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Relevant bibliographies by topics / Argonaute Proteins

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Academic literature on the topic 'Argonaute Proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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Journal articles on the topic "Argonaute Proteins"

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Mirzaei, Khaled, Bahman Bahramnejad, Mohammad Hasan Shamsifard, and Wahid Zamani. "In SilicoIdentification, Phylogenetic and Bioinformatic Analysis of Argonaute Genes in Plants." International Journal of Genomics 2014 (2014): 1–17. http://dx.doi.org/10.1155/2014/967461.

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Argonaute protein family is the key players in pathways of gene silencing and small regulatory RNAs in different organisms. Argonaute proteins can bind small noncoding RNAs and control protein synthesis, affect messenger RNA stability, and even participate in the production of new forms of small RNAs. The aim of this study was to characterize and perform bioinformatic analysis of Argonaute proteins in 32 plant species that their genome was sequenced. A total of 437 Argonaute genes were identified and were analyzed based on lengths, gene structure, and protein structure. Results showed that Argonaute proteins were highly conserved across plant kingdom. Phylogenic analysis divided plant Argonautes into three classes. Argonaute proteins have three conserved domains PAZ, MID and PIWI. In addition to three conserved domains namely, PAZ, MID, and PIWI, we identified few more domains in AGO of some plant species. Expression profile analysis of Argonaute proteins showed that expression of these genes varies in most of tissues, which means that these proteins are involved in regulation of most pathways of the plant system. Numbers of alternative transcripts of Argonaute genes were highly variable among the plants. A thorough analysis of large number of putative Argonaute genes revealed several interesting aspects associated with this protein and brought novel information with promising usefulness for both basic and biotechnological applications.

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Kaya, Emine, Kevin W. Doxzen, Kilian R. Knoll, Ross C. Wilson, Steven C. Strutt, Philip J. Kranzusch, and Jennifer A. Doudna. "A bacterial Argonaute with noncanonical guide RNA specificity." Proceedings of the National Academy of Sciences 113, no. 15 (March 30, 2016): 4057–62. http://dx.doi.org/10.1073/pnas.1524385113.

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Eukaryotic Argonaute proteins induce gene silencing by small RNA-guided recognition and cleavage of mRNA targets. Although structural similarities between human and prokaryotic Argonautes are consistent with shared mechanistic properties, sequence and structure-based alignments suggested that Argonautes encoded within CRISPR-cas [clustered regularly interspaced short palindromic repeats (CRISPR)-associated] bacterial immunity operons have divergent activities. We show here that the CRISPR-associated Marinitoga piezophila Argonaute (MpAgo) protein cleaves single-stranded target sequences using 5′-hydroxylated guide RNAs rather than the 5′-phosphorylated guides used by all known Argonautes. The 2.0-Å resolution crystal structure of an MpAgo–RNA complex reveals a guide strand binding site comprising residues that block 5′ phosphate interactions. Using structure-based sequence alignment, we were able to identify other putative MpAgo-like proteins, all of which are encoded within CRISPR-cas loci. Taken together, our data suggest the evolution of an Argonaute subclass with noncanonical specificity for a 5′-hydroxylated guide.

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Cenik, Elif Sarinay, and Phillip D. Zamore. "Argonaute proteins." Current Biology 21, no. 12 (June 2011): R446—R449. http://dx.doi.org/10.1016/j.cub.2011.05.020.

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Pfaff, Janina, and Gunter Meister. "Argonaute and GW182 proteins: an effective alliance in gene silencing." Biochemical Society Transactions 41, no. 4 (July 18, 2013): 855–60. http://dx.doi.org/10.1042/bst20130047.

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Argonaute proteins interact with small RNAs and facilitate small RNA-guided gene-silencing processes. Small RNAs guide Argonaute proteins to distinct target sites on mRNAs where Argonaute proteins interact with members of the GW182 protein family (also known as GW proteins). In subsequent steps, GW182 proteins mediate the downstream steps of gene silencing. The present mini-review summarizes and discusses our current knowledge of the molecular basis of Argonaute–GW182 protein interactions.

