liddle's syndrome, and the regulation of blood pressure in general.
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Cooper, S. E. "Studies of the E3 ubiquitin ligase Sina-Homologue." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.597976.

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I have identified Sina-Homologue (SinaH) as a novel Drosophila protein that is homologous to the E3 ubiquitin ligase Sina, but has different expression patterns throughout development. In this thesis I investigate the biochemical mechanisms of SinaH directed degradation in cells, and the physiological role of SinaH in Drosophila. I show that SinaH can direct the degradation of the transcriptional repressor Tramtrack using two different mechanisms. One is similar to Sina and requires the adaptor Phyllopod (Phyl), and the other is a novel mechanism of recognition. This novel mode of targeting for degradation is specific for the Tramtrack isoform, Ttk69. Ttk69 contains a region that is required for binding of SinaH and for SinaH directed degradation. This region contains an AxVxP motif, which is the consensus sequence found in substrates of the mammalian Sina like proteins. These results suggest that degradation directed by SinaH is more similar to that found in higher eukaryotes. In order to identify novel SinaH substrates and potential adaptor proteins, a yeast 2-hybrid screen was carried out. As well as others, this identified Numb as a potential substrate, and the protein Bruce as an E2 ligase and adaptor molecule. GST pulldown assays and coimmunoprecipitation experiments were used to verify some of these interactors, and Numb was found to be directed for degradation in cells. Flies that were deficient in SinaH and in Sina and SinaH were created using homogolous recombination. The genetic data, cell degradation assays and expression profiles together suggest that Sina and SinaH have distinct functions.
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Van, den Boomen Dick Johannes Hendrikus. "Functional characterisation of the TRC8 E3 ubiquitin ligase." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609481.

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Chaugule, V. K. "Regulation of the ubiquitin RING E3 ligase Parkin." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1306179/.

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Post-translational modification of proteins by ubiquitin is a central regulatory process in all eukaryotic cells. Substrate selection and type of modification are events catalyzed by the E3 ligase, a component of the ubiquitin pathway. Several ubiquitin E3 ligases are implicated in cancer and other disease states, underlying the need for mechanistic insight of these enzymes. Parkinson’s disease is a neurodegenerative disorder characterised by the loss of dopaminergic neurons from the substantia nigra, the presence of Lewy Bodies, and pathogenic aggregates rich in ubiquitin. Autosomal Recessive Juvenile Parkinsonism (AR-JP), which is one of the most common familial forms of the disease, is directly linked to mutations in the Parkin gene (PARK2). Parkin is a RING E3 and catalyses a range of ubiquitination events (mono, multi mono, K48- and K63- linked poly) in concert with several E2s on a variety of substrates, including itself. Furthermore, Parkin is capable of binding the 26S proteasome and mediates selective degradation of target substrates. The data presented will demonstrate that the Ubiquitin-like domain (UblD) of Parkin functions to inhibit its auto-ubiquitination via a novel mechanism. Pathogenic Parkin mutations disrupt this inhibition and result in a constitutively active molecule. The inhibition is mediated by an intra-molecular interaction between UblD and the C-terminus of Parkin, and Lysine 48 on UblD participates in this interaction. The study also uncovered unique UblD/Ubiquitin Binding Regions (UBRs) on the C-terminus of Parkin that play a novel role in its RING E3 ligase activity. The observations provide critical mechanistic insights into the myriad functions of Parkin and the underlying basis of Parkinson’s disease.
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Cheng, Chi Ying. "Characterization of the adenovirus E4orf6/E1B55K E3 ubiquitin ligase." Thesis, McGill University, 2011. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=103505.

