Relevant bibliographies by topics / RBBP4

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers
  5. Reports

Academic literature on the topic 'RBBP4'

Author: Grafiati
Published: 3 July 2021
Last updated: 21 February 2023

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Journal articles on the topic "RBBP4"

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Nabeel-Shah, Syed, Jyoti Garg, Alejandro Saettone, et al. "Functional characterization of RebL1 highlights the evolutionary conservation of oncogenic activities of the RBBP4/7 orthologue in Tetrahymena thermophila." Nucleic Acids Research 49, no. 11 (2021): 6196–212. http://dx.doi.org/10.1093/nar/gkab413.

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Abstract Retinoblastoma-binding proteins 4 and 7 (RBBP4 and RBBP7) are two highly homologous human histone chaperones. They function in epigenetic regulation as subunits of multiple chromatin-related complexes and have been implicated in numerous cancers. Due to their overlapping functions, our understanding of RBBP4 and 7, particularly outside of Opisthokonts, has remained limited. Here, we report that in the ciliate protozoan Tetrahymena thermophila a single orthologue of human RBBP4 and 7 proteins, RebL1, physically interacts with histone H4 and functions in multiple epigenetic regulatory p
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Wang, Juan, Zongxing Yang, Linfang Cheng, et al. "Retinoblastoma binding protein 4 represses HIV-1 long terminal repeat–mediated transcription by recruiting NR2F1 and histone deacetylase." Acta Biochimica et Biophysica Sinica 51, no. 9 (2019): 934–44. http://dx.doi.org/10.1093/abbs/gmz082.

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Abstract Human immunodeficiency virus (HIV) transcription is closely associated with chromatin remodeling. Retinoblastoma binding protein 4 (RBBP4) is a histone chaperone implicated in chromatin remodeling. However, the role of RBBP4 in HIV-1 infection and the underlying mechanism remain elusive. In the present study, we showed that RBBP4 plays a negative regulatory role during HIV-1 infection. RBBP4 expression was significantly increased in HIV-1–infected T cells. RBBP4 binds to the HIV-1 long terminal repeat (LTR)， represses HIV-1 LTR-mediated transcription through recruiting nuclear recepto
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Miao, Xiaosu, Tieqi Sun, Holly Barletta, Jesse Mager, and Wei Cui. "Loss of RBBP4 results in defective inner cell mass, severe apoptosis, hyperacetylated histones and preimplantation lethality in mice†." Biology of Reproduction 103, no. 1 (2020): 13–23. http://dx.doi.org/10.1093/biolre/ioaa046.

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Abstract Retinoblastoma-binding protein 4 (RBBP4) (also known as chromatin-remodeling factor RBAP48) is an evolutionarily conserved protein that has been involved in various biological processes. Although a variety of functions have been attributed to RBBP4 in vitro, mammalian RBBP4 has not been studied in vivo. Here we report that RBBP4 is essential during early mouse embryo development. Although Rbbp4 mutant embryos exhibit normal morphology at E3.5 blastocyst stage, they cannot be recovered at E7.5 early post-gastrulation stage, suggesting an implantation failure. Outgrowth (OG) assays reve
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Goos, Jacqueline A. C., Walter K. Vogel, Hana Mlcochova, et al. "A de novo substitution in BCL11B leads to loss of interaction with transcriptional complexes and craniosynostosis." Human Molecular Genetics 28, no. 15 (2019): 2501–13. http://dx.doi.org/10.1093/hmg/ddz072.

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Abstract Craniosynostosis, the premature ossification of cranial sutures, is a developmental disorder of the skull vault, occurring in approximately 1 in 2250 births. The causes are heterogeneous, with a monogenic basis identified in ~25% of patients. Using whole-genome sequencing, we identified a novel, de novo variant in BCL11B, c.7C>A, encoding an R3S substitution (p.R3S), in a male patient with coronal suture synostosis. BCL11B is a transcription factor that interacts directly with the nucleosome remodelling and deacetylation complex (NuRD) and polycomb-related complex 2 (PRC2) through
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Balboula, Ahmed Z., and Richard M. Schultz. "RBBP4 and RBBP7 Regulate Histone Deacetylation During Oocyte Maturation in Mouse." Biology of Reproduction 87, Suppl_1 (2012): 306. http://dx.doi.org/10.1093/biolreprod/87.s1.306.

