Log in

Relevant bibliographies by topics / SCF E3 ubiquitin ligase

Contents

Journal articles
Dissertations / Theses
Books
Book chapters
Conference papers
Reports

Academic literature on the topic 'SCF E3 ubiquitin ligase'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'SCF E3 ubiquitin ligase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "SCF E3 ubiquitin ligase"

1

Horn-Ghetko, Daniel, David T. Krist, J. Rajan Prabu, Kheewoong Baek, Monique P. C. Mulder, Maren Klügel, Daniel C. Scott, Huib Ovaa, Gary Kleiger, and Brenda A. Schulman. "Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly." Nature 590, no. 7847 (February 3, 2021): 671–76. http://dx.doi.org/10.1038/s41586-021-03197-9.

Full text

Abstract:

AbstractE3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates1,2. However, rather than functioning individually, many neddylated cullin–RING E3 ligases (CRLs) and RBR-type E3 ligases in the ARIH family—which together account for nearly half of all ubiquitin ligases in humans—form E3–E3 super-assemblies3–7. Here, by studying CRLs in the SKP1–CUL1–F-box (SCF) family, we show how neddylated SCF ligases and ARIH1 (an RBR-type E3 ligase) co-evolved to ubiquitylate diverse substrates presented on various F-box proteins. We developed activity-based chemical probes that enabled cryo-electron microscopy visualization of steps in E3–E3 ubiquitylation, initiating with ubiquitin linked to the E2 enzyme UBE2L3, then transferred to the catalytic cysteine of ARIH1, and culminating in ubiquitin linkage to a substrate bound to the SCF E3 ligase. The E3–E3 mechanism places the ubiquitin-linked active site of ARIH1 adjacent to substrates bound to F-box proteins (for example, substrates with folded structures or limited length) that are incompatible with previously described conventional RING E3-only mechanisms. The versatile E3–E3 super-assembly may therefore underlie widespread ubiquitylation.

APA, Harvard, Vancouver, ISO, and other styles

2

Kawakami, T. "NEDD8 recruits E2-ubiquitin to SCF E3 ligase." EMBO Journal 20, no. 15 (August 1, 2001): 4003–12. http://dx.doi.org/10.1093/emboj/20.15.4003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Gorelik, Maryna, Stephen Orlicky, Maria A. Sartori, Xiaojing Tang, Edyta Marcon, Igor Kurinov, Jack F. Greenblatt, et al. "Inhibition of SCF ubiquitin ligases by engineered ubiquitin variants that target the Cul1 binding site on the Skp1–F-box interface." Proceedings of the National Academy of Sciences 113, no. 13 (March 14, 2016): 3527–32. http://dx.doi.org/10.1073/pnas.1519389113.

Full text

Abstract:

Skp1–Cul1–F-box (SCF) E3 ligases play key roles in multiple cellular processes through ubiquitination and subsequent degradation of substrate proteins. Although Skp1 and Cul1 are invariant components of all SCF complexes, the 69 different human F-box proteins are variable substrate binding modules that determine specificity. SCF E3 ligases are activated in many cancers and inhibitors could have therapeutic potential. Here, we used phage display to develop specific ubiquitin-based inhibitors against two F-box proteins, Fbw7 and Fbw11. Unexpectedly, the ubiquitin variants bind at the interface of Skp1 and F-box proteins and inhibit ligase activity by preventing Cul1 binding to the same surface. Using structure-based design and phage display, we modified the initial inhibitors to generate broad-spectrum inhibitors that targeted many SCF ligases, or conversely, a highly specific inhibitor that discriminated between even the close homologs Fbw11 and Fbw1. We propose that most F-box proteins can be targeted by this approach for basic research and for potential cancer therapies.

APA, Harvard, Vancouver, ISO, and other styles

4

Sun, Yi. "Sag/Rbx2 E3 Ubiquitin Ligase: From Target Validation to Drug Discovery." Proceedings 22, no. 1 (November 14, 2019): 102. http://dx.doi.org/10.3390/proceedings2019022102.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Risseeuw, Eddy P., Timothy E. Daskalchuk, Travis W. Banks, Enwu Liu, Julian Cotelesage, Hanjo Hellmann, Mark Estelle, David E. Somers, and William L. Crosby. "Protein interaction analysis of SCF ubiquitin E3 ligase subunits fromArabidopsis." Plant Journal 34, no. 6 (June 2003): 753–67. http://dx.doi.org/10.1046/j.1365-313x.2003.01768.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Chang, Shu-Chun, Chin-Sheng Hung, Bo-Xiang Zhang, Tsung-Han Hsieh, Wayne Hsu, and Jeak Ling Ding. "A Novel Signature of CCNF-Associated E3 Ligases Collaborate and Counter Each Other in Breast Cancer." Cancers 13, no. 12 (June 8, 2021): 2873. http://dx.doi.org/10.3390/cancers13122873.