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Human adenovirus type 5 (Ad5) has been engineered as therapeutic oncolytic viruses to selectively kill cancer cells. The earliest and most widely used is the Ad5 ONYX-015 virus which lacks the viral protein E1B55K. The adenoviral proteins E1B55K and E4orf6 were shown previously to be important for multiple functions during viral infection. Most of these functions are dependent on their formation of the E3 ligase complex with cellular proteins Cul5, Elongins B and C, and Rbx1. Therefore, in order to improve the current oncolytic adenovirus therapy, a better understanding on this E3 ligase complex is required. As the E4orf6/E1B55K E3 ligase contains components similar to other cullin E3 ligase complexes, the mechanism of the E3 ligase assembly was investigated. I showed that the E4orf6/E1B55K E3 ligase complex is formed in an unconventional way: E4orf6 uniquely contains three BC box motifs for its interaction with Elongin C unlike other cellular proteins, which contain only one BC box. In addition, the complex utilises neither of the two known mechanisms for recruiting Cul5. Ad5 is by far the best characterized of the more than fifty different adenovirus serotypes; however, it is unclear how representative its properties are with respect to all adenoviruses. Thus, the conservation of the E4orf6/E1B55K E3 ligase was studied systematically in members of other adenovirus subgroups. I demonstrated that the E4orf6 and E1B55K proteins from all serotypes can form an E3 ligase complex but with different cullin specificities: Ad4, Ad5, Ad9 and Ad34 recruit primarily Cul5, Ad12 and Ad40 recruit primarily Cul2, and Ad16 can recruit both. As for function, I showed that different serotypes degrade different ranges of substrates with the only common substrate to all being DNA ligase IV. I found clear evidence that E1B55K is the substrate binding component of the complex; however, I demonstrated that there is no correlation between binding and the capability to degrade specific substrates. These studies have shown clearly that considerable heterogeneity exists in the formation and function of the adenovirus E4orf6/E1B55K E3 ligase.
L'adénovirus humain de type 5 (Ad5) a été modifié génétiquement à des fins thérapeutiques afin d'éliminer sélectivement les cellules cancéreuses. Le premier virus décrit et le plus communément utilisé est le Ad5 virus ONYX-015 dans lequel la protéine virale E1B55K est absente. Il a été précédemment démontré que les protéines adénovirales E1B55K et E4orf6 sont importantes pour de multiples fonctions lors de l'infection virale. La plupart de ces fonctions dépendent de la formation du complexe E3 ligase avec les protéines cellulaires Cul5, Elongine B et C, ainsi que Rbx1. Ainsi, une meilleure compréhension de ce complexe E3 ligase est nécessaire à l'amélioration des thérapies oncolytiques adénovirales actuelles. Puisque le complexe E4orf6/E1B55K E3 ligase contient des composants similaires à d'autres complexes culline E3 ligase, nous avons étudié le mécanisme d'assemblage de l'E3 ligase. J'ai ainsi démontré que le complexe E4orf6/E1B55K E3 ligase est formé de façon non conventionnelle : E4orf6 contient uniquement trois motifs BC pour son interaction avec l'Elongine C contrairement aux protéines cellulaires qui n'en contiennent qu'un. De plus, le complexe n'utilise aucun des deux mécanismes connus pour recruter Cul5. Ad5 est de loin le mieux caractérisé des plus de cinquante sérotypes différents d'adénovirus, pourtant on ne sait pas exactement à quel point ses propriétés sont représentatives des autres sérotypes, d'où l'importance de l'étude systématique de la conservation du complexe E4orf6/E1B55K E3 ligase parmi les membres des autres sous-groupes d'adénovirus. J'ai démontré que les protéines E4orf6 et E1B55K peuvent former un complexe E3 ligase dans tous les sérotypes, mais avec des cullines spécifiques différentes : les sérotypes viraux Ad4, Ad5, Ad9 et Ad34 recrutent principalement Cul5, Ad12 et Ad40 recrute principalement Cul2 alors que Ad16 recrute à la fois Cul5 et Cul2. En ce qui concerne les fonctions, j'ai démontré que différents sérotypes sont capables de dégrader des substrats différents, le seul substrat commun à tous les sérotypes étant la ligase d'ADN IV. J'ai mis en évidence qu'E1B55K est le membre du complexe qui se lie au substrat, mais il n'y a pas de correspondance entre la capacité de lier un substrat et celle de le dégrader. Ces expériences ont clairement démontré la grande hétérogénéité existant entre la formation et les fonctions du complexe adénoviral E4orf6/E1B55K E3 ligase.
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Books on the topic "Ubiquitin ligase"

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Di, Napoli Mario, and Wójcik Cezary 1968-, eds. The ubiquitin proteasome system in the central nervous system: From physiology to pathology : 2008 update. Hauppauge, NY: Nova Science, 2009.