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Vavougios, Georgios D., Evgeniy I. Solenov, Chrissi Hatzoglou, et al. "Computational genomic analysis of PARK7 interactome reveals high BBS1 gene expression as a prognostic factor favoring survival in malignant pleural mesothelioma." American Journal of Physiology-Lung Cellular and Molecular Physiology 309, no. 7 (2015): L677—L686. http://dx.doi.org/10.1152/ajplung.00051.2015.

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The aim of our study was to assess the differential gene expression of Parkinson protein 7 (PARK7) interactome in malignant pleural mesothelioma (MPM) using data mining techniques to identify novel candidate genes that may play a role in the pathogenicity of MPM. We constructed the PARK7 interactome using the ConsensusPathDB database. We then interrogated the Oncomine Cancer Microarray database using the Gordon Mesothelioma Study, for differential gene expression of the PARK7 interactome. In ConsensusPathDB, 38 protein interactors of PARK7 were identified. In the Gordon Mesothelioma Study, 34
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Yang, Sile F., Ai-ai Sun, Yunyu Shi, Fudong Li, and Hilda A. Pickett. "Structural and functional characterization of the RBBP4–ZNF827 interaction and its role in NuRD recruitment to telomeres." Biochemical Journal 475, no. 16 (2018): 2667–79. http://dx.doi.org/10.1042/bcj20180310.

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The nucleosome remodeling and histone deacetylase (NuRD) complex is an essential multi-subunit protein complex that regulates higher-order chromatin structure. Cancers that use the alternative lengthening of telomere (ALT) pathway of telomere maintenance recruit NuRD to their telomeres. This interaction is mediated by the N-terminal domain of the zinc-finger protein ZNF827. NuRD–ZNF827 plays a vital role in the ALT pathway by creating a molecular platform for recombination-mediated repair. Disruption of NuRD binding results in loss of ALT cell viability. Here, we present the crystal structure
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Kitange, Gaspar J., Danielle M. Burgenske, Katrina K. Bakken, et al. "EXTH-12. INHIBITION OF CBP/p300 HISTONE ACETYLATION ACTIVITY ENHANCES TEMOZOLOMIDE ACTIVITY IN GLIOBLASTOMA PATIENT DERIVED XENOGRAFTS." Neuro-Oncology 22, Supplement_2 (2020): ii89. http://dx.doi.org/10.1093/neuonc/noaa215.366.

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Abstract There is an unmet need to identify novel targets that can sensitize temozolomide (TMZ) or prevent resistance in GBM. We have demonstrated that retinoblastoma binding protein 4 (RBBP4) interacts with p300 to modulate expression of genes involved in homologous recombination (HR), including RAD51. In vitro, RBBP4- or p300-shRNA significantly sensitized TMZ in patient derived xenograft (PDX) GBM43 cells (relative fluorescence for 100µM TMZ treated control shNT cells was 0.89 ± 0.1 vs 0.47± 0.09 and 0.39 ± 0.01 for shRBBP4 and shp300, respectively (p< 0.01)). TMZ sensitization incre
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Soontornniyomkij, Virawudh, Rachel C. Chang, Benchawanna Soontornniyomkij, Jan M. Schilling, Hemal H. Patel, and Dilip V. Jeste. "Loss of Immunohistochemical Reactivity in Association With Handling-Induced Dark Neurons in Mouse Brains." Toxicologic Pathology 48, no. 3 (2020): 437–45. http://dx.doi.org/10.1177/0192623319896263.

