Relevant bibliographies by topics / SR proteins

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

Academic literature on the topic 'SR proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 16 November 2024

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Journal articles on the topic "SR proteins"

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Kataoka, Naoyuki, Jennifer L. Bachorik, and Gideon Dreyfuss. "Transportin-SR, a Nuclear Import Receptor for SR Proteins." Journal of Cell Biology 145, no. 6 (1999): 1145–52. http://dx.doi.org/10.1083/jcb.145.6.1145.

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The SR proteins, a group of abundant arginine/serine (RS)-rich proteins, are essential pre-mRNA splicing factors that are localized in the nucleus. The RS domain of these proteins serves as a nuclear localization signal. We found that RS domain–bearing proteins do not utilize any of the known nuclear import receptors and identified a novel nuclear import receptor specific for SR proteins. The SR protein import receptor, termed transportin-SR (TRN-SR), binds specifically and directly to the RS domains of ASF/SF2 and SC35 as well as several other SR proteins. The nuclear transport regulator RanGTP abolishes this interaction. Recombinant TRN-SR mediates nuclear import of RS domain– bearing proteins in vitro. TRN-SR has amino acid sequence similarity to several members of the importin β/transportin family. These findings strongly suggest that TRN-SR is a nuclear import receptor for the SR protein family.
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Jin, Xiaoli. "Regulatory Network of Serine/Arginine-Rich (SR) Proteins: The Molecular Mechanism and Physiological Function in Plants." International Journal of Molecular Sciences 23, no. 17 (2022): 10147. http://dx.doi.org/10.3390/ijms231710147.

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Serine/arginine-rich (SR) proteins are a type of splicing factor. They play significant roles in constitutive and alternative pre-mRNA splicing, and are involved in post-splicing activities, such as mRNA nuclear export, nonsense-mediated mRNA decay, mRNA translation, and miRNA biogenesis. In plants, SR proteins function under a complex regulatory network by protein–protein and RNA–protein interactions between SR proteins, other splicing factors, other proteins, or even RNAs. The regulatory networks of SR proteins are complex—they are regulated by the SR proteins themselves, they are phosphorylated and dephosphorylated through interactions with kinase, and they participate in signal transduction pathways, whereby signaling cascades can link the splicing machinery to the exterior environment. In a complex network, SR proteins are involved in plant growth and development, signal transduction, responses to abiotic and biotic stresses, and metabolism. Here, I review the current status of research on plant SR proteins, construct a model of SR proteins function, and ask many questions about SR proteins in plants.
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Allemand, Eric, Svetlana Dokudovskaya, Rémy Bordonné, and Jamal Tazi. "A Conserved DrosophilaTransportin-Serine/Arginine-rich (SR) Protein Permits Nuclear Import ofDrosophila SR Protein Splicing Factors and Their Antagonist Repressor Splicing Factor 1." Molecular Biology of the Cell 13, no. 7 (2002): 2436–47. http://dx.doi.org/10.1091/mbc.e02-02-0102.

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Members of the highly conserved serine/arginine-rich (SR) protein family are nuclear factors involved in splicing of metazoan mRNA precursors. In mammals, two nuclear import receptors, transportin (TRN)-SR1 and TRN-SR2, are responsible for targeting SR proteins to the nucleus. Distinctive features in the nuclear localization signal between Drosophila and mammalian SR proteins prompted us to examine the mechanism by whichDrosophila SR proteins and their antagonist repressor splicing factor 1 (RSF1) are imported into nucleus. Herein, we report the identification and characterization of a Drosophilaimportin β-family protein (dTRN-SR), homologous to TRN-SR2, that specifically interacts with both SR proteins and RSF1. dTRN-SR has a broad localization in the cytoplasm and the nucleus, whereas an N-terminal deletion mutant colocalizes with SR proteins in nuclear speckles. Far Western experiments established that the RS domain of SR proteins and the GRS domain of RSF1 are required for the direct interaction with dTRN-SR, an interaction that can be modulated by phosphorylation. Using the yeast model system in which nuclear import of Drosophila SR proteins and RSF1 is impaired, we demonstrate that complementation with dTRN-SR is sufficient to target these proteins to the nucleus. Together, the results imply that the mechanism by which SR proteins are imported to the nucleus is conserved between Drosophila and humans.
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Manley, J. L., and R. Tacke. "SR proteins and splicing control." Genes & Development 10, no. 13 (1996): 1569–79. http://dx.doi.org/10.1101/gad.10.13.1569.

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Wan, Ledong, Min Deng, and Honghe Zhang. "SR Splicing Factors Promote Cancer via Multiple Regulatory Mechanisms." Genes 13, no. 9 (2022): 1659. http://dx.doi.org/10.3390/genes13091659.

