Relevant bibliographies by topics / Ribonucleoprotein particles RNPs

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  2. Dissertations / Theses
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Academic literature on the topic 'Ribonucleoprotein particles RNPs'

Author: Grafiati
Published: 9 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Ribonucleoprotein particles RNPs"

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Peek, R., G. J. Pruijn, A. J. van der Kemp, and W. J. van Venrooij. "Subcellular distribution of Ro ribonucleoprotein complexes and their constituents." Journal of Cell Science 106, no. 3 (1993): 929–35. http://dx.doi.org/10.1242/jcs.106.3.929.

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Ro ribonucleoprotein particles (Ro RNPs) are complexes of several proteins with a small RNA polymerase III-transcribed Ro RNA. Despite their relative abundance and evolutionary conservation no function has as yet been ascribed to these complexes. Also their subcellular distribution is still largely unknown as immunofluorescence studies concerning their localization have produced conflicting data. We have used cell enucleation to fractionate cells into cytoplasmic and nuclear fractions. Analysis of these fractions revealed an exclusively cytoplasmic localization for the Ro RNPs. The majority of
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Liang, Bo, and Hong Li. "Structures of ribonucleoprotein particle modification enzymes." Quarterly Reviews of Biophysics 44, no. 1 (2010): 95–122. http://dx.doi.org/10.1017/s0033583510000235.

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AbstractSmall nucleolar and Cajal body ribonucleoprotein particles (RNPs) are required for the maturation of ribosomes and spliceosomes. They consist of small nucleolar RNA or Cajal body RNA combined with partner proteins and represent the most complex RNA modification enzymes. Recent advances in structure and function studies have revealed detailed information regarding ribonucleoprotein assembly and substrate binding. These enzymes form intertwined RNA–protein assemblies that facilitate reversible binding of the large ribosomal RNA or small nuclear RNA. These revelations explain the specific
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Simons, F. H., G. J. Pruijn, and W. J. van Venrooij. "Analysis of the intracellular localization and assembly of Ro ribonucleoprotein particles by microinjection into Xenopus laevis oocytes." Journal of Cell Biology 125, no. 5 (1994): 981–88. http://dx.doi.org/10.1083/jcb.125.5.981.

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Xenopus laevis oocytes have been used to determine the intracellular localization of components of Ro ribonucleoprotein particles (Ro RNPs) and to study the assembly of these RNA-protein complexes. Microinjection of the protein components of human Ro RNPs, i.e., La, Ro60, and Ro52, in X. laevis oocytes showed that all three proteins are able to enter the nucleus, albeit with different efficiencies. In contrast, the RNA components of human Ro RNPs (the Y RNAs) accumulate in the X. laevis cytoplasm upon injection. Localization studies performed at low temperatures indicated that both nuclear imp
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Peek, R., G. J. Pruijn, and W. J. van Venrooij. "Epitope specificity determines the ability of anti-Ro52 autoantibodies to precipitate Ro ribonucleoprotein particles." Journal of Immunology 153, no. 9 (1994): 4321–29. http://dx.doi.org/10.4049/jimmunol.153.9.4321.

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Abstract Ro ribonucleoprotein particles (Ro RNPs) are evolutionarily conserved cytoplasmic complexes of unknown function. They are composed of several proteins and a small, RNA polymerase III-transcribed Ro or Y RNA. Abs directed against the protein moiety of Ro RNPs are often found in sera of patients suffering from certain autoimmune disorders. The association of one of the Ro proteins, a protein of 52 kDa (Ro52), with Ro RNPs is still questionable. In this study, we have used anti-Ro52 Abs isolated from autoimmune sera to locate the antigenic determinants of Ro52 and to analyze the correlat
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Hall, Kathleen B. "RNA and Proteins: Mutual Respect." F1000Research 6 (March 27, 2017): 345. http://dx.doi.org/10.12688/f1000research.10572.1.

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Proteins and RNA are often found in ribonucleoprotein particles (RNPs), where they function in cellular processes to synthesize proteins (the ribosome), chemically modify RNAs (small nucleolar RNPs), splice pre-mRNAs (the spliceosome), and, on a larger scale, sequester RNAs, degrade them, or process them (P bodies, Cajal bodies, and nucleoli). Each RNA–protein interaction is a story in itself, as both molecules can change conformation, compete for binding sites, and regulate cellular functions. Recent studies of Xist long non-coding RNP, the U4/5/6 tri-small nuclear RNP complex, and an activat
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Bachmann, M., W. J. Mayet, H. C. Schröder, K. Pfeifer, K. H. Meyer zum Büschenfelde, and W. E. G. Müller. "Identification of the Ro and La antigens in the endoribonuclease VII–ribonucleoprotein complex." Biochemical Journal 243, no. 1 (1987): 189–94. http://dx.doi.org/10.1042/bj2430189.