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Pare, Justin M., Nasser Tahbaz, Joaquín López-Orozco, Paul LaPointe, Paul Lasko, and Tom C. Hobman. "Hsp90 Regulates the Function of Argonaute 2 and Its Recruitment to Stress Granules and P-Bodies." Molecular Biology of the Cell 20, no. 14 (July 15, 2009): 3273–84. http://dx.doi.org/10.1091/mbc.e09-01-0082.

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Argonaute proteins are effectors of RNA interference that function in the context of cytoplasmic ribonucleoprotein complexes to regulate gene expression. Processing bodies (PBs) and stress granules (SGs) are the two main types of ribonucleoprotein complexes with which Argonautes are associated. Targeting of Argonautes to these structures seems to be regulated by different factors. In the present study, we show that heat-shock protein (Hsp) 90 activity is required for efficient targeting of hAgo2 to PBs and SGs. Furthermore, pharmacological inhibition of Hsp90 was associated with reduced microRNA- and short interfering RNA-dependent gene silencing. Neither Dicer nor its cofactor TAR RNA binding protein (TRBP) associates with PBs or SGs, but interestingly, protein activator of the double-stranded RNA-activated protein kinase (PACT), another Dicer cofactor, is recruited to SGs. Formation of PBs and recruitment of hAgo2 to SGs were not dependent upon PACT (or TRBP) expression. Together, our data suggest that Hsp90 is a critical modulator of Argonaute function. Moreover, we propose that Ago2 and PACT form a complex that functions at the level of SGs.

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Monti, Manuela. "Argonaute proteins - Methods and protocols." European Journal of Histochemistry 56, no. 1 (March 13, 2012): 1. http://dx.doi.org/10.4081/ejh.2012.br1.

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Ender, C., and G. Meister. "Argonaute proteins at a glance." Journal of Cell Science 123, no. 11 (May 19, 2010): 1819–23. http://dx.doi.org/10.1242/jcs.055210.

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Park, Mi Seul, GeunYoung Sim, Audrey C. Kehling, and Kotaro Nakanishi. "Human Argonaute2 and Argonaute3 are catalytically activated by different lengths of guide RNA." Proceedings of the National Academy of Sciences 117, no. 46 (October 29, 2020): 28576–78. http://dx.doi.org/10.1073/pnas.2015026117.

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RNA interfering is a eukaryote-specific gene silencing by 20∼23-nucleotide (nt) microRNAs and small interfering RNAs that recruit Argonaute proteins to complementary RNAs for degradation. In humans, Argonaute2 (AGO2) has been known as the only slicer while Argonaute3 (AGO3) barely cleaves RNAs. Therefore, the intrinsic slicing activity of AGO3 remains controversial and a long-standing question. Here, we report 14-nt 3′ end-shortened variants of let-7a, miR-27a, and specific miR-17–92 families that make AGO3 an extremely competent slicer, increasing target cleavage up to ∼82-fold in some instances. These RNAs, named cleavage-inducing tiny guide RNAs (cityRNAs), conversely lower the activity of AGO2, demonstrating that AGO2 and AGO3 have different optimum guide lengths for target cleavage. Our study sheds light on the role of tiny guide RNAs.

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Felice, Kristin M., David W. Salzman, Jonathan Shubert-Coleman, Kevin P. Jensen, and Henry M. Furneaux. "The 5′ terminal uracil of let-7a is critical for the recruitment of mRNA to Argonaute2." Biochemical Journal 422, no. 2 (August 13, 2009): 329–41. http://dx.doi.org/10.1042/bj20090534.

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Small RNAs modulate gene expression by forming a ribonucleoprotein complex with Argonaute proteins and directing them to specific complementary sites in target nucleic acids. However, the interactions required for the recruitment of the target nucleic acid to the ribonucleoprotein complex are poorly understood. In the present manuscript we have investigated this question by using let-7a, Argonaute2 and a fully complementary mRNA target. Importantly, we have found that recombinant Argonaute2 is sufficient to direct let-7a guided cleavage of mRNA. Thus this model system has allowed us to investigate the mechanistic basis of silencing in vitro and in vivo. Current models suggest that Argonaute proteins bind to both the 5′ and 3′ termini of the guide RNA. We have found that the termini of the let-7a microRNA are indeed critical, since circular let-7a does not support mRNA cleavage. However, the 5′ end is the key determinant, since its deletion abrogates activity. Surprisingly, we have found that alteration of the 5′ terminal uracil compromises mRNA cleavage. Importantly, we have found that substitution of this base has little effect upon the formation of the binary let-7a–Argonaute2 complex, but inhibits the formation of the ternary let-7a–Argonaute2–mRNA complex. Thus we conclude that the interaction of the 5′ uracil base with Argonaute2 plays a critical and novel role in the recruitment of mRNA.