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Substantial emerging evidence supports that dysregulated RNA metabolism is associated with tumor initiation and development. Serine/Arginine-Rich proteins (SR) are a number of ultraconserved and structurally related proteins that contain a characteristic RS domain rich in arginine and serine residues. SR proteins perform a critical role in spliceosome assembling and conformational transformation, contributing to precise alternative RNA splicing. Moreover, SR proteins have been reported to participate in multiple other RNA-processing-related mechanisms than RNA splicing, such as genome stability, RNA export, and translation. The dysregulation of SR proteins has been reported to contribute to tumorigenesis through multiple mechanisms. Here we reviewed the different biological roles of SR proteins and strategies for functional rectification of SR proteins that may serve as potential therapeutic approaches for cancer.
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Slišković, Irena, Hannah Eich, and Michaela Müller-McNicoll. "Exploring the multifunctionality of SR proteins." Biochemical Society Transactions 50, no. 1 (2021): 187–98. http://dx.doi.org/10.1042/bst20210325.

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Members of the arginine–serine-rich protein family (SR proteins) are multifunctional RNA-binding proteins that have emerged as key determinants for mRNP formation, identity and fate. They bind to pre-mRNAs early during transcription in the nucleus and accompany bound transcripts until they are translated or degraded in the cytoplasm. SR proteins are mostly known for their essential roles in constitutive splicing and as regulators of alternative splicing. However, many additional activities of individual SR proteins, beyond splicing, have been reported in recent years. We will summarize the different functions of SR proteins and discuss how multifunctionality can be achieved. We will also highlight the difficulties of studying highly versatile SR proteins and propose approaches to disentangle their activities, which is transferrable to other multifunctional RBPs.
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Blencowe, Benjamin J., John AL Bowman, Susan McCracken, and Emanuel Rosonina. "SR-related proteins and the processing of messenger RNA precursors." Biochemistry and Cell Biology 77, no. 4 (1999): 277–91. http://dx.doi.org/10.1139/o99-048.

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The processing of messenger RNA precursors (pre-mRNA) to mRNA in metazoans requires a large number of proteins that contain domains rich in alternating arginine and serine residues (RS domains). These include members of the SR family of splicing factors and proteins that are structurally and functionally distinct from the SR family, collectively referred to below as SR-related proteins. Both groups of RS domain proteins function in constitutive and regulated pre-mRNA splicing. Recently, several SR-related proteins have been identified that are associated with the transcriptional machinery. Other SR-related proteins are associated with mRNA 3prime end formation and have been implicated in export. We review these findings and evidence that proteins containing RS domains may play a fundamental role in coordinating different steps in the synthesis and processing of pre-mRNA.Key words: SR protein, RNA polymerase, spliceosome, polyadenylation, nuclear matrix.
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Bubulya, Paula A., Kannanganattu V. Prasanth, Thomas J. Deerinck, et al. "Hypophosphorylated SR splicing factors transiently localize around active nucleolar organizing regions in telophase daughter nuclei." Journal of Cell Biology 167, no. 1 (2004): 51–63. http://dx.doi.org/10.1083/jcb.200404120.

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Upon completion of mitosis, daughter nuclei assemble all of the organelles necessary for the implementation of nuclear functions. We found that upon entry into daughter nuclei, snRNPs and SR proteins do not immediately colocalize in nuclear speckles. SR proteins accumulated in patches around active nucleolar organizing regions (NORs) that we refer to as NOR-associated patches (NAPs), whereas snRNPs were enriched at other nuclear regions. NAPs formed transiently, persisting for 15–20 min before dissipating as nuclear speckles began to form in G1. In the absence of RNA polymerase II transcription, NAPs increased in size and persisted for at least 2 h, with delayed localization of SR proteins to nuclear speckles. In addition, SR proteins in NAPs are hypophosphorylated, and the SR protein kinase Clk/STY colocalizes with SR proteins in NAPs, suggesting that phosphorylation releases SR proteins from NAPs and their initial target is transcription sites. This work demonstrates a previously unrecognized role of NAPs in splicing factor trafficking and nuclear speckle biogenesis.
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Prasad, Jayendra, Karen Colwill, Tony Pawson, and James L. Manley. "The Protein Kinase Clk/Sty Directly Modulates SR Protein Activity: Both Hyper- and Hypophosphorylation Inhibit Splicing." Molecular and Cellular Biology 19, no. 10 (1999): 6991–7000. http://dx.doi.org/10.1128/mcb.19.10.6991.