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45 S RNP (ribonucleoprotein) particles from calf thymus or L5178y mouse lymphoma cells contain the poly(A)-modulated and oligo(U)-binding endoribonuclease VII [Bachmann, Zahn & Müller (1983) J. Biol. Chem. 258, 7033-7040]. From these particles a 4.5 S RNA was isolated that possesses an oligo(U) sequence. By using monospecific and non-cross-reacting antibodies directed against the La or Ro antigen, both proteins were identified in the endoribonuclease VII-RNP complex after phosphorylation in vitro. In a second approach, endoribonuclease VII activity was identified in immunoaffinity-purified
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Wurtz-T, E. Kiseleva, G. Nacheva, A. Alzhanova-Ericcson, A. Rosén, and B. Daneholt. "Identification of two RNA-binding proteins in Balbiani ring premessenger ribonucleoprotein granules and presence of these proteins in specific subsets of heterogeneous nuclear ribonucleoprotein particles." Molecular and Cellular Biology 16, no. 4 (1996): 1425–35. http://dx.doi.org/10.1128/mcb.16.4.1425.

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Balbiani ring (BR) granules are premessenger ribonucleoprotein particles (RNPs) generated in giant chromosomal puffs, the BRs, in the larval salivary glands of the dipteran chironomus tentans. Monoclonal antibodies were raised against nuclear proteins collected on a single-stranded-DNA-agarose affinity column, and two of them were used to identify RNA-binding proteins in BR granules. First, in Western blots (immunoblots), one of the antibodies recognized a 36-kDa protein and the other recognized a 45-KDa protein. Second, both antibodies bound to the BRs in immunocytological experiments. It was
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Kedersha, Nancy L., and Leonard H. Rome. "Immunolocalization of vault particles in cultured cells." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (1992): 458–59. http://dx.doi.org/10.1017/s0424820100122691.

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We first reported on the existence of vault ribonucleoprotein particles in 1986, and since this study we have demonstrated that these unusual RNPs are ubiquitously expressed and highly conserved among diverse eukaryotes. These particles are quite large (65 x 35 nm) and distinctly regular in shape and dimensions. The polypeptide composition of vaults is also similar between species, dominated by a∼100 Kd protein which makes up >70% of the particles mass. The RNA component of vaults, which has been sequenced and characterized from both rat and bullfrog, does not appear to serve a structural r
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Zillmann, M., M. L. Zapp, and S. M. Berget. "Gel electrophoretic isolation of splicing complexes containing U1 small nuclear ribonucleoprotein particles." Molecular and Cellular Biology 8, no. 2 (1988): 814–21. http://dx.doi.org/10.1128/mcb.8.2.814-821.1988.

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Assembly of splicing precursor RNAs into ribonucleoprotein particle (RNP) complexes during incubation in in vitro splicing extracts was monitored by a new system of RNP gel electrophoresis. The temporal pattern of assembly observed by our system was identical to that obtained by other gel and gradient methodologies. In contrast to the results obtained by other systems, however, we observed requirements of U1 small nuclear RNPs (snRNPs) and 5' splice junction sequences for formation of specific complexes and retention of U1 snRNPs within gel-fractionated complexes. Single-intron substrate RNAs
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Zillmann, M., M. L. Zapp, and S. M. Berget. "Gel electrophoretic isolation of splicing complexes containing U1 small nuclear ribonucleoprotein particles." Molecular and Cellular Biology 8, no. 2 (1988): 814–21. http://dx.doi.org/10.1128/mcb.8.2.814.

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Assembly of splicing precursor RNAs into ribonucleoprotein particle (RNP) complexes during incubation in in vitro splicing extracts was monitored by a new system of RNP gel electrophoresis. The temporal pattern of assembly observed by our system was identical to that obtained by other gel and gradient methodologies. In contrast to the results obtained by other systems, however, we observed requirements of U1 small nuclear RNPs (snRNPs) and 5' splice junction sequences for formation of specific complexes and retention of U1 snRNPs within gel-fractionated complexes. Single-intron substrate RNAs
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Dissertations / Theses on the topic "Ribonucleoprotein particles RNPs"

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SALA, SIMONA. "THE E3 UBIQUITIN LIGASE HECW1 IN NEURONAL HOMEOSTASIS." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/883944.

