Log in

Relevant bibliographies by topics / Argonaute Proteins / Journal articles

To see the other types of publications on this topic, follow the link: Argonaute Proteins.

Journal articles on the topic 'Argonaute Proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Argonaute Proteins.'

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

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

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

5

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

10

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

11

Hall, Traci M. Tanaka. "Structure and Function of Argonaute Proteins." Structure 13, no. 10 (October 2005): 1403–8. http://dx.doi.org/10.1016/j.str.2005.08.005.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Peters, Lasse, and Gunter Meister. "Argonaute Proteins: Mediators of RNA Silencing." Molecular Cell 26, no. 5 (June 2007): 611–23. http://dx.doi.org/10.1016/j.molcel.2007.05.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Swarts, Daan C., Kira Makarova, Yanli Wang, Kotaro Nakanishi, René F. Ketting, Eugene V. Koonin, Dinshaw J. Patel, and John van der Oost. "The evolutionary journey of Argonaute proteins." Nature Structural & Molecular Biology 21, no. 9 (September 2014): 743–53. http://dx.doi.org/10.1038/nsmb.2879.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Meister, Gunter, Markus Landthaler, Lasse Peters, Po Yu Chen, Henning Urlaub, Reinhard Lührmann, and Thomas Tuschl. "Identification of Novel Argonaute-Associated Proteins." Current Biology 15, no. 23 (December 2005): 2149–55. http://dx.doi.org/10.1016/j.cub.2005.10.048.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Winter, Julia, and Sven Diederichs. "Argonaute proteins regulate microRNA stability: Increased microRNA abundance by Argonaute proteins is due to microRNA stabilization." RNA Biology 8, no. 6 (November 2011): 1149–57. http://dx.doi.org/10.4161/rna.8.6.17665.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Flygaard, Rasmus, Rune Kidmose, Maja Nielsen, and Lasse Jenner. "Regulation of the ribosome and protein synthesis by RNAi." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1400. http://dx.doi.org/10.1107/s2053273314085994.

Full text

Abstract:

In many biological processes, e.g. the development of multicellular organisms, a tight regulation of the protein synthesis is a necessity. Among numerous mechanisms for translational control, RNA interference (RNAi) based mechanisms have been shown to regulate the translation of messenger RNA (mRNA) and hence regulate the synthesis of proteins. The key proteins in all RNAi mechanisms are the argonaute proteins. The only catalytically active argonaute protein is denoted argonaute2 (Ago2) in humans. This single chain protein is comprised of four globular domains arranged in a crescent shape tertiary structure [1]. The guide RNA binding specificity lies within the Mid and PAZ domain while the active site resides in the PIWI domain. In 2011 it was reported that the receptor for activated C-kinase (RACK1), an integral protein of the ribosomal 40S subunit, directly binds the microRNA induced silencing complex (miRISC) [2] and thereby contributes to gene repression through RNAi mediated knockdown. This interaction of RACK1 with miRISC was furthermore shown to be a specific interaction between Ago2 and RACK1. Structural investigation of this interaction will be of great interest to elucidate how Ago2 is positioned in relation to ribosome bound mRNA and if this positioning of Ago2 on the ribosome facilitates mRNA binding to the guide RNA bound in Ago2. In our studies we will co-crystallize recombinantly expressed Ago2 with 80S ribosome from S. cerevisiae [3] and solve the structure by x-ray crystallography. Recent project progress will be presented on the conference poster.

APA, Harvard, Vancouver, ISO, and other styles

17

Huang, Vera, and Long-Cheng Li. "Demystifying the nuclear function of Argonaute proteins." RNA Biology 11, no. 1 (January 1, 2014): 18–24. http://dx.doi.org/10.4161/rna.27604.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Rüdel, Sabine, and Gunter Meister. "Phosphorylation of Argonaute proteins: regulating gene regulators." Biochemical Journal 413, no. 3 (July 15, 2008): e7-e9. http://dx.doi.org/10.1042/bj20081244.

Full text

Abstract:

Members of the Ago (Argonaute) protein family are the mediators of small RNA-guided gene-silencing pathways including RNAi (RNA interference), translational regulation by miRNAs (microRNAs) and transcriptional silencing. Recent findings by Zeng et al. in this issue of the Biochemical Journal demonstrate that Ago proteins are post-translationally modified by phosphorylation of Ser387. Mutating Ser387 to alanine leads to reduced localization of human Ago2 to cytoplasmic P-bodