Relevant bibliographies by topics / NEDD8 E3 ligases

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  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'NEDD8 E3 ligases'

Author: Grafiati
Published: 1 February 2023

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Journal articles on the topic "NEDD8 E3 ligases"

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Furukawa, Manabu, Yanping Zhang, Joseph McCarville, Tomohiko Ohta, and Yue Xiong. "The CUL1 C-Terminal Sequence and ROC1 Are Required for Efficient Nuclear Accumulation, NEDD8 Modification, and Ubiquitin Ligase Activity of CUL1." Molecular and Cellular Biology 20, no. 21 (2000): 8185–97. http://dx.doi.org/10.1128/mcb.20.21.8185-8197.2000.

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ABSTRACT Members of the cullin and RING finger ROC protein families form heterodimeric complexes to constitute a potentially large number of distinct E3 ubiquitin ligases. We report here that the highly conserved C-terminal sequence in CUL1 is dually required, both for nuclear localization and for modification by NEDD8. Disruption of ROC1 binding impaired nuclear accumulation of CUL1 and decreased NEDD8 modification in vivo but had no effect on NEDD8 modification of CUL1 in vitro, suggesting that ROC1 promotes CUL1 nuclear accumulation to facilitate its NEDD8 modification. Disruption of NEDD8
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Baek, Kheewoong, Daniel C. Scott, and Brenda A. Schulman. "NEDD8 and ubiquitin ligation by cullin-RING E3 ligases." Current Opinion in Structural Biology 67 (April 2021): 101–9. http://dx.doi.org/10.1016/j.sbi.2020.10.007.

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Kamada, Shinji. "Inhibitor of apoptosis proteins as E3 ligases for ubiquitin and NEDD8." BioMolecular Concepts 4, no. 2 (2013): 161–71. http://dx.doi.org/10.1515/bmc-2012-0036.

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AbstractThe inhibitors of apoptosis proteins (IAPs) are endogenous inhibitors for apoptosis. Apoptosis is carried out by caspases, which are the family of cystein proteases. IAPs regulate caspases through two conserved regions, the baculovirus IAP repeats (BIRs) and the really interesting new gene (RING) domains. Although the BIRs are responsible for binding to caspases, the RING domain can act as a ubiquitin-E3 ligase, leading to ubiquitylation of IAPs themselves and their pro-apoptotic IAP counterparts such as caspases. Recently, it is reported that another ubiquitin-like protein, neuronal p
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Benjamin, Sigi, and Hermann Steller. "Another Tier for Caspase Regulation: IAPs as NEDD8 E3 Ligases." Developmental Cell 19, no. 6 (2010): 791–92. http://dx.doi.org/10.1016/j.devcel.2010.11.014.

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Keuss, Matthew J., Yann Thomas, Robin Mcarthur, Nicola T. Wood, Axel Knebel, and Thimo Kurz. "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases." Journal of Cell Science 129, no. 7 (2016): 1441–54. http://dx.doi.org/10.1242/jcs.181784.

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Broemer, Meike, Tencho Tenev, Kristoffer T. G. Rigbolt, et al. "Systematic In Vivo RNAi Analysis Identifies IAPs as NEDD8-E3 Ligases." Molecular Cell 40, no. 5 (2010): 810–22. http://dx.doi.org/10.1016/j.molcel.2010.11.011.

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Hjerpe, Roland, Yann Thomas, Jesse Chen, et al. "Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes." Biochemical Journal 441, no. 3 (2012): 927–39. http://dx.doi.org/10.1042/bj20111671.

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Ubiquitin and UBL (ubiquitin-like) modifiers are small proteins that covalently modify other proteins to alter their properties or behaviours. Ubiquitin modification (ubiquitylation) targets many substrates, often leading to their proteasomal degradation. NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8) is the UBL most closely related to ubiquitin, and its best-studied role is the activation of CRLs (cullin-RING ubiquitin ligases) by its conjugation to a conserved C-terminal lysine residue on cullin proteins. The attachment of UBLs requires three UBL-specific enzymes, t
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Zhou, Lihong, and Felicity Z. Watts. "Nep1, a Schizosaccharomyces pombe deneddylating enzyme." Biochemical Journal 389, no. 2 (2005): 307–14. http://dx.doi.org/10.1042/bj20041991.

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Nedd8 is a ubiquitin-like modifier that is attached to the cullin components of E3 ubiquitin ligases. More recently, p53 has also been shown to be Nedd8-modified. Nedd8 attachment occurs in a manner similar to that observed for other ubiquitin-like modifiers. In the present study, we report on the characterization of Nep1, a deneddylating enzyme in fission yeast (Schizosaccharomyces pombe). Unlike loss of ned8, deletion of the nep1 gene is not lethal, although nep1.d cells are heterogeneous in length, suggesting a defect in cell-cycle progression. Viability of nep1.d cells is dependent on a fu
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Adhvaryu, Keyur K., Jordan D. Gessaman, Shinji Honda, Zachary A. Lewis, Paula L. Grisafi, and Eric U. Selker. "The Cullin-4 Complex DCDC Does Not Require E3 Ubiquitin Ligase Elements To Control Heterochromatin in Neurospora crassa." Eukaryotic Cell 14, no. 1 (2014): 25–28. http://dx.doi.org/10.1128/ec.00212-14.