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Hyŏmnyŏktan, Koryŏ Taehakkyo Sanhak. E3, ubiquitin ligase chŏhaeje rŭl wihan E1-E2-E3-substrate cognate pair network chŏngnip kisul kaebal kwa i rŭl iyong han tanangsŏng sinjŭnghugun (ADPKD) ch'iryoje kaebal yŏn'gu =: Study on E1-E2-E3-substrate cognate pair network for E3 ligase inhibitor and application. [Seoul]: Pogŏn Pokchi kajokpu, 2008.

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Inuzuka, Hiroyuki, and Wenyi Wei. SCF and APC E3 Ubiquitin Ligases in Tumorigenesis. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05026-3.

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Inuzuka, Hiroyuki. SCF and APC E3 ubiquitin ligases in tumorigenesis. Cham: Springer, 2014.

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Harris, Edward T. Ubiquitin Ligase: New Insights, Emerging Roles and Clinical Implications. Nova Science Publishers, Incorporated, 2017.

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Groettrup, Marcus. Conjugation and Deconjugation of Ubiquitin Family Modifiers. Springer, 2010.

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Groettrup, Marcus. Conjugation and Deconjugation of Ubiquitin Family Modifiers. Springer, 2016.

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Conjugation And Deconjugation Of Ubiquitin Family Modifiers. Springer, 2010.

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Smith, Derek B. Investigating a role for the ubiquitin ligase Itch in lymphocyte development. 2005.

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Plant, Pamela J. A role for the C2 domain of the ubiquitin-protein ligase Nedd4. 2000.

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Book chapters on the topic "Ubiquitin ligase"

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Schomburg, Dietmar, and Dörte Stephan. "Ubiquitin-calmodulin ligase." In Enzyme Handbook 17, 321–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58969-0_75.

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Westermann, Frank. "Ubiquitin Ligase SCF-Skp2." In Encyclopedia of Cancer, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-27841-9_6086-3.

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Westermann, Frank. "Ubiquitin Ligase SCF-Skp2." In Encyclopedia of Cancer, 4709–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_6086.

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Westermann, Frank. "Ubiquitin Ligase SCF-Skp2." In Encyclopedia of Cancer, 3825–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_6086.

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Tang, Juan, and Jian Zhang. "E3 Ubiquitin Ligase CBL-B." In Encyclopedia of Signaling Molecules, 1471–77. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101569.

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Tokuyama, Takeshi, and Shigeru Yanagi. "Mitochondrial Ubiquitin Ligase MITOL/MARCH5." In Encyclopedia of Signaling Molecules, 3130–37. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101579.

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Higa, Leigh Ann, and Hui Zhang. "The SCF Ubiquitin E3 Ligase." In Protein Degradation, 135–55. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/352760586x.ch6.

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Tang, Juan, and Jian Zhang. "E3 Ubiquitin Ligase CBL-B." In Encyclopedia of Signaling Molecules, 1–6. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101569-1.

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Tokuyama, Takeshi, and Shigeru Yanagi. "Mitochondrial Ubiquitin Ligase MITOL/MARCH5." In Encyclopedia of Signaling Molecules, 1–7. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101579-1.

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Yu, Tao, Yinfeng Zhang, and Pei-feng Li. "Mitochondrial Ubiquitin Ligase in Cardiovascular Disorders." In Advances in Experimental Medicine and Biology, 327–33. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-55330-6_17.

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Conference papers on the topic "Ubiquitin ligase"

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Zhi, Xu, Dong Zhao, Zhongmei Zhou, and Ceshi Chen. "Abstract 213: RNF126 E3 ubiquitin ligase targets p21cipfor ubiquitin-mediated degradation." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-213.