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Ubiquitination is one of the most abundant and versatile post-translation modifications in eukaryotes that affects many biological processes by modifying protein activity, interactions, localization and stability of substrates. E3 ligases have a key function in the process, acting as molecular ubiquitin-substrate matchmakers and providing specificity to the reaction. In this thesis, we aimed at characterizing the physiological and pathological functions of the human HECW1, a poorly studied E3 ligase which belongs to the NEDD4 family. HECW1 is preferentially expressed in the central nervous
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Kylberg, Karin. "Transcription and transport of a messenger RNP particle : novel regulatory mechanisms /." Stockholm : Karolinska institutet, 2007. http://diss.kib.ki.se/2007/978-91-7357-318-4/.

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Zorbas, Christiane. "Etudes de la biogenèse du ribosome chez l'Homme." Doctoral thesis, Universite Libre de Bruxelles, 2015. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/209010.

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Les ribosomes sont des macrocomplexes ribonucléoprotéiques sophistiqués, essentiels pour décoder l’information génétique et la traduire en protéines fonctionnelles. Chez les organismes eucaryotes, le ribosome est constitué de deux sous-unités, la petite (40S) et la grande (60S). Leur biogenèse est un processus fondamental, très complexe, qui mène à la synthèse et l’assemblage de 4 ARNr et 80 protéines ribosomiques (79 chez la levure). La biogenèse du ribosome a longtemps été étudiée chez Saccharomyces cerevisiae. Près de 20 ans de recherches ont été nécessaires à la communauté scientifique pou
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Neuenkirchen, Nils. "An in vitro system for the biogenesis of small nuclear ribonucleoprotein particles." Doctoral thesis, 2012. https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-71300.

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Most protein-encoding genes in Eukaryotes are separated into alternating coding and non-coding sequences (exons and introns). Following the transcription of the DNA into pre-messenger RNA (pre-mRNA) in the nucleus, a macromolecular complex termed spliceosome removes the introns and joins the exons to generate mature mRNA that is exported to the cytoplasm. There, it can be interpreted by ribosomes to generate proteins. The spliceosome consists of five small nuclear ribonucleic acids (snRNAs) and more than 150 proteins. Integral components of this complex are RNA-protein particles (RNPs) compose
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Liu, Wen-ti. "Strategies to stabilize RNP complexes for structural determination by 3D cryo-electron microscopy." Doctoral thesis, 2013. http://hdl.handle.net/11858/00-1735-0000-0023-9915-E.

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Books on the topic "Ribonucleoprotein particles RNPs"

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Johannes, Schenkel, ed. RNP particles, splicing, and autoimmune diseases. Springer, 1998.

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Schenkel, Johannes. RNP Particles, Splicing and Autoimmune Diseases. Springer London, Limited, 2012.

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Schenkel, Johannes. RNP Particles, Splicing and Autoimmune Diseases. Springer Berlin / Heidelberg, 2012.

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Book chapters on the topic "Ribonucleoprotein particles RNPs"

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Mandal, Prabhat K., and Haig H. Kazazian. "Purification of L1-Ribonucleoprotein Particles (L1-RNPs) from Cultured Human Cells." In Methods in Molecular Biology. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3372-3_19.

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Marchand, Virginie, Annie Mougin, Agnès Méreau, Isabelle Behm-Ansmant, Yuri Motorin, and Christiane Branlant. "Study of RNA-Protein Interactions and RNA Structure in Ribonucleoprotein Particles (RNPs)." In Handbook of RNA Biochemistry. Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527647064.ch44.

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Reddy, Ram, and Harris Busch. "Small Nuclear RNAs: RNA Sequences, Structure, and Modifications." In Structure and Function of Major and Minor Small Nuclear Ribonucleoprotein Particles. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73020-7_1.

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Dahlberg, James E., and Elsebet Lund. "The Genes and Transcription of the Major Small Nuclear RNAs." In Structure and Function of Major and Minor Small Nuclear Ribonucleoprotein Particles. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73020-7_2.

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Teubl, Fabian, Katrin Schwank, Uli Ohmayer, Joachim Griesenbeck, Herbert Tschochner, and Philipp Milkereit. "Tethered MNase Structure Probing as Versatile Technique for Analyzing RNPs Using Tagging Cassettes for Homologous Recombination in Saccharomyces cerevisiae." In Ribosome Biogenesis. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_8.