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The handling-induced dark neuron is a histological artifact observed in brain samples handled before fixation with aldehydes. To explore associations between dark neurons and immunohistochemical alterations in mouse brains, we examined protein products encoded by Cav3 (neuronal perikarya/neurites), Rbbp4 (neuronal nuclei), Gfap (astroglia), and Aif1 (microglia) genes in adjacent tissue sections. Here, dark neurons were incidental findings from our prior project, studying the effects of age and high-fat diet on metabolic homeostasis in male C57BL/6N mice. Available were brains from 4 study grou
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Wang, Nianwu, Wei Wang, Wenli Mao, et al. "RBBP4 Enhances Platinum Chemo Resistance in Lung Adenocarcinoma." BioMed Research International 2021 (January 9, 2021): 1–21. http://dx.doi.org/10.1155/2021/6905985.

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Background. The majority of lung cancers are adenocarcinomas, with the proportion being 40%. The patients are mostly diagnosed in the middle and late stages with metastasis and easy recurrence, which poses great challenge to the treatment and prognosis. Platinum-based chemotherapy is a primary treatment for adenocarcinoma, which frequently causes drug resistance. As a result, it is important to uncover the mechanisms of the chemoresponse of adenocarcinoma to platinum-based chemotherapy. Methods. The genes from the dataset GSE7880 were gathered into gene modules with the assistance of weighted
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Dissertations / Theses on the topic "RBBP4"

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Alqarni, Saad. "Protein Interactions in the Nucieosome Remodelling and Deacetylase (NuRD) complex." Thesis, The University of Sydney, 2013. http://hdl.handle.net/2123/9792.

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Chapter 1 presents a general introduction to NuRD. The NuRD complex is a widely conserved transcriptional coregulator that harbours both nucleosome remodelling and histone deacetylase activities. Abnormalities in a number of its constituent proteins are associated with both cancer and ageing. Although we have a fairly complete ‘parts list’ for NuRD, our understanding of what the parts actually look like and, in particular, how they fit together lags a long way behind. In mammals, the NuRD complex consists of approximately 10 proteins that are consistently observed in purifications of the compl
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Pretorius, Ashley. "Functional analysis of the mouse RBBP6 gene using Interference RNA." Thesis, University of the Western Cape, 2007. http://etd.uwc.ac.za/index.php?module=etd&action=viewtitle&id=gen8Srv25Nme4_4435_1264363734.

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<p>The aim of this thesis was to investigate the cellular role of the mouse RBBP6 gene using the interference RNA (RNAi) gene targeting technology and also to understand the relevance of two promoters for the RBBP6 gene.</p>
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Sun, Meidai. "Structural and functional characterization of human DNA repair protein CtIP/RBBP8." Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.648261.

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Muleya, Victor. "Structural characterisation of the interaction between RBBP6 and the multifunctional protein YB-1." Thesis, University of the Western Cape, 2010. http://etd.uwc.ac.za/index.php?module=etd&action=viewtitle&id=gen8Srv25Nme4_7667_1305266746.

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<p>As a means of further localising the interaction, truncated fragments derived from the C-terminal region of YB-1, were tested for their interaction with the RING finger domain of RBBP6 using three different assays: a directed yeast 2-hybrid assay, co-immunoprecipitation and NMR chemical shift perturbation analysis. Our results suggest that the entire 62 amino acid region at the C-terminal domain of YB-1 may be involved in the interaction with RBBP6. Using chemical shift perturbation analysis, this study provides an indication of where YB-1 binds to the RING finger. This represents the first
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Mosweu, Mpho. "Investigating the effects of RBBP6 gene expression on telomerase activity in cervical cancer." Diss., University of Pretoria, 2020. http://hdl.handle.net/2263/75200.

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Cancer remains a major health problem. It is ranked the second most common cause of death to cardiovascular diseases worldwide, with about 9.6 million deaths annually. This burden is greatly carried by developing countries, which are accountable for about 65% of cancer death worldwide. Retinoblastoma binding protein 6 (RBBP6) is one of the genes identified as proliferative gene that plays a role in cancer development. It has been shown together with telomerase activity to be highly increased in various cancer cells. E6 protein of human papillomavirus (HPV) and RBBP6 are known to enhance the pr
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Maumela, Matodzi Portia. "Characterisation of N-terminal fragments of Retinoblastoma Binding Protein 6 for structural analysis." University of the Western Cape, 2016. http://hdl.handle.net/11394/5313.