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Yoshida, Yukiko, Koji Matsuoka, Tomoki Chiba, Toshiaki Suzuki, Keiji Tanaka, and Tadashi Tai. "N-GLYCANS ARE RECOGNIZED BY E3 UBIQUITIN-LIGASE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.430.

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Cole, Alexander J., Kristie-Ann Dickson, Roderick Clifton-Bligh, and Deborah J. Marsh. "Abstract 3538: Targeting the E3 ubiquitin ligase RNF20 in ovarian cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3538.

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"Functional roles of the E3 ubiquitin ligase HYD in Drosophila tissues." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-012.

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Nelson, David E., and Heike Laman. "Abstract 2961: Spatiotemporal regulation of the SCF ubiquitin ligase component, Fbxo7." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2961.

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Ho, King Ching, and Xiaolong Yang. "Abstract 5097: ITCH E3 ubiquitin ligase regulates LATS1 tumor suppressor stability." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5097.

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Scott, Timothy L., Suganya Rangaswamy, Bithika Dhar, LianTeng Zhi, Hansruedi Bueler, and Tadahide Izumi. "Abstract 622: Degradation of APE1 by the E3 ubiquitin ligase Parkin." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-622.

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Hatchwell, Luke, Adan Collison, Ana Pereira de Siqueira, Paul S. Foster, Nicole Verrills, Anthony Don, Peter Wark, and Joerg Mattes. "A Novel E3 Ubiquitin Ligase Links Rhinovirus Infection To Exacerbation Of Asthma." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a6198.

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Wang, Zehua, Arun Seth, and Ceshi Chen. "Abstract 509: RNF115/BCA2 E3 ubiquitin ligase promotes breast cancer cell proliferation through targeting p21Waf1/Cip1for ubiquitin-mediated degradation ." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-509.

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Blank, M. "PO-208 Emerging roles of HECT type E3 ubiquitin ligase smurf2 in cancer." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.243.

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Reports on the topic "Ubiquitin ligase"

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Royer, Lacey. Cul3 Ubiquitin Ligase and Ctb73 Protein Interactions. Portland State University Library, January 2014. http://dx.doi.org/10.15760/honors.48.

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Zhang, Hui. The Role of Ubiquitin E3 Ligase SCFSKP2 in Prostate Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, February 2005. http://dx.doi.org/10.21236/ada435854.

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Davidge, Brittney. The Cul3 Ubiquitin Ligase: An Essential Regulator of Diverse Cellular Processes. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5666.

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Chen, Ceshi. The Oncogenic Role of WWP1 E3 Ubiquitin Ligase in Prostate Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, May 2011. http://dx.doi.org/10.21236/ada549835.

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Zhang, Hui. The Role of Ubiquitin E3 Ligase SCF-SKP2 in Prostate Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, February 2007. http://dx.doi.org/10.21236/ada470865.

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Mitchell, Jennifer. Characterization of Functional Domains of Cul3, an E3 Ubiquitin Ligase, Using Chimeric Analysis. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.1969.

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Chen, Xiaowei. BRCC36, A Novel Subunit of a BRCA1 E3 Ubiquitin Ligase Complex: Candidates for BRCA3. Fort Belvoir, VA: Defense Technical Information Center, June 2005. http://dx.doi.org/10.21236/ada440291.

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Spiegelman, Vladimir S. The Role of Beta-TrCP Ubiquitin Ligase Receptor in the Development of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 2006. http://dx.doi.org/10.21236/ada484616.

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Chen, Xiaowei. BRCC36, a Novel Subunit of a BRCA1 E3 Ubiquitin Ligase Complex: Candidates for BRCA3. Fort Belvoir, VA: Defense Technical Information Center, June 2008. http://dx.doi.org/10.21236/ada486006.

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Harper, Jeffrey. Regulation of NF (kappa) B-Dependent Cell Survival Signals Through the SCF (Slimb) Ubiquitin Ligase Pathway. Fort Belvoir, VA: Defense Technical Information Center, July 2000. http://dx.doi.org/10.21236/ada395543.

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