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AbstractMicrococcal nuclease (MNase) originating from Staphylococcus aureus is a calcium dependent ribo- and desoxyribonuclease which has endo- and exonucleolytic activity of low sequence preference. MNase is widely used to analyze nucleosome positions in chromatin by probing the enzyme’s DNA accessibility in limited digestion reactions. Probing reactions can be performed in a global way by addition of exogenous MNase, or locally by “chromatin endogenous cleavage” (ChEC) reactions using MNasefusion proteins. The latter approach has recently been adopted for the analysis of local RNA environmen
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Hajduk, Stephen L., and robert S. Sabatini. "RNA editing: posttranscriptional restructuring of genetic information." In Molecular Biology of Parasitic Protozoa. Oxford University PressOxford, 1996. http://dx.doi.org/10.1093/oso/9780199636020.003.0008.

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Abstract The formation of translatable mRNAs in the mitochondrion of kinetoplastid protozoa often requires the precise addition or deletion of uridines by RNA editing. The sites of uridine insertion and deletion are specified by small guide RNAs (gRNAs) which appear to function in directing the editing reactions. The extent of RNA editing can vary from the modest four uridines inserted into the cytochrome oxidase II mRNA, to the extensive editing seen in the cytochrome oxidase III mRNA of Trypanosoma brucei, in which hundreds of uridines are added and dozens are deleted. In most cases, the pre
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Will, Cindy L., Berthold Kastner, and Reinhard Lührmann. "Analysis of ribonucleoprotein interactions." In RNA Processing. Oxford University PressOxford, 1994. http://dx.doi.org/10.1093/oso/9780199633449.003.0005.

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Abstract Elucidation of the precise function of small ribonucleoprotein particles (snRNPs) in RNA processing will be greatly aided by information regarding their biochemical composition and higher order structure. To date, significant biochemical and structural information has been gathered for the mammalian spliceosomal snRNPs Ul, U2, U5, and U4/U6, although their characterization is far from complete. The snRNA component of these functionally important RNP particles has been shown to be evolutionarily conserved and, with the exception of U6, possesses a unique 5’ cap structure, namely 2,2,7-
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TOKAR, S. L. "INHIBITION OF PROTON CONDUCTANCE OF THE INFLUENZA A M2 CHANNEL BY AMINOADAMANTANES." In ESSAYS ON NEUROPHYSIOLOGY BY PLATON KOSTYUK AND HIS STUDENTS. AKADEMPERIODYKA, 2020. https://doi.org/10.15407/biph.books.essneur.279.

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The M2 protein of in］ uenza A virus is the smallest known protein which exhibits the basic properties of an ion channel. It is characterized by high proton selectivity and a proton regulated gating mechanism (Chizhmakov et al., 1996a). The proton conductivity of the M2 protein plays important roles in two stages of virus replication. As virus particles enter cells by endocytosis, the M2 channel transfers protons from the acidic endosomal environment to the virus interior, triggering dissociation of the viral matrix protein from the viral ribonucleoprotein (RNP) and release of free viral RNP. t
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Benarroch, Eduardo E. "Messenger RNA Metabolism." In Neuroscience for Clinicians, edited by Eduardo E. Benarroch. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780190948894.003.0005.

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Metabolism of messenger RNA (mRNA) is critical for control of cell phenotype and includes several steps: transcription of DNA into a pre-mRNA, mRNA maturation, nucleocytoplasmic export and transport to specific cellular locations, translation into proteins, and decay. All these steps are seamlessly integrated and controlled by a large number of RNA-binding proteins that interact with RNA, forming messenger ribonucleoprotein particles. Several noncoding RNAs, such as microRNAs, also regulate mRNA metabolism. Activity-dependent control of mRNA transcription, splicing, and translation are critica
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Will, Cindy l., and reinhard lÜhrmann. "snRNP structure and function." In Eukaryotic mRNA Processing. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780199634187.003.0005.

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Abstract In contrast to self-splicing RNA molecules which contain extensive, highly con¬ served structural elements sufficient for intron excision and exon ligation, nuclear pre-mRNA molecules possess short, conserved sequences which are limited to the 5’ and 3’ splice site and branchpoint regions (see Chapters 1, 4, and 8). While these sequences are necessary for the conversion of the pre-mRNA to mRNA, they are not sufficient. Nuclear pre-mRNA splicing is thus dependent upon the activity of a number of trans-acting splicing factors, which in addition to protein factors, include the four small
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