Full text

Abstract:

Breast cancer (BRCA) malignancy causes major fatalities amongst women worldwide. SCF (Skp1-cullin-F-box proteins) E3 ubiquitin ligases are the most well-known members of the ubiquitination–proteasome system (UPS), which promotes cancer initiation and progression. Recently, we demonstrated that FBXL8, a novel F-box protein (SCFF-boxes) of SCF E3 ligase, accelerates BRCA advancement and metastasis. Since SCFF-boxes is a key component of E3 ligases, we hypothesized that other SCFF-boxes besides FBXL8 probably collaborate in regulating breast carcinogenesis. In this study, we retrospectively profiled the transcriptome of BRCA tissues and found a notable upregulation of four SCFF-box E3 ligases (FBXL8, FBXO43, FBXO15, and CCNF) in the carcinoma tissues. Similar to FBXL8, the knockdown of FBXO43 reduced cancer cell viability and proliferation, suggesting its pro-tumorigenic role. The overexpression of CCNF inhibited cancer cell progression, indicating its anti-tumorigenic role. Unexpectedly, CCNF protein was markedly downregulated in BRCA tissues, although its mRNA level was high. We showed that both E3 ligases, FBXL8 and FZR1, pulled down CCNF. Double knockdown of FBXL8 and FZR1 caused CCNF accumulation. On the other hand, CCNF itself pulled down a tumorigenic factor, RRM2, and CCNF overexpression reduced RRM2. Altogether, we propose a signature network of E3 ligases that collaboratively modulates CCNF anti-cancer activity. There is potential to target BRCA through modulation of the partnership axes of (i) CCNF-FBXL8, (ii) CCNF-FZR1, and (iii) CCNF-RRM2, particularly, via CCNF overexpression and activation and FBXL8/FZR1 suppression.

APA, Harvard, Vancouver, ISO, and other styles

7

Willems, A. R., T. Goh, L. Taylor, I. Chernushevich, A. Shevchenko, and M. Tyers. "SCF ubiquitin protein ligases and phosphorylation–dependent proteolysis." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 354, no. 1389 (September 29, 1999): 1533–50. http://dx.doi.org/10.1098/rstb.1999.0497.

Full text

Abstract:

Many key activators and inhibitors of cell division are targeted for degradation by a recently described family of E3 ubiquitin protein ligases termed Skp1–Cdc53–F–box protein (SCF) complexes. SCF complexes physically link substrate proteins to the E2 ubiquitin–conjugating enzyme Cdc34, which catalyses substrate ubiquitination, leading to subsequent degradation by the 26S proteasome. SCF complexes contain a variable subunit called an F–box protein that confers substrate specificity on an invariant core complex composed of the subunits Cdc34, Skp1 and Cdc53. Here, we review the substrates and pathways regulated by the yeast F–box proteins Cdc4, Grr1 and Met30. The concepts of SCF ubiquitin ligase function are illustrated by analysis of the degradation pathway for the G1 cyclin Cln2. Through mass spectrometric analysis of Cdc53 associated proteins, we have identified three novel F–box proteins that appear to participate in SCF–like complexes. As many F–box proteins can be found in sequence databases, it appears that a host of cellular pathways will be regulated by SCF–dependent proteolysis.

APA, Harvard, Vancouver, ISO, and other styles

8

Chen, Wei-Yi, Jui-Hsia Weng, Chen-Che Huang, and Bon-chu Chung. "Histone Deacetylase Inhibitors Reduce Steroidogenesis through SCF-Mediated Ubiquitination and Degradation of Steroidogenic Factor 1 (NR5A1)." Molecular and Cellular Biology 27, no. 20 (August 20, 2007): 7284–90. http://dx.doi.org/10.1128/mcb.00476-07.

Full text

Abstract:

ABSTRACT Histone deacetylase (HDAC) inhibitors such as trichostatin A and valproic acid modulate transcription of many genes by inhibiting the activities of HDACs, resulting in the remodeling of chromatin. Yet this effect is not universal for all genes. Here we show that HDAC inhibitors suppressed the expression of steroidogenic gene CYP11A1 and decreased steroid secretion by increasing the ubiquitination and degradation of SF-1, a factor important for the transcription of all steroidogenic genes. This was accompanied by increased expression of Ube2D1 and SKP1A, an E2 ubiquitin conjugase and a subunit of the E3 ubiquitin ligase in the Skp1/Cul1/F-box protein (SCF) family, respectively. Reducing SKP1A expression with small interfering RNA resulted in recovery of SF-1 levels, demonstrating that the activity of SCF E3 ubiquitin ligase is required for the SF-1 degradation induced by HDAC inhibitors. Overexpression of exogenous SF-1 restored steroidogenic activities even in the presence of HDAC inhibitors. Thus, increased SF-1 degradation is the cause of the reduction in steroidogenesis caused by HDAC inhibitors. The increased SKP1A expression and SCF-mediated protein degradation could be the mechanism underlying the mode of action of HDAC inhibitors.

APA, Harvard, Vancouver, ISO, and other styles

9

Rogers, Gregory C., Nasser M. Rusan, David M. Roberts, Mark Peifer, and Stephen L. Rogers. "The SCFSlimb ubiquitin ligase regulates Plk4/Sak levels to block centriole reduplication." Journal of Cell Biology 184, no. 2 (January 26, 2009): 225–39. http://dx.doi.org/10.1083/jcb.200808049.

Full text

Abstract:

Restricting centriole duplication to once per cell cycle is critical for chromosome segregation and genomic stability, but the mechanisms underlying this block to reduplication are unclear. Genetic analyses have suggested an involvement for Skp/Cullin/F box (SCF)-class ubiquitin ligases in this process. In this study, we describe a mechanism to prevent centriole reduplication in Drosophila melanogaster whereby the SCF E3 ubiquitin ligase in complex with the F-box protein Slimb mediates proteolytic degradation of the centrosomal regulatory kinase Plk4. We identified SCFSlimb as a regulator of centriole duplication via an RNA interference (RNAi) screen of Cullin-based ubiquitin ligases. We found that Plk4 binds to Slimb and is an SCFSlimb target. Both Slimb and Plk4 localize to centrioles, with Plk4 levels highest at mitosis and absent during S phase. Using a Plk4 Slimb-binding mutant and Slimb RNAi, we show that Slimb regulates Plk4 localization to centrioles during interphase, thus regulating centriole number and ensuring the block to centriole reduplication.

APA, Harvard, Vancouver, ISO, and other styles

10

Jia, L., and Y. Sun. "SCF E3 Ubiquitin Ligases as Anticancer Targets." Current Cancer Drug Targets 11, no. 3 (March 1, 2011): 347–56. http://dx.doi.org/10.2174/156800911794519734.

Full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

Dissertations / Theses on the topic "SCF E3 ubiquitin ligase"

1

Moon, Jennifer Kathryn. "Characterization of CUL1 and CUL2: Subunits of SCF E3 ubiquitin ligases in Arabidopsis thaliana." [Bloomington, Ind.] : Indiana University, 2004. http://wwwlib.umi.com/dissertations/fullcit/3162252.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Loos, Trina Jane. "Determining the Function of Nuclear Bmp4." BYU ScholarsArchive, 2010. https://scholarsarchive.byu.edu/etd/2586.

Full text

Abstract:

Bone morphogenetic protein 4 (Bmp4) is a well known growth factor that regulates gene expression through the SMAD signaling pathway. Bmp4 is involved in many developmental processes and has been identified as an important factor in several cancers, including melanoma, ovarian cancer, and colon cancer. Madoz-Gurpide et al. recently observed Bmp4 in the nuclei of a minor percentage of cells in colon cancer tissues. In addition, our lab has recently discovered a nuclear variant of Bmp2 (nBmp2), the TGF-β family member most closely related to Bmp4. These observations led us to hypothesize that a nuclear variant of Bmp4 (nBmp4) also exists. The results of chapter one report the existence of a nuclear variant of Bmp4. nBmp4 is translated from an alternative start codon downstream of the signal peptide sequence which allows a bipartite nuclear localization signal to direct translocation of nBmp4 to the nucleus. Chapter 2 and 3 further report that nBmp4 interacts with several subunits in the SCF E3 ubiquitin ligase, namely two Regulator of Cullins (ROC) proteins, five Cullin proteins, and two F-box proteins. Due to the known role of the SCF E3 ubiquitin ligase in regulating the cell cycle, the effect of nBmp4 on cell cycle progression was analyzed and the results show that nBmp4 affects the cell cycle by causing cells to accumulate in G0/G1. The association of nBmp4 and the SCF E3 ubiquitin ligase components and the affect that nBmp4 has on the cell cycle suggest that nBmp4 functions in the nucleus by inhibiting the SCF E3 ubiquitin ligase from ubiquitinating target proteins that are involved in regulating cell cycle progression. Finally, the initial stages in the generation of an nBmp4 over-expression mouse are described. The results of this research clearly change the traditional paradigm that Bmp4 performs all of its functions via extracellular signaling and introduce the existence of a nuclear variant that is involved in cell cycle regulation.

APA, Harvard, Vancouver, ISO, and other styles

3

Vadhvani, Mayur [Verfasser], Judith [Akademischer Betreuer] Stegmüller, Klaus-Armin [Akademischer Betreuer] Nave, and Till [Akademischer Betreuer] Marquardt. "The role of E3 ubiquitin ligase FBXO31-SCF in neuronal morphogenesis / Mayur Vadhvani. Gutachter: Judith Stegmüller ; Klaus-Armin Nave ; Till Marquardt. Betreuer: Judith Stegmüller." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2013. http://d-nb.info/1044047453/34.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Brockelt, David [Verfasser], Judith [Akademischer Betreuer] [Gutachter] Stegmüller, and Tiago Fleming [Gutachter] Outeiro. "The role of the E3 ubiquitin ligase FBXO7-SCF in early-onset Parkinson's disease / David Brockelt. Betreuer: Judith Stegmüller. Gutachter: Judith Stegmüller ; Tiago Fleming Outeiro." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2016. http://d-nb.info/1112736522/34.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

El, Beji Imen. "Caractérisation biochimique et moléculaire du complexe SCF (SKP1-CULLIN-FBOX) chez le blé tendre." Phd thesis, Université Blaise Pascal - Clermont-Ferrand II, 2011. http://tel.archives-ouvertes.fr/tel-00999477.

Full text

Abstract:

Les modifications post-traductionnelles des protéines constituent un niveau crucial de régulation de l'expression des gènes. Parmi elles, la conjugaison peptidique impliquant l'ubiquitine intervient entre autre dans la régulation de la stabilité protéique. La fixation de ce peptide de 76 acides aminés, extrêmement conservé, sous forme de chaîne de polyubiquitine, nécessite l'intervention de trois enzymes (E1, E2 et E3) et constitue un signal de dégradation de la protéine ainsi modifiée. Cette voie de régulation intervient dans de très nombreux processus biologiques. Les complexes SCF sont impliqués dans la voie de protéolyse ciblée. Ils représentent l' une des classes les plus fréquentes d'ubiquitine ligase E3 et ils sont composés de quatre sous-unités (Rbx, Cullin, SKP1, et F-box). La structure et la fonction des complexes SCF, ont été étudiées chez la levure, l'Homme et la plante modèle A. thaliana. Cependant, peu de travaux ont été réalisés chez des plantes cultivées, en particulier les céréales, telles que le blé. Cinq gènes codant pour la sous-unité Skp1 (TSK1, TSK3, TSK6, TSK11 et TSK16), cinq gènes codant pour la sous-unité F-box (ZTL, ATFBL5, EBF, TIR1 et ABA-T), un gène codant pour la sous-unité Cullin1 et un gène codant pour la protéine RBX du complexe SCF du blé, ont été isolés et clonés. Les différents tests d'interaction entre les quatre sous-unités du complexe SCF ont été réalisés par la méthode du double-hybride dans la levure en utilisant la technologie Gateway. Ces études ont montré que les deux protéines, TSK1 et TSK3, fixent spécifiquement différentes sous-unités F-box. Parallèlement, nous avons montré que la protéine TSK11 représente une structure particulière. Des études d'insertion/délétion sur la protéine TSK11 ont permis d'identifier un nouveau domaine indispensable à l'interaction. Les analyses par PCR semi-quantitative des différents gènes codant pour la sous-unité Skp1, dans trois tissus différents (feuille tige et racine), ont mis en évidence une expression constitutive des gènes TSK3, TSK6 et TSK11. Tandis que les gènes TSK1 et TSK16 sont exprimés préférentiellement dans les racines. Les analyses par PCR semi-quantitative sur des plantules de blé à différents stades de développement, ont mis en évidence une surexpression du gène TSK11 au moment de la floraison. Ce qui suggère que TSK11 est probablement un équivalent fonctionnel d'ASK1 chez Arabidopsis thaliana.

APA, Harvard, Vancouver, ISO, and other styles

6

Shang, Jinsai. "STRUCTURAL AND FUNCTIONAL STUDIES OF F-BOX-ONLY PROTEIN FBXO7 AND ITS INTERACTIONS WITH PROTEASOME INHIBITOR PI31." OpenSIUC, 2015. https://opensiuc.lib.siu.edu/dissertations/1053.

Full text

Abstract:

F-box only protein 7 (Fbxo7), a member of the F-box-only subfamily of FBPs, is a biologically and pathophysiologically important human protein that assumes many critical functions. The different functions of Fbxo7 depend on the formation of various multi-protein complexes. Possible interplay between different Fbxo7 functions further complicate the protein-protein interaction networks involved in Fbxo7 biology. Although significant progresses have been made to understand the functions, regulation, specificity, and protein interaction network of Fbxo7, a myriad of questions remain to be answered. The objectives of the work presented in this dissertation are to elucidate the molecular structures underlying the functions of Fbxo7 and the interaction with its protein partners, such as proteasome inhibitor PI31. The best known biological function of Fbxo7 is its role as the substrate-recognition subunit of the SCFFbxo7 (Skp1-Cul1-F-box protein) E3 ubiquitin ligase that catalyzes the ubiquitination of hepatoma up-regulated protein (HURP) and inhibitor of apoptosis protein (IAP). Fbxo7 also assumes various SCF-independent functions through interact with its protein partners that are not the substrates of the ubiquitin proteasome system, such as PI31, Cdk6, p27, PINK1 (PTEN-induced kinase 1), and Parkin. PI31 is a known proteasome regulator which was initially characterized as a proteasome inhibitor in vitro. The binding affinity between Fbxo7 and PI31 is very strong, and The Fbxo7-PI31 interaction is mediated by heterodimerization of the FP domains of the two proteins. This work is focus on study the protein structure of the two FP domains in Fbxo7 and PI3. Chapter 1 reviewed the F-box-only protein Fbxo7 biology including the function of Fbxo7 protein in ubiquitination proteasome pathway and some SCF-independent functions which are relate to human disease. Chapter 2 discussed the function of proteasome inhibitor PI31. With the many important biological functions, Fbxo7 is clearly an extraordinary important protein, but the lack of structural knowledge has hampered efforts to achieve a better understanding of Fbxo7 biology. In this work, we have determined the crystal structure of Fbxo7 FP domain (residues 181-335) and the crystal structure of the PI31 FP domain (residues 1-161) using a longer protein construct both at 2.0Å resolution. The Fbxo7 FP domain adopts an α/β-fold similar to that of the PI31 FP domain and the secondary structure elements of the two FP domains are comparable including the C-terminal helix, indicating that the two FP domains share the same overall global fold. However, an α helix and three β strands in the Fbxo7 are longer than their counterparts in the PI31 FP domain. The two FP domains also differ substantially in the length and conformation of the longest connecting loop. More importantly, structural differences between the two FP domains lead to drastically different modes of inter-domain protein–protein interaction: the PI31 FP domain utilizes either an α interface or β interface for homodimeric interaction, whereas the Fbxo7 FP domain utilizes an αβ interface. We have note that the inter-domain interaction of the Fbxo7 FP domain is much more extensive, featuring a larger contact surface area, better shape complementarity and more hydrophobic and hydrogen-bonding interactions. The results of this structural study provide critical insights into how Fbxo7 may dimerize (or multimerize) and interact with PI31 via the FP domain. Chapter 4 and Chapter 5 discussed the structure determinations, structure features and detail of protein-protein interactions of Fbxo7 and PI31 FP domains. Chapter 2 reviewed the corresponding fundamental biochemical techniques that been used in this study. Chapter 3 discussed protein structure determination by X-ray crystallography in structural biology studies. It was believed that the FP domains of Fbxo7 and PI31 mediate homodimerization and heterodimerization of the proteins and the FP domain is not present in other human proteins. In order to study the Fbxo7-PI31 heterodimerization protein-protein interactions, we performed modeling studies. Chapter 6 discussed the model building and binding studies. Based on the result of model building studies, we propose that an interaction between the two FP domains of Fbxo7 and PI31 should be mediated by a αβ interface using the α-helical surface of the Fbxo7 FP domain and the β-sheet surface of the PI31 FP domain. According to the result of pull down assay, the PI31 FP domain may complete with Skp1 for the binding with Fbxo7. It is possible that the formation of heterodimer between the Fbxo7 and PI31 mediate by FP domains may lead to the Fbxo7 dissociation from SCFFbxo7 complex which might reveal a new regulation mechanism.