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ABSTRACT The cullin-4 (CUL4) complex DCDC ( D IM-5/-7/-9/ C UL4/ D DB1 c omplex) is essential for DNA methylation and heterochromatin formation in Neurospora crassa . Cullins form the scaffold of cullin-RING E3 ubiquitin ligases (CRLs) and are modified by the covalent attachment of NEDD8, a ubiquitin-like protein that regulates the stability and activity of CRLs. We report that neddylation is not required for CUL4-dependent DNA methylation or heterochromatin formation but is required for the DNA repair functions. Moreover, the RING domain protein RBX1 and a segment of the CUL4 C terminus that
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Onel, Melis, Fidan Sumbul, Jin Liu, Ruth Nussinov, and Turkan Haliloglu. "Cullin neddylation may allosterically tune polyubiquitin chain length and topology." Biochemical Journal 474, no. 5 (2017): 781–95. http://dx.doi.org/10.1042/bcj20160748.

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Conjugation of Nedd8 (neddylation) to Cullins (Cul) in Cul-RING E3 ligases (CRLs) stimulates ubiquitination and polyubiquitination of protein substrates. CRL is made up of two Cul-flanked arms: one consists of the substrate-binding and adaptor proteins and the other consists of E2 and Ring-box protein (Rbx). Polyubiquitin chain length and topology determine the substrate fate. Here, we ask how polyubiquitin chains are accommodated in the limited space available between the two arms and what determines the polyubiquitin linkage topology. We focus on Cul5 and Rbx1 in three states: before Cul5 ne
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Dissertations / Theses on the topic "NEDD8 E3 ligases"

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Meszka, Igor. "Chemical biology approaches within the NEDD8 pathway." Thesis, Université de Montpellier (2022-….), 2022. http://www.theses.fr/2022UMONT015.

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Une famille de petites protéines, appelée famille des molécules d'ubiquitine (Ubls), joue un rôle essentiel dans de nombreux aspects de la réponse au stress. Des défauts dans les composants de la famille de l'ubiquitine sont souvent retrouvés dans les pathologies, notamment dans certain type de cancer et les maladies neurodégénératives.L'une des Ubls qui présente le plus d'identité et de similarité avec l'Ubiquitine est NEDD8. NEDD8 fonctionne de manière similaire à Ub mais utilise un mécanisme de conjugaison distinct. La modification de NEDD8 est essentielle au maintien de l'homéostasie de la
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Drinjakovic, Jovana. "E3 ligase Nedd4 regulates axon branching by downregulating PTEN." Thesis, University of Cambridge, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611503.

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Ruetalo, Buschinger Natalia [Verfasser], and Silke [Akademischer Betreuer] Wiesner. "Mechanisms underlying the regulation of Nedd4-family E3 Ubiquitin ligases / Natalia Ruetalo Buschinger ; Betreuer: Silke Wiesner." Tübingen : Universitätsbibliothek Tübingen, 2020. http://d-nb.info/1202774091/34.

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Escobedo, Pascual Albert. "Structural Insights into Substrate Binding and Regulation of E3 Ubiquitin Ligases in the Nedd4 Family using NMR Spectroscopy." Doctoral thesis, Universitat de Barcelona, 2014. http://hdl.handle.net/10803/284605.

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Nedd4L is a HECT-type E3 ubiquitin ligase (it covalently binds ubiquitin molecules before transferring them to the final substrate). Ubiquitination is a posttranslational modification (PTM) that labels proteins for a variety of fates, the most relevant one being proteasome-mediated degradation. Nedd4L is responsible for the regulation of the turnover of the sodium channel ß-ENaC as well as Smad2/3, mediator proteins of the signalling pathway activated by TGF-ß-like cytokines. It also targets the TGF-ß receptor itself. Defects in its function have been related to hereditary hypertension (Liddle
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Takeda, Michiko [Verfasser], Hiroshi [Akademischer Betreuer] Kawabe, Nils [Akademischer Betreuer] Brose, and Andreas [Akademischer Betreuer] Stumpner. "The Role of the E3 Ubiquitin Ligases Nedd4-1 and Nedd4-2 in Synaptic Transmission and Plasticity / Michiko Takeda. Gutachter: Nils Brose ; Andreas Stumpner. Betreuer: Hiroshi Kawabe." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2013. http://d-nb.info/104430779X/34.

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Visvalingam, Shivanthy Majella. "Regulation of growth, and insulin/TOR signalling by protein shuttling and the E3 ubiquitin protein ligase nedd4 in drosophila." Thesis, University of Oxford, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.510254.

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Fiedorowicz, Katarzyna [Verfasser]. "Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells / Katarzyna Fiedorowicz." Berlin : Freie Universität Berlin, 2013. http://d-nb.info/1032899344/34.