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ABSTRACT The splicing of mammalian mRNA precursors requires both protein phosphorylation and dephosphorylation, likely involving modification of members of the SR protein family of splicing factors. Several kinases have been identified that can phosphorylate SR proteins in vitro, and transfection assays have provided evidence that at least one of these, Clk/Sty, can modulate splicing in vivo. But evidence that a specific kinase can directly affect the splicing activity of SR proteins has been lacking. Here, by using purified recombinant Clk/Sty, a catalytically inactive mutant, and individual SR proteins, we show that Clk/Sty directly affects the activity of SR proteins, but not other essential splicing factors, in reconstituted splicing assays. We also provide evidence that both hyper- and hypophosphorylation inhibit SR protein splicing activity, repressing constitutive splicing and switching alternative splice site selection. These findings indicate that Clk/Sty directly and specifically influences the activity of SR protein splicing factors and, importantly, show that both under- and overphosphorylation of SR proteins can modulate splicing.
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Sanford, J. R., J. Ellis, and J. F. Cáceres. "Multiple roles of arginine/serine-rich splicing factors in RNA processing." Biochemical Society Transactions 33, no. 3 (2005): 443–46. http://dx.doi.org/10.1042/bst0330443.

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SR proteins (serine- and arginine-rich proteins) are an evolutionarily conserved family consisting of essential pre-mRNA splicing factors. Since their discovery and initial characterization, roles of SR proteins in pre-mRNA splicing and in subsequent steps of post-transcriptional gene expression have expanded significantly. The current hypotheses suggest that SR proteins are multifunctional adaptor molecules that may couple distinct steps of RNA metabolism. In the present study, we will provide an overview of the roles of SR proteins in different steps of post-transcriptional gene expression.
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Dissertations / Theses on the topic "SR proteins"

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Xu, Xiangdong. "Characterization of SR proteins during organ development /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2005. http://wwwlib.umi.com/cr/ucsd/fullcit?p3166408.

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Brugiolo, Mattia. "The dynamic RNA-binding behavior of SR proteins." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2016. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-191373.

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In the cell, the genetic information encoded in the DNA is transcribed to RNA. All RNAs that are transcribed in the cell are initially produced as precursor RNAs, which have to undergo various steps of processing to obtain their mature form. The maturation and processing for all RNA classes requires the activity of multiple RNA binding proteins (RBPs). An important family of RBPs that is involved in RNA maturation and processing is the SR-protein family. SR proteins are important for the regulation of a multitude of processes that include: splicing, transcription, export, RNA stabilization, translation and ncRNA processing. As of yet, there have been no comprehensive studies that describe how SR proteins dynamically regulate the maturation of RNAs. The results presented in this thesis provide new insights into the function and activity of SR proteins during RNA maturation. My experiments greatly expand the knowledge surrounding the action of RNA-binding proteins in vivo and in different cell compartments. To study the action of two different SR proteins in different cell compartments, I developed a new technique that combines cell fractionation and iCLIP, which I named FRACKING. For the first time, this method allowed me to collect information regarding the subcellular location where the RNA-protein interactions are taking place, giving a dynamic picture of the in vivo binding of SR proteins and of RNA binding proteins (RBP) in general. By using FRACKING on two heavily shuttling SR proteins, SRSF3 and SRSF7, I showed that both SR proteins are very dynamic in their binding behavior with RNAs. My research showed that both SRSF3 and SRSF7 strongly associate with RNAs during transcription (co-transcriptionally) and that they often remain bound to these transcripts until they are exported to the cytoplasm. The functions of SRSF3 and SRSF7 are closely related to their binding location on the target RNAs. I identified a subset of highly conserved introns that associated with SR proteins and are retained in their transcripts. These intron-retaining isoforms, contrary to textbook knowledge, are exported to the cytoplasm. I showed, for the first time, that SRSF3 and SRSF7 strongly interact with snoRNAs in the chromatin, and that this snoRNA-SR-protein binding behavior is distinct between SRSF3 and SRSF7. SRSF3 binds to the mature snoRNA sequence, and also to the surrounding intronic sequences, pointing towards a possible activity in guiding snoRNA maturation. Whereas SRSF7 associates to mature snoRNA sequences. Taken together, my study identified a dynamic pool of interactions for two SR proteins, in different cell compartments and discovered new activities for the two SR proteins. Importantly, this study challenges textbook knowledge on splicing and export of mRNAs by identifying a subset of transcripts that can be exported even when they retain introns.
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Baierlein, Claudia [Verfasser], and Heike [Akademischer Betreuer] Krebber. "Analysen des SR-Proteins Npl3 in der Translation und Charakterisierung von SR-Domänen-vermittelten Protein-Interaktionen von Npl3 / Claudia Baierlein. Betreuer: Heike Krebber." Marburg : Philipps-Universität Marburg, 2014. http://d-nb.info/1051934346/34.

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Stark, Jeremy M. "SR proteins can function during alternative splicing to mediate exon/exon associations /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/5020.

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Estmer, Nilsson Camilla. "Viral Control of SR Protein Activity." Doctoral thesis, Uppsala : Acta Universatis Upsaliensis : Univ.-bibl. [distributör], 2001. http://publications.uu.se/theses/91-554-5124-1/.