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>Magister Scientiae - MSc<br>Retinoblastoma Binding Protein 6 (RBBP6) is a 200 kDa RING finger-containing protein that plays a role in 3'-end poly-adenylation of mRNA transcripts as well as acting as an E3 ubiquitin ligase against a number of proteins involved in tumourigenesis, including p53. Since the human protein is too large and poorly structured for heterologous expression in bacteria, it would be advantageous to identify smaller fragments suitable for expression in bacteria. Many E3 ubiquitin ligases form homo-dimers and dimerisation is important for their activity; structural studies o
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Nagl, Britta [Verfasser]. "Bedeutung der Nieren für die Retinol-Bindungsprotein 4 (RBP4)-Plasma-Homöostase / Britta Nagl." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2011. http://d-nb.info/1025510208/34.

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Mlaza, Mihlali. "Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles." University of the Western Cape, 2018. http://hdl.handle.net/11394/6200.

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Retinoblastoma Binding Protein 6 (RBBP6) is a 200 KDa protein shown to play a role in 3'- polyadenylation of mRNA transcripts, as well as to function as an E3 ligase catalysing ubiquitination of cancer-associated proteins. RBBP6 has been previously reported to localise to nuclear speckles, which are thought to play a role in mRNA splicing, presumably as a result of its RS domain, which is known to target mRNA splicing factors to nuclear speckles. However recent studies in our laboratory have shown that isoform 3 of RBBP6, consisting mainly of the DWNN domain, also localises to speckles i
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Avdic, Vanja. "Structural and Functional Dissection of the MLL1 Histone Methyltransferase Complex." Thèse, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/19997.

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The mixed lineage leukemia (MLL) proteins regulate an array of developmental and differentiation processes. Similar to other members of the SET1 family, association of MLL1-4 with Ash2L, RbBP5 and WDR5, collectively termed the MLL core complex, is required for MLL mediated histone H3 Lys-4 di/tri-methylation. Each member of the core complex has a unique role in modulating the activity of MLL1. WDR5 is key in nucleating the formation of the core complex by acting as a structural scaffold, whereas Ash2L and RbBP5 are responsible for stimulating MLL methyltransferase activity. Currently, the stru
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Madi, Maher [Verfasser]. "Bedeutung des Retinol-bindenden Proteins 4 (RBP4) in der Pathogenese der nichtalkoholischen Fettlebererkrankung (NAFLD) / Maher Madi." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2013. http://d-nb.info/1043197028/34.

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Book chapters on the topic "RBBP4"

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Zabetian-Targhi, Fateme, and Maryame Mahmoudi. "Retinol-Binding Protein 4 (RBP4)." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101853.

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Zabetian-Targhi, Fateme, and Maryame Mahmoudi. "Retinol-Binding Protein 4 (RBP4)." In Encyclopedia of Signaling Molecules. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101853-1.

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Saucedo, Renata, Jorge Valencia, Lourdes Basurto, et al. "The Retinol Binding Protein-4 (RBP4) Gene and Gestational Diabetes." In Nutrition and Diet in Maternal Diabetes. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-56440-1_12.

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Laversenne, L. "Synthesis and crystal structure of alkali metal borohydrides LiBH4, NaBH4, KBH4, RbBH4 and CsBH4." In Hydrogen Storage Materials. Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-54261-3_50.

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"RBP4." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_103254.

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Chiefari, Eusebio, Francesco Paonessa, Stefania Iiritano, et al. "The Camp-HMGA1-RBP4 System." In Recent Advances in Biochemistry. Apple Academic Press, 2011. http://dx.doi.org/10.1201/b13131-11.

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Hotiana, M. M., A. Yaqub, J. Wheaton, R. Staneck, T. Gress, and Y. Elitsur. "Association of Retinol-Binding Protein 4 (RBP4) and Obesity in Children." In Posters XV. Endocrine Society, 2010. http://dx.doi.org/10.1210/endo-meetings.2010.part2.p15.p2-713.