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Dueck, Anne, and Gunter Meister. "Assembly and function of small RNA – Argonaute protein complexes." Biological Chemistry 395, no. 6 (June 1, 2014): 611–29. http://dx.doi.org/10.1515/hsz-2014-0116.

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Abstract Small RNAs such as microRNAs (miRNAs), short interfering RNAs (siRNAs) or Piwi-interacting RNAs (piRNAs) are important regulators of gene expression in various organisms. Small RNAs bind to a member of the Argonaute protein family and are incorporated into larger structures that mediate diverse gene silencing events. The loading of Argonaute proteins with small RNAs is aided by a number of auxiliary factors as well as ATP hydrolysis. This review will focus on the mechanisms of Argonaute loading in different organisms. Furthermore, we highlight the versatile functions of small RNA-Argonaute protein complexes in organisms from all three kingdoms of life.

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Dissertations / Theses on the topic "Argonaute Proteins"

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Heimstadt, Susanne Barbara. "Functional diversification of Arabidopsis Argonaute proteins." Thesis, University of East Anglia, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.492957.

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Yigit, Erbay. "The Argonaute Family of Genes in Caenorhabditis Elegans: a Dissertation." eScholarship@UMMS, 2007. https://escholarship.umassmed.edu/gsbs_diss/328.

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Members of the Argonaute family of proteins, which interact with small RNAs, are the key players of RNAi and other related pathways. The C. elegans genome encodes 27 members of the Argonaute family. During this thesis research, we sought to understand the functions of the members of this gene family in C. elegans. Among the Argonaute family members, rde-1 and alg-1/2have previously been shown to be essential for RNAi and development, respectively. In this work, we wanted to assign functions to the remaining members of this large family of proteins. Here, we describe the phenotype of 31 deletion alleles representing all of the previously uncharacterized Argonaute members. In addition to rde-1, our analysis revealed that two other Argonaute members csr-1 and prg-1 are also essential for development. csr-1 is partially required for RNAi, and essential for proper chromosome segregation. prg-1, a member of PIWI subfamily of Argonaute genes, exhibits reduced brood size and temperature-sensitive sterile phenotype, implicating that it is required for germline maintenance. Additionally, we showed that RDE-1 interacts with trigger-derived sense and antisense siRNAs (primary siRNAs) to initiate RNAi, while several other Argonaute proteins, SAGO-1, SAGO-2, and perhaps others, functioning redundantly, interact with amplified siRNAs (secondary siRNAs) to mediate downstream silencing. Moreover, our analysis uncovered that another member of Argonaute gene family, ergo-1, is essential for the endogenous RNAi pathway. Furthermore, we built an eight-fold Argonaute mutant, MAGO8, and analyzed its developmental phenotype and sensitivity to RNAi. Our analysis revealed that the genes deleted in the MAGO8 mutant function redundantly with each other, and are required for RNAi and the maintenance of the stem cell totipotency.

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Åström, Miranda. "Search for the Argonaute protein that governs miRNA regulation in Dictyostelium discoideum." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2021. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-432967.

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MicroRNAs are small non-coding RNAs that regulate gene expression through RNA interference. These small RNAs enact gene silencing by forming a RNA-inducing silencing complex together with the effector protein Argonaute. The function of the Argonautes in the social amoeba Dictyostelium discoideum is not yet fully understood. In this study, we look closer at Argonaute B by investigating if it is possible to extract the protein from the cells by the addition of a polypeptide protein tag called 3xFlag. At the same time, we also look into if Argonaute B is important for cell growth. Sequences of the 3xFlag tag with or without the Argonaute B gene (agnB) attached had previously been cloned into a vector and transformed into Dictyostelium discoideum cell. The 3xFlag::agnB sequence was confirmed in wild type and agnB knock-out strains through polymerase chain reaction. We then verified the expression of the fusion protein in the cells by western blot. The cell growth was measured by how the number of cells changed over time. The experiment suggested that Argonaute B is important for growth. Our result show that the construct 3xFlag::agnB sequenced had correctly been transformed into the strains and is highly expressed under tested conditions. We could also see that Argonaute B is an important factor in cell growth.

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Seth, Meetu. "Functions of Argonaute Proteins in Self Versus Non-Self Recognition in the C. elegans Germline: A Dissertation." eScholarship@UMMS, 2008. http://escholarship.umassmed.edu/gsbs_diss/874.

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Organisms employ sophisticated mechanisms to silence foreign nucleic acid, such as viruses and transposons. Evidence exists for pathways that sense copy number, unpaired DNA, or aberrant RNA (e.g., dsRNA), but the mechanisms that distinguish “self” from “non-self” are not well understood. Our studies on transgene silencing in C. elegans have uncovered an RNA surveillance system in which the PIWI protein, PRG-1, uses a vast repertoire of piRNAs to recognize foreign transcripts and to initiate epigenetic silencing. Partial base pairing by piRNAs is sufficient to guide PRG-1 targeting. PRG-1 in turn recruits RdRP to synthesize perfectly matching antisense siRNAs (22G-RNAs) that are loaded onto worm-specific Argonaute (WAGO) proteins. WAGOs collaborate with chromatin factors to maintain epigenetic silencing (RNAe). Since mismatches are allowed during piRNA targeting, piRNAs could—in theory— target any transcript expressed in the germline, but germline genes are not subject to silencing by RNAe. Moreover, some foreign sequences are expressed and appear to be adopted as “self.” How are “self” transcripts distinguished from foreign transcripts? We have found that another Argonaute, CSR-1, and its siRNAs—also synthesized by RdRP—protect endogenous genes from silencing by RNAe. We refer to this pathway as RNA-mediated gene activation (RNAa). Reducing CSR-1 or PRG-1 or increasing piRNA targeting can shift the balance towards expression or silencing, indicating that PRG-1 and CSR-1 compete for control over their targets. Thus worms have evolved a remarkable nucleic acids immunity mechanism in which opposing Argonaute pathways generate and maintain epigenetic memories of self and non-self nucleotide sequences.

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Seth, Meetu. "Functions of Argonaute Proteins in Self Versus Non-Self Recognition in the C. elegans Germline: A Dissertation." eScholarship@UMMS, 2016. https://escholarship.umassmed.edu/gsbs_diss/874.

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Organisms employ sophisticated mechanisms to silence foreign nucleic acid, such as viruses and transposons. Evidence exists for pathways that sense copy number, unpaired DNA, or aberrant RNA (e.g., dsRNA), but the mechanisms that distinguish “self” from “non-self” are not well understood. Our studies on transgene silencing in C. elegans have uncovered an RNA surveillance system in which the PIWI protein, PRG-1, uses a vast repertoire of piRNAs to recognize foreign transcripts and to initiate epigenetic silencing. Partial base pairing by piRNAs is sufficient to guide PRG-1 targeting. PRG-1 in turn recruits RdRP to synthesize perfectly matching antisense siRNAs (22G-RNAs) that are loaded onto worm-specific Argonaute (WAGO) proteins. WAGOs collaborate with chromatin factors to maintain epigenetic silencing (RNAe). Since mismatches are allowed during piRNA targeting, piRNAs could—in theory— target any transcript expressed in the germline, but germline genes are not subject to silencing by RNAe. Moreover, some foreign sequences are expressed and appear to be adopted as “self.” How are “self” transcripts distinguished from foreign transcripts? We have found that another Argonaute, CSR-1, and its siRNAs—also synthesized by RdRP—protect endogenous genes from silencing by RNAe. We refer to this pathway as RNA-mediated gene activation (RNAa). Reducing CSR-1 or PRG-1 or increasing piRNA targeting can shift the balance towards expression or silencing, indicating that PRG-1 and CSR-1 compete for control over their targets. Thus worms have evolved a remarkable nucleic acids immunity mechanism in which opposing Argonaute pathways generate and maintain epigenetic memories of self and non-self nucleotide sequences.

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Salomon, William E. "Single-Molecule Imaging Reveals that Argonaute Re-Shapes the Properties of its Nucleic Acid Guides: A Dissertation." eScholarship@UMMS, 2015. http://escholarship.umassmed.edu/gsbs_diss/804.

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Small RNA silencing pathways regulate development, viral defense, and genomic integrity in all kingdoms of life. An Argonaute (Ago) protein, guided by a tightly bound, small RNA or DNA, lies at the core of these pathways. Argonaute uses its small RNA or DNA to find its target sequences, which it either cleaves or stably binds, acting as a binding scaffold for other proteins. We used Co-localization Single-Molecule Spectroscopy (CoSMoS) to analyze target binding and cleavage by Ago and its guide. We find that both eukaryotic and prokaryotic Argonaute proteins re-shape the fundamental properties of RNA:RNA, RNA:DNA, and DNA:DNA hybridization: a small RNA or DNA bound to Argonaute as a guide no longer follows the well-established rules by which oligonucleotides find, bind, and dissociate from complementary nucleic acid sequences. Counter to the rules of nucleic acid hybridization alone, we find that mouse AGO2 and its guide bind to microRNA targets 17,000 times tighter than the guide without Argonaute. Moreover, AGO2 can distinguish between microRNA-like targets that make seven base pairs with the guide and the products of cleavage, which bind via nine base pairs: AGO2 leaves the cleavage products faster, even though they pair more extensively. This thesis presents a detailed kinetic interrogation of microRNA and RNA interference pathways. We discovered sub-domains within the previously defined functional domains created by Argonaute and its bound DNA or RNA guide. These sub-domains have features that no longer conform to the well-established properties of unbound oligonucleotides. It is by re-writing the rules for nucleic acid hybridization that Argonautes allow oligonucleotides to serve as specificity determinants with thermodynamic and kinetic properties more typical of RNA-binding proteins than that of RNA or DNA. Taken altogether, these studies further our understanding about the biology of small RNA silencing pathways and may serve to guide future work related to all RNA-guided endonucleases.

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Urban, Marc [Verfasser], and Thomas [Akademischer Betreuer] Dresselhaus. "Gametogenesis-related small RNAs and Argonaute Proteins in Arabidopsis thaliana / Marc Urban ; Betreuer: Thomas Dresselhaus." Regensburg : Universitätsbibliothek Regensburg, 2016. http://d-nb.info/1136471480/34.

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Zeitler, Daniela [Verfasser], and Gunter [Akademischer Betreuer] Meister. "Regulation of human Argonaute proteins and its implications in disease / Daniela Zeitler ; Betreuer: Gunter Meister." Regensburg : Universitätsbibliothek Regensburg, 2020. http://d-nb.info/1210701936/34.

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Urban, Marc Verfasser], and Thomas [Akademischer Betreuer] [Dresselhaus. "Gametogenesis-related small RNAs and Argonaute Proteins in Arabidopsis thaliana / Marc Urban ; Betreuer: Thomas Dresselhaus." Regensburg : Universitätsbibliothek Regensburg, 2016. http://d-nb.info/1136471480/34.

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Jacobsen, Annette. "Lactobacilli Suppress Gene Expression of Key Proteins Involved in miRNA Biogenesis in HT29 and VK2/E6E7 Cells." Thesis, Örebro universitet, Institutionen för naturvetenskap och teknik, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:oru:diva-32633.

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It has previously been demonstrated that lactic acid bacteria are able to influence the innate immune response of host cells. One way this can be achieved is through modulation of inflammatory cascades initiated by pattern recognition elements such as toll-like receptors. Micro RNA can also have an effect on innate immunity, and has been shown to have an influence in regulation of these pathways in immune responsive cells. However, it is yet to be determined if the interaction between lactic acid bacteria and host cells involves regulation of the RNA interference machinery involved in micro RNA biogenesis. Three of the key proteins responsible for miRNA production and activation are Argonaute 2, Dicer and Drosha. Together, these are responsible for the processing and activation of miRNA to enable post-transcriptional gene regulation. In this study we have used quantitative PCR to evaluate changes in gene expression of these enzymes in HT29 and VK2/E6E7 mucosal epithelial cells after treatment with Lactobacillus and uropathogenic bacteria. We have found that bacterial treatment downregulates gene expression of elements responsible for miRNA biogenesis, and our results showed different responses dependent on the cell line. In addition to this we have also determined stable reference genes for use in further studies involving this model. Our findings indicate that modulation of the RNAi machinery might be an important element of immune regulation by bacterial colonists.

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Books on the topic "Argonaute Proteins"

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Hobman, Tom C., and Thomas F. Duchaine, eds. Argonaute Proteins. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-046-1.

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Okamura, Katsutomo, and Kotaro Nakanishi, eds. Argonaute Proteins. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7339-2.

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Carbonell, Alberto, ed. Plant Argonaute Proteins. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7165-7.

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Argonaute proteins: Methods and protocols. New York: Humana Press/Springer, 2011.

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Book chapters on the topic "Argonaute Proteins"

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Li, Jing, Nima Najand, Wendy Long, and Andrew Simmonds. "Imaging the Cellular Dynamics of Drosophila Argonaute Proteins." In Methods in Molecular Biology, 143–59. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-046-1_10.

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Miyoshi, Keita, Hiroshi Uejima, Tomoko Nagami-Okada, Haruhiko Siomi, and Mikiko C. Siomi. "In vitro RNA Cleavage Assay for Argonaute-Family Proteins." In Methods in Molecular Biology™, 29–43. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-191-8_3.

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Pare, Justin M., Joaquin Lopez-Orozco, and Tom C. Hobman. "Live Cell Imaging of Argonaute Proteins in Mammalian Cells." In Methods in Molecular Biology, 161–72. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-046-1_11.

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León-Martínez, Gloria, Edgar Demesa-Arévalo, and Jean-Philippe Vielle-Calzada. "Immunolocalization to Study ARGONAUTE Proteins in Developing Ovules of the Brassicaceae." In Methods in Molecular Biology, 335–45. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9042-9_24.

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Su, Hong, and Xiaozhong Wang. "Generation of an Inducible Mouse ES Cell Lines Deficient for Argonaute Proteins." In Methods in Molecular Biology, 295–313. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-046-1_19.

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Phan, Hong-Duc, Junan Li, Ming Poi, and Kotaro Nakanishi. "Quantification of miRNAs Co-Immunoprecipitated with Argonaute Proteins Using SYBR Green-Based qRT-PCR." In Methods in Molecular Biology, 29–40. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7339-2_2.

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Leung, Anthony K. L., and Phillip A. Sharp. "Quantifying Argonaute Proteins In and Out of GW/P-Bodies: Implications in microRNA Activities." In Advances in Experimental Medicine and Biology, 165–82. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5107-5_10.

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Eckhardt, Stephanie, Emilia Szostak, Zhaolin Yang, and Ramesh Pillai. "Artificial Tethering of Argonaute Proteins for Studying their Role in Translational Repression of Target mRNAs." In Methods in Molecular Biology, 191–206. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-046-1_13.

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Mehlhorn, Heinz. "Argonaute Protein Family." In Encyclopedia of Parasitology, 209. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-43978-4_4466.

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Mehlhorn, Heinz. "Argonaute Protein Family." In Encyclopedia of Parasitology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27769-6_4466-1.

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Conference papers on the topic "Argonaute Proteins"

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Yang, Shanshan, Jinjin Long, Heng Chen, and Bifang He. "AGOPredict: A Predictor for Identifying Argonaute Proteins." In 2020 7th International Conference on Information Science and Control Engineering (ICISCE). IEEE, 2020. http://dx.doi.org/10.1109/icisce50968.2020.00048.

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Rabinovich, Einat I., Guoying Yu, Maria Kapetanaki, Frank Schneider, and Naftali Kaminski. "Changes In Expression Of Argonaut Proteins In IPF." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3473.

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Kabos, P., E. Kline, J. Brown, K. Flory, C. Sartorius, J. Hesselberth, and MM Pillai. "Abstract PD01-07: High throughput sequencing following cross-linked immune-precipitation (HITS-CLIP) of Argonaute protein reveals novel miRNA regulatory pathways of Estrogen Receptor in breast cancer." In Abstracts: Thirty-Fifth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 4‐8, 2012; San Antonio, TX. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/0008-5472.sabcs12-pd01-07.

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