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Ring, Andreas. "Serine/Arginine-rich proteins in Physcomitrella patens." Thesis, Linköpings universitet, Molekylär genetik, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-80870.

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Serine/Arginine-rich proteins (SR-proteins) have been well characterized in metazoans and in the flowering plant Arabidopsis thaliana. But so far no attempts on characterizing SR-proteins in the moss Physcomitrella patens have been done. SR-proteins are a conserved family of splicing regulators essential for constitutive- and alternative splicing. SR-proteins are mediators of alternative splicing (AS) and may be alternatively spliced themselves as a form of gene regulation. Three novel SR-proteins of the SR-subfamily were identified in P. patens. The three genes show conserved intron-exon structure and protein domain distribution, not surprising since the gene family has evidently evolved through gene duplications. The SR-proteins PpSR40 and PpSR36 show differential tissue-specific expression, whereas PpSR39 does not. Tissue-specific expression of SR-proteins has also been seen in A. thaliana. SR-proteins determine splice-site usage in a concentration dependent manner. SR-protein overexpression experiments in A. thaliana and Oryza sativa have shown alteration of splicing patterns of endogenous SR-proteins. Overexpression of PpSR40 did not alter the splicing patterns of PpSR40, PpSR36 and PpSR39. This suggests that they might not be a substrate for PpSR40. These first results of SR-protein characterization in P. patens may provide insights on the SR-protein regulation mechanisms of the common land plant ancestor.
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VIVARELLI, SILVIA. "New roles for RNA processing factors CFIm68 and SRPK2 highlight unexpected links in the control of mammalian gene expression." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2010. http://hdl.handle.net/10281/10747.

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The aim of the first work (presented in the Chapter 2) was to investigate the role performed by SRPK2 kinase in the regulation of alternative splicing in SH-SY5Y neuroblastoma cells after paraquat treatment (a complex I mitochondrial respiratory chain inhibitor). Alternative splicing is a versatile form of genetic control whereby a common precursor messenger RNA (pre-mRNA) is processed into multiple mRNA isoforms differing in their precise combination of exon sequences. This process is particularly important in the nervous system and its essential nature is underscored by the finding that its misregulation is a common feature of human diseases, including neurodegenerative pathologies. Our approach to gain insight the regulation of neuron specific pre-mRNA splicing brought us to the characterization of SRPK2 kinase because this protein phosphorylates Serine/Arginine-rich domain (RS-domain)-containing proteins and it is expressed almost exclusively in the nervous system. In order to understand how SRPK2 intracellular localization and activity are regulated, in first instance we performed a mutational analysis. These mutants have been characterized by transient transfection in SH-SY5Y neuroblastoma cells. We analysed SRPK2 intracellular localization both under physiological condition and after generating stress through mitochondrial damage, since mitochondrial damage and oxidative stress are found in many neurodegenerative diseases. We also determined the effect of this stress treatment on SRPK2 phosphorylation and its nuclear translocation. We did this first by using the minigene E1A, an alternative splicing reporter system, and also by analysing both SR proteins intracellular localization and their phosphorylation status. This work showed that not only paraquat treatment increased the phosphorylated SRPK2 fraction, but also that a specific phosphorylation at its 581 residue could be connected with the nuclear translocation of SRPK2. Consequently, this nuclear translocation brought to a splicing change in the isoform ratio of the minigene reporter system. After the drug treatment we also observed a specific speckled enlarged pattern coupled with an increase in the phosphorylation level for the SR classical proteins, known targets of SR protein kinase 2. These findings supported a functional link between the nuclear translocation and the activity of this neuronal specific kinase. In the second line of our research (presented in the Chapter 3) we performed experiments assessing the function of the mammalian 3’ end processing factor CFIm68 in the mRNA export, thus confirming its action as an adaptor for TAP/NXF1 mRNA export receptor. In particular I helped to demonstrate that the tethering of CFIm68 promoted mRNA export by designing and performing an RNA FISH assay. I used a RNA-biotinylated probe that detected the intracellular localisation of an mRNA reporter construct co-transfected with the CFIm68 protein or control proteins. Therefore we observed an increase of the probe fluorescent cytoplasmic signal only in the presence of the overexpressed CFIm68 but not with other control proteins, observation confirmed by further Real Time PCR data. In the third line of our research (presented in the Chapter 4) we reported that CFIm68 was also involved in the 3’ end cleavage of mammalian histone transcripts (not polyadenylated) by interacting with the LSM11 U7 snRNP component both in vitro and in vivo thus increasing the efficiency of the 3’ end processing in vivo. In this context I performed the Bimolecular Fluorescence Complementation (BiFC) analysis. I co-transfected the CFIm68 and the LSM11 proteins (or its MPL loss-of-function mutant) fused respectively with the C-terminus and the N-terminus of a Venus-Yellow Fluorescent Protein. Thus I detected a nuclear fluorescent complementation in more than 90% of the cells (or not complementation with the MPL mutant counterpart). This data supported our whole characterized observation concerning the involvement of this mammalian cleavage factor in 3’ histone mRNAs processing.
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Mole, Sarah. "Regulation of splicing related SR proteins during the life cycle of human papillomavirus type 16." Thesis, University of Glasgow, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.438066.