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Chen, Jie-Gen, Anna Spagnoli, Zehra Pamuklar, and Alfonso Torquati. "Regulation of RBP4 Effect on Insulin Response by STRA6 in Human Adipocyte." In BASIC/TRANSLATIONAL - Diabetes & Glucose Homeostasis: Genetic & Translational Approaches. The Endocrine Society, 2011. http://dx.doi.org/10.1210/endo-meetings.2011.part3.p6.p2-522.

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Chielle, Eduardo Ottobelli, Eliandra Mirlei Rossi, and Eliane Maria de Carli. "INFLUÊNCIA DA PROTEINA LIGADORA DO RETINOL 4 (RBP4) NO DESENVOLVIMENTO DE RESISTÊNCIA INSULÍNICA EM OBESOS." In Princípios em Farmácia 2. Atena Editora, 2019. http://dx.doi.org/10.22533/at.ed.0991902083.

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"Effects of aerobic exercise and a high-carbohydrate diet on RBP4 expression in rat skeletal muscle." In Advances in Biomolecular Medicine, edited by Nuroh Najmi, Yunia Sribudiani, Bethy S. Hernowo, Hanna Goenawan Setiawan, Vita M. Tarawan, and Ronny Lesmana. CRC Press, 2017. http://dx.doi.org/10.1201/9781315208619-9.

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Conference papers on the topic "RBBP4"

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Reed, Rebecca A., Miao-Chia Lo, and Duxin Sun. "Abstract 106: Characterization of polycomb repressive complex 2 (PRC2) subunits retinoblastoma-binding protein 4 and 7 (RbBP4/7) in triple-negative breast cancer." 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.am2015-106.

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Reed, Rebecca, Miao-Chia Lo, Chang-Ching Lin, and Duxin Sun. "Abstract 3091: Development and optimization of a fluorescence polarization-based assay for the discovery of inhibitors of the RBBP4/7-Histone H3 interaction." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3091.

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Moela, Pontsho, Lesetja Motadi, and Marcia Lekganyane. "Abstract 3040: The expressional effects of RBBP6 in breast cancer cells are p53-dependent." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3040.

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Moela, Pontsho, Lesetja Motadi, and Marcia Lekganyane. "Abstract 3040: The expressional effects of RBBP6 in breast cancer cells are p53-dependent." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3040.

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Dlamini, Zodwa, and Zukile Mbita. "Abstract 99: Posttranslational modification of the RBBP6 isoform 3 is required for excessive cell proliferation." 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.am2012-99.

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Choene, Mpho, Pontsho Moela, and Lesetja Motadi. "Abstract 3517: Expression studies of RBBP6 in breast and cervical cancer suggests a role in apoptosis activation." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3517.

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Motadi, Lesetja Raymond, Pontsho Moela, and Mpho S. Choene. "Abstract 344: Silencing RBBP6 (retinoblastoma binding protein 6) sensitizes breast cancer cells to staurosporine and camptothecin-induced cell death." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-344.

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Mbita, Zukile, Amanda Skepu, David Pugh, Jasper Rees, Zodwa Dlamini, and Mervin Meyer. "Abstract 1085: RbBP6 isoform 3/DWNN is essential for arsenic trioxide-induced G2/M arrest in cancer cell lines." 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.am10-1085.

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Motadi, lesetja R., and pontsho Moela. "Abstract 4308: RBBP6 expressional effects on cell proliferation and apoptosis in breast cancer cell lines with distinct p53 statuses." 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.am2018-4308.

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Dlamini, Zodwa, Zukile Mbita, Amanda Skepu, David Pugh, Jasper Rees, and Mervin Meyer. "Abstract 1265: RbBP6 Isoform 3 (DWNN) is a p53 stabilizer in arsenic trioxide-induced apoptosis in human cancer cell lines." 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.am10-1265.

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Reports on the topic "RBBP4"

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Aldaz, C. M. CtlP (RBBP8) a Critical Player in the Development of Tamoxifen Resistance in Human Breast Cancer. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada456009.

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