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Altas, Bekir [Verfasser], Nils [Akademischer Betreuer] Brose, Judith [Gutachter] Stegmüller, and Dirk [Gutachter] Goerlich. "Roles of the Nedd4 Family E3 Ligases in Glial Function and Nerve Cell Development / Bekir Altas ; Gutachter: Judith Stegmüller, Dirk Goerlich ; Betreuer: Nils Brose." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2017. http://d-nb.info/1131875710/34.

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Hsia, Hung-En [Verfasser], Hiroshi [Akademischer Betreuer] Kawabe, Nils [Akademischer Betreuer] Brose, Judith [Akademischer Betreuer] Stegmüller, and Andreas [Akademischer Betreuer] Wodarz. "Roles of the HECT-Type Ubiquitin E3 Ligases of the Nedd4 and WWP Subfamilies in Neuronal Development / Hung-En Hsia. Gutachter: Nils Brose ; Judith Stegmüller ; Andreas Wodarz. Betreuer: Hiroshi Kawabe." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2015. http://d-nb.info/1071713493/34.

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Spiegelberg, Larissa [Verfasser], and Friedemann [Akademischer Betreuer] Weber. "Das Ubiquitin-Proteasom-System und die Ubiquitin-E3-Ligase Nedd4 sind involviert in den Abbau der RNA-Polymerase II durch den Virulenzfaktor NSs des La Crosse-Virus / Larissa Spiegelberg. Betreuer: Friedemann Weber." Marburg : Philipps-Universität Marburg, 2016. http://d-nb.info/1082347027/34.

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Book chapters on the topic "NEDD8 E3 ligases"

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Butt, Ghazala, Ilhan Yaylim, Rukset Attar, et al. "NEDD4 Family of E3 Ubiquitin Ligases in Breast Cancer: Spotlight on SMURFs, WWPs and NEDD4." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-20301-6_19.

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Fu, Xiaoli, Jie Chu, Yuyin Li, et al. "Design, Synthesis, and Biological Evaluation of Nedd4 E3 Ubiquitin Ligase Small Molecule Inhibitors." In Proceedings of the 2012 International Conference on Applied Biotechnology (ICAB 2012). Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-37925-3_195.

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Jing, Lei, Xin Huo, Yufeng Li, Yuyin Li, and Aipo Diao. "Identification of the Binding Domains of Nedd4 E3 Ubiquitin Ligase with Its Substrate Protein TMEPAI." In Lecture Notes in Electrical Engineering. Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-45657-6_6.

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I. Kane, Emma, and Donald E. Spratt. "New Discoveries on the Roles of “Other” HECT E3 Ubiquitin Ligases in Disease Development." In Ubiquitin - Proteasome Pathway. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.91770.

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HECT E3 ubiquitin ligases selectively recognize, bind, and ubiquitylate their substrate proteins to target them for 26S proteasomal degradation. There is increasing evidence that HECT E3 ubiquitin ligase dysfunction due to misfolding and/or the gene encoding the protein being mutated is responsible for the development of different diseases. Apart from the more prominent and well-characterized E6AP and members of the NEDD4 family, new studies have begun to reveal how other members of the HECT E3 ubiquitin ligase family function as well as their links to disease and developmental disorders. This chapter provides a comprehensive discussion on the more mysterious members of the HECT E3 ubiquitin ligase family and how they control intracellular processes. Specifically, AREL1, HACE1, HECTD1, HECTD4, G2E3, and TRIP12 will be examined as these enzymes have recently been identified as contributors to disease development.
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Tanaka, Tomoaki, and Tatsuya Nakatani. "Anticancer Target Molecules Against the SCF Ubiquitin E3 Ligase in RCC: Potential Approaches to the NEDD8 Pathway." In Emerging Research and Treatments in Renal Cell Carcinoma. InTech, 2012. http://dx.doi.org/10.5772/26409.

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Conference papers on the topic "NEDD8 E3 ligases"

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Song, Fei, Chuandong Fan, Xiaojing Zhang, Xinjiang Wang, and David W. Goodrich. "Abstract LB-280: RNP biogenesis factor Thoc1 is targeted for ubiquitination by NEDD4-1 E3 ligase." 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-lb-280.

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Knudsen, LM, A. Sveen, CH Bergsland, et al. "PO-127 Role of the NEDD4 family of E3 ubiquitin ligases in colorectal cancer pathogenesis and their potential as biomarkers." 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-eacr25.168.

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Knudsen, Lars M., Anita Sveen, Christer A. Andreassen, et al. "Abstract 1433: Role of the E3 ubiquitin ligase NEDD4 in the regulation of PTEN and MDM2 in colorectal cancer." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-1433.

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Li, Hua, Albert Dobi, and Shiv Srivastava. "Abstract 3914: Androgen receptor (AR) degradation is controlled by the co-operation of PMEPA1 and the E3 ubiquitin ligase NEDD4-1." 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.am2012-3914.

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Li, Hua, Elizabeth Umeda, Yingjie Song, et al. "Abstract 4679: Silencing of PMEPA1, a NEDD4 E3 ubiquitin ligase binding protein, stabilizes androgen receptor and confers resistance to AR inhibitors." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4679.

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