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Lopez, Mejia Isabel Cristina. "Alternative splicing of LMNA gene : lessons from a new mouse model of Hutchinson-Gilfort progeria syndrome." Thesis, Montpellier 2, 2011. http://www.theses.fr/2011MON20077.

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Le vieillissement est un processus complexe qui peut être influencé par des facteurs environnementaux et génétiques. Le syndrome progéroïde de Hutchinson-Gilford (HGPS ou progéria) fourni une preuve irréfutable de l'implication de l'épissage dans le processus de vieillissement. La progéria est une maladie due à une mutation hétérozygote silencieuse qui renforce l'utilisation d'un site 5' d'épissage interne dans l'exon 11 de l'ARN pré-messager LMNA, ce qui entraîne la production d'une protéine tronquée appelée «progérine». Le défaut d'épissage du gène LMNA a aussi lieu dans les cellules de personnes âgées, et la correction de ce défaut permet un sauvetage partiel des anomalies qu'il provoque. Ceci fait de l'ARN pré-messager LMNA une cible très attractive pour des thérapies ayant pour but de corriger l'épissage. Mes travaux de thèse ont montré que cette mutation silencieuse active un site d'épissage 5' dans l'exon 11 en changeant la structure de l'ARN. Ce changement de structure facilite l'interaction de la snRNP U1 avec le site d'épissage et permet ainsi sa modulation par les protéines SR SRSF1 et SRSF6. J'ai aussi participé à la caractérisation d'un nouveau modèle murin qui reproduit l'altération d'épissage des patients HGPS au niveau du gène Lmna souris. De façon surprenante, ce modèle récapitule tous les phénotypes du syndrome HGPS. Les souris homozygotes, dans lesquelles la plupart de la lamine A est convertie en progérine, ne vivent pas plus de 5 mois, alors que les souris hétérozygotes vivent autour d'un an et que les contrôles sauvages vivent deux ans. Étonnamment, des souris qui n'expriment ni la lamine A ni la progérine, mais uniquement de la lamine C, vivent plus longtemps que les souris contrôle, suggérant que la lamine A et la progérine, qui sont produites à partir du même transcrit, participent à la régulation de la durée de la vie. De plus, la caractérisation initiale des souris HGPS indique que l'expression de la progérine est délétère pour le tissu adipeux, établissant ainsi un lien inattendu entre l'épuisement du tissu adipeux et le vieillissement accéléré. Ce nouveau modèle murin est actuellement en train d'être utilisé pour des approches de modulation de l'épissage aberrant du gène LMNA avec des oligonucléotides antisense et des petites molécules chimiques
Aging is a complex cellular and organismal process that can be influenced by environmental as well as genetic factors. A striking proof-of-concept that splicing regulation plays an important role in the aging process is provided by Hutchinson-Gilford progeria syndrome (HGPS), a disease caused by a heterozygous silent mutation that enhances the use of an internal 5' splice site in exon 11 of LMNA pre-mRNA and leads to the production of a truncated protein called “progerin”. The LMNA splicing defect also occurs with increased frequency in cells from healthy aged individuals and correction of this defect leads to partial reversal of age-related dysfunction. This makes LMNA pre-mRNA an attractive target for splicing-correction therapies. During my PhD thesis I have characterized the splicing mechanism responsible for progerin production and demonstrated that this process is conserved from mouse to human. I have found that HGPS mutation changes the accessibility of the exon 11 internal 5' splice site, allowing its modulation by U1 snRNP and a subset of SR proteins, namely SRSF6 and SRSF1. I have also participated to the characterization of a new mouse model reproducing human HGPS splicing alteration in the mouse Lmna gene. Strikingly, this model recapitulates all phenotypic manifestations of HGPS. The homozygous mice, where most lamin A is converted to progerin, lived no longer than 5 months, whereas heterozygous mice lived in average one year and wild type littermates up to two years. Unexpectedly, mice expressing neither lamin A nor progerin, but only lamin C, lived longer than wild type littermates mice, suggesting that lamin A and progerin which are produced from the same transcript, control critical steps of lifespan. Furthermore, initial characterization of HGPS mouse model indicated that progerin expression is deleterious for adipose tissue, establishing an unexpected link between adipose tissue depletion and accelerated aging. The new mouse model is currently being used for pharmacological modulation of LMNA aberrant splicing by antisense oligonucleotides and small molecules
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Chandler, Sharon Doc. "Specific recognition in splicing is determined by the modular nature of SR proteins and the pre-mRNA /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 1998. http://wwwlib.umi.com/cr/ucsd/fullcit?p9911847.