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

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/.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

More sources

Books on the topic "SCF E3 ubiquitin ligase"

1

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

Find full text

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

4

Patton, E. Elizabeth. E3 ubiquitin protein ligase complexes that regulate G1-phase in budding yeast. 2001.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

5

Atfield, Alexandre David. The E3 ubiquitin ligase Cbl-b is essential for the induction of in vivo T-cell anergy. 2005.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

6

Atfield, Alexandre David. The E3 ubiquitin ligase Cbl-b is essential for the induction of in vivo T-cell anergy. 2005.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

7

Barañano, Kristin W. Angelman Syndrome. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0055.

Full text

Abstract:

Angelman syndrome (AS) is a severe neurodevelopmental disorder caused by maternal deficiency of the epigenetically imprinted gene UBE3A. It is characterized by severe developmental delay, an ataxic gait disorder, an apparent happy demeanor with frequent smiling or laughing, and severe expressive language impairments. Understanding the neurobiology of AS has focused on understanding how UBE3A is regulated by neuronal activity, as well as the targets of its ubiquitin E3 ligase activity. This has led to a model of the role of UBE3A in the regulation of experience-dependent sculpting of synaptic circuits. At this time, treatment is largely supportive, but efforts directed toward reversing the epigenetic silencing machinery may lead to improved synaptic function in AS patients.

APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "SCF E3 ubiquitin ligase"

1

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Zhang, Jinfang, Lixin Wan, Brian J. North, Hiroyuki Inuzuka, and Wenyi Wei. "The Role of APC E3 Ubiquitin Ligase Complex in Tumorigenesis." In SCF and APC E3 Ubiquitin Ligases in Tumorigenesis, 89–111. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05026-3_5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Liu, Pengda, Hiroyuki Inuzuka, and Wenyi Wei. "Introduction." In SCF and APC E3 Ubiquitin Ligases in Tumorigenesis, 1–13. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05026-3_1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Lau, Alan W., Yueyong Liu, Adriana E. Tron, Hiroyuki Inuzuka, and Wenyi Wei. "The Role of FBXW Subfamily of F-box Proteins in Tumorigenesis." In SCF and APC E3 Ubiquitin Ligases in Tumorigenesis, 15–45. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05026-3_2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

North, Brian J., Yueyong Liu, Hiroyuki Inuzuka, and Wenyi Wei. "The Role of FBXL Subfamily of F-box Proteins in Tumorigenesis." In SCF and APC E3 Ubiquitin Ligases in Tumorigenesis, 47–71. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05026-3_3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Guo, Jianping, Brian J. North, Adriana E. Tron, Hiroyuki Inuzuka, and Wenyi Wei. "The Role of FBXO Subfamily of F-box Proteins in Tumorigenesis." In SCF and APC E3 Ubiquitin Ligases in Tumorigenesis, 73–87. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05026-3_4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Liu, Pengda, Brian J. North, Hiroyuki Inuzuka, and Wenyi Wei. "Conclusions and Research Perspectives." In SCF and APC E3 Ubiquitin Ligases in Tumorigenesis, 113–16. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05026-3_6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Nguyen, Khai M., and Luca Busino. "The Biology of F-box Proteins: The SCF Family of E3 Ubiquitin Ligases." In Advances in Experimental Medicine and Biology, 111–22. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-1025-0_8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "SCF E3 ubiquitin ligase"

1

Egbuta, Chinaza, Julien Dubrulle, Ana Tellechea, Miguel A. Manzanares, Yunfeng Li, Shanshan Duan, John K. Dickson, et al. "Abstract 5231: Small-molecule inhibitors of SCF-Skp2-Cks1 ubiquitin E3 ligase stabilize nuclear p27kip1as a novel therapeutic approach to endometrial 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.am2018-5231.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

"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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "SCF E3 ubiquitin ligase"

1

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

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 2001. http://dx.doi.org/10.21236/ada396779.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

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 2002. http://dx.doi.org/10.21236/ada407554.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Godwin, Andrew K. BRCC36, A Novel Subunit of a BRCA1/2 E3 Ubiquitin Ligase Complex: Candidate Breast Cancer Susceptibility Gene. Fort Belvoir, VA: Defense Technical Information Center, September 2005. http://dx.doi.org/10.21236/ada446684.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!