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Books on the topic "SR proteins"

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Bubenik, Jodi Lynne. Modulation of HIV-1 Rev function by SR and SR-related proteins. 2005.

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Book chapters on the topic "SR proteins"

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Barta, A., M. Kalyna, and Z. J. Lorković. "Plant SR Proteins and Their Functions." In Current Topics in Microbiology and Immunology. Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-76776-3_5.

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Soret, Johann, Mathieu Gabut, and Jamal Tazi. "SR Proteins as Potential Targets for Therapy." In Alternative Splicing and Disease. Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/978-3-540-34449-0_4.

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Lin, Shengrong, and Xiang-Dong Fu. "SR Proteins and Related Factors in Alternative Splicing." In Advances in Experimental Medicine and Biology. Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-77374-2_7.

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Wegener, Marius, and Michaela Müller-McNicoll. "View from an mRNP: The Roles of SR Proteins in Assembly, Maturation and Turnover." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-31434-7_3.

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Salazar-García, Domingo C., Christina Warinner, Jelmer W. Eerkens, and Amanda G. Henry. "The Potential of Dental Calculus as a Novel Source of Biological Isotopic Data." In Exploring Human Behavior Through Isotope Analysis. Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-32268-6_6.

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AbstractStable isotope analysis has become an essential tool in investigations of ancient migration and paleodietary reconstruction. Because the biogeochemistry of bone collagen and apatite is well known, current methods rely almost exclusively on analyses of bones and teeth; however, dental calculus represents a potentially additional biological source of isotopic data from ancient skeletons. Dental calculus is a mineralized bacterial biofilm that forms on the surfaces of teeth. Sampling dental calculus does not damage the dentition and thus can be used in cases where it is not possible to perform destructive analyses of conventional mineralized tissues. Like bone and dentine, dental calculus contains both inorganic and organic components, allowing measurement of C, N, O, H, and Sr isotopes. Additionally, dental calculus forms as serial, non-remodeling laminar accretions on the tooth surface, opening up the possibility of analyzing discrete time points during the lifetime of an individual. However, as a microbial biofilm and not a human tissue, the biochemistry of dental calculus is complex, containing multiple calcium phosphate mineral phases, organic and inorganic food remains, hundreds of human and bacterial proteins, and diverse biomolecules from thousands of endogenous bacterial taxa. Isotopic investigation of dental calculus is still in its infancy, and many questions remain regarding its formation and processes of diagenesis. This chapter (1) reviews the unique advantages presented by dental calculus as a novel source of biological isotopic data, (2) critically evaluates published isotopic studies of dental calculus, and (3) explores the current challenges of dental calculus stable isotope analysis through a case study of an Ancient Puebloan Basketmaker II population from the American Southwest.
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Zhang, Xin. "A Multistep Mechanism for Assembly of the SRP–SR Complex." In Multistate GTPase Control Co-translational Protein Targeting. Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-7808-0_2.

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Sanford, J. R., D. Longman, and J. F. Cáceres. "Multiple Roles of the SR Protein Family in Splicing Regulation." In Regulation of Alternative Splicing. Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-662-09728-1_2.

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Ikemoto, Mamoru, Dongdong Feng, Hiroyuki Arai, Masafumi Tsujimoto, and Keizo Inoue. "Identification and Characterization of a PDZ Domain-containing Protein That Interacts with the HDL Receptor SR-BI." In Lipoprotein Metabolism and Atherogenesis. Springer Japan, 2000. http://dx.doi.org/10.1007/978-4-431-68424-4_43.

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Hasenfuss, Gerd, Hans Reinecke, Roland Studer, et al. "Altered Force-Frequency Relation and Excitation-Contraction Coupling in the Failing Human Heart: Relevance of SR-Ca2+-ATPase Protein Levels." In Diastolic Relaxation of the Heart. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2594-3_12.

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Tanabe, Noriaki, Ayako Kimura, Kazuya Yoshimura, and Shigeru Shigeoka. "Identification of Interacting Factors with a High-Light Responsible SR Protein, atSR45a, Involved in the Regulation of Alternative Splicing in Arabidopsis." In Photosynthesis. Energy from the Sun. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6709-9_290.

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Conference papers on the topic "SR proteins"

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Ralić, Vanja, Maja Nešić, Anamarija Abu el Rub, et al. "SR FTIR spectroscopy investigation of Pd@S-CD nanocomposite system effects on biomolecules in cervical carcinoma cells." In 2nd International Conference on Chemo and Bioinformatics. Institute for Information Technologies, University of Kragujevac, 2023. http://dx.doi.org/10.46793/iccbi23.467r.

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Nanocomposite system formulated from surface-modified S-doped carbon dot (S-CD) nanoparticle with a potential metallodrug, palladium(II) complex, dichloro(1,2-diaminocyclohexane)palladium(II), [Pd(dach)Cl2] (Pd@S-CD), was investigated as a model system for the treatment of cervical carcinoma (HeLa) cells. To examine the intracellular biochemical effects induced by the Pd@S-CD, we used Synchrotron Radiation-based Fourier-transform infrared spectroscopy (SR FTIR). SR FTIR spectroscopy was employed to investigate the alterations in cellular components’ biochemical composition and secondary structure upon exposure to Pd@S-CD. Spectral analysis, complemented by statistical techniques, revealed changes in biomolecules, lipids, proteins, nucleic acids, and carbohydrates caused by the treatment with Pd@CDs. These results and the increased cytotoxicity of the system demonstrate its high anti-cervical cancer therapeutic potential.
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Rymell, L., M. Berglund, and H. M. Hertz. "Debris-free laser-plasma source for x-ray microscopy." In The European Conference on Lasers and Electro-Optics. Optica Publishing Group, 1996. http://dx.doi.org/10.1364/cleo_europe.1996.cfa6.

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X-ray microscopy allows high-resolution imaging of biological samples in their natural aqueous environment without staining, sectioning or fixation. In particular attention has been focused to the “water window”, i.e., the wavelength region between the oxygen K-edge at λ = 2.3 nm and the carbon K-edge at λ = 4.4 nm, where different absorption coefficients for water and proteins create a natural contrast. Current, operational x-ray microscopes normally utilise zone-plate optics in combination with synchrotron sources. However, these sources suffer from drawbacks such as high cost, limited accessibility for biological researchers and relatively long exposure times. We have developed a compact high-brightness x-ray source based on a laser-produced plasma from a liquid droplet target [1]. A 10 Hz, 70 mJ, 120 ps laser is focused onto ~15 μm droplets generated from a capillary nozzle. By choosing different target liquids spectrally tailored emission can be obtained. For x-ray microscopy we use ammonium hydroxide droplets which generates nitrogen line-emission in the water window [2]. The spectrum over this region is shown in Fig. 1. The emission has been filtered through 600 nm of titanium in order to achieve quasimonochromacy. By using only N VI radiation at λ = 2.88 nm chromatic aberrations in zone plates are efficiently eliminated. Furthermore, λ/Δλ has been estimated to >440, which makes high-resolution imaging possible. Depending on the temporal laser parameters we obtain plasmas from a diameter of ~10 μm with unfiltered single-line flux of 3x1011 photons/(sr pulse) up to a diameter of ~35 μm with 3×1012 photons/(sr pulse) [3]. A major advantage using this new droplet target is the elimination of debris from the laser-plasma. Measurements have proven that the debris emission from the plasma based on ammonium hydroxide is more than 5 orders of magnitude less than from any other conventional low-debris target [4].
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de Serres, M., H. M. Reisner, D. Monroe, and H. Roberts. "A MONOCLONAL ANTIBODY WHOSE BINDING IS INHIBITED BY DIVALENT CATIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644075.

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Factor IX (FIX), a vitamin K dependent coagulation protein, is functionally deficient or absent in patients with hemophilia B. Binding of Ca++ by the gammacarboxyglutamic acid residues (Gla) of FIX is necessary for coagulant activity. Antibodies havebeendes-cribed which selectively bind to FIX in the presence of Ca++ and appear to interact with Ca-H- stabilized epitopes of FIX. One IgM, Kappa murine monoclonal antibody (Mab), 129-1, has been found to react preferentially with FIX in the absence of Ca-H- or with FIX having a reduction in gammacarboxylation. 129-1 was characterized by direct binding ELISA assays, the standard assay buffer (.02M Tris - .15M NaCL pH 7.5) was supplemented with Ca-H- or ED TA to final concentrations to 5mM and lOmM respectively. In the presence of Ca-H-, titers ranged from 10 to 100 as compared to 100 K to 500 K in the presence of EDTA. Control Mab's, FIX-30 and 2D521 showed no such effect. Maximum inhibition occurred ≥2.5 mM Ca-H- concentration. Mg++, Sr-H- and Mn-H- were tested with similar results. Chemically degammacarboxylated FIXa was compared to FIX and FIXa controls in the presence of Ca-H- or EDTA, to determine the importance of Gla residues. In the presence of EDTA, Mab 129-1 had essentially equal reactivity with all these proteins (titers 100 K). In the presence of Ca-H-, binding to FIX and FIXa was inhibited (500 and 1 K respectively). However, the binding to Gla modified FIXa in the presence of Ca-H- was only slightly reduced (10 K), suggesting the importance of Gla residues in the Ca-H- mediated inhibition. FIX was purified from concentrate, coumadinized plasma and culture supernatant (produced in the absence of vitamin K) from the cell line PMN45 using HPLC affinity chromatography with Mab 2D521. Mab 129-1 binding to FIX immunopurified from concentrate and a control biochemically purified FIX protein preparation was significantly higher in the presence of EDTA (titers 500 and 5 K) than in Ca-H- (titers 10 and 10). FIX purified from coumadinized plasma or PMN45 cells showed equal low reactivity with 129-1 in the presence or absence of Ca-H- (titer 10 in all cases). FIX-30 and 2D521 controls showed no such reduction in binding. Therefore, Gla residues may play a role in the binding of 129-1 to FIX.
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Vladu, Alina, Emilia Visileanu, Alina Popescu, and Roxana Rodica Constantinescu. "Antimicrobial treatments of undergarments designed for the combat-protective clothing of soldiers." In AHFE 2023 Hawaii Edition. AHFE International, 2023. http://dx.doi.org/10.54941/ahfe1004210.

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Military forces around the world must be equipped with combat-protective clothing made from the best technical textiles available that must provide sufficient protection, increased comfort, and even antimicrobial protection, especially for underwear pieces. Antibacterial treatments for textile materials include the use of various substances such as chitosan, silver, collagen and so on. Chitosan is a polysaccharide that promotes changes in the permeability properties of the membrane wall causing internal osmotic imbalances and consequently inhibits the growth of microorganisms. Silver can also damage the bacterial RNA and DNA, eventually leading to the bacteria`s death. Moreover, collagen, a fibrous natural protein, has an intrinsic ability to fight infection and contributes to keeping the infection site sterile.This paper focuses on the functionalization of four variants of textile materials with different compositions to increase their antibacterial properties. The variants were treated through two different technologies: exhaustion (30 min at 40°C, 500 rpm) and padding (3 consecutive passes). V1-V4 were functionalized with colloidal silver and V1-V3 with a mixture of collagen hydrolysate and colloidal silver through exhaustion. Variants V1-V3 were also treated through the padding technique using 0.5% chitosan, 1% collagen hydrolysate and a mixture of chitosan and colloidal silver. Untreated textile variants were evaluated regarding their physical-mechanical characteristics. Moreover, the functionalized variants were characterised according to their pH, loading degree with active substances (%), wettability by drop test and contact angle methods, thermal resistance (m2K/W) and vapour resistance (m2Pa/W) according to ISO 11092. Treated textile samples were also investigated relating to their antimicrobial resistance using two methods according to ISO 20743/2013 and SR EN ISO 20645/2005. The evaluation of antibacterial resistance using the standards SR EN ISO 20645/2005 and SR EN ISO 20645/2005 demonstrated the effectiveness of treatments with active substances for approx. 95% of the tested variants.
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Ko, Mei Chuan, Huiping Ding, Norikazu Kiguchi, Dehui Zhang, and Yanan Zhang. "Effects of a highly G Protein-Biased Mu Opioid Receptor Agonist, SR-17018, in Non-human Primates." In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.203910.

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Lin, E. E. "Cluster mechanism of stochastic kinetics of mutation formation protein nanoparticles and mesoobjects." In Наука России: Цели и задачи. LJournal, 2019. http://dx.doi.org/10.18411/sr-10-04-2019-68.

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Liu, Yuying, Adnan Al-Ayoubi, Hui Zheng, Jennifer Bethard, and Scott T. Eblen. "Abstract 3077: The SR protein kinase Clk1 phosphorylates SPF45 and regulates its localization, degradation and alternative splicing activity." 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.am2011-3077.

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Gryzunov, V. V., S. I. Klimshin, A. M. Levi, and A. A. Varlahova. "Physiological sleep as a moderator of elimination of intracellular abnormal protein inducers of neurodegeneration." In Наука России: Цели и задачи. LJournal, 2019. http://dx.doi.org/10.18411/sr-10-04-2019-57.

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Yang, Yi, Jianhua Zhang, Li Zhang, et al. "Phosphorylated Physarum Polycephalum 14-3-3 Modulates the Distribution of the P. Polycephalum SR-like Protein through the Arginine/serine-rich Domain." In ICBET '21: 2021 11th International Conference on Biomedical Engineering and Technology. ACM, 2021. http://dx.doi.org/10.1145/3460238.3460261.

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Craig, Grant, Dan Bevan, Jenny Roberts, et al. "Evolution of in-situ Rb/Sr by LA-MC-ICP-MS/MS: from Proteus to Neoma MS/MS." In Goldschmidt2022. European Association of Geochemistry, 2022. http://dx.doi.org/10.46427/gold2022.10921.

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Reports on the topic "SR proteins"

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Reddy, A. S. N. Functional analysis of U1-70K interacting SR proteins in pre-mRNA splicing in Arabidopsis. Office of Scientific and Technical Information (OSTI), 2008. http://dx.doi.org/10.2172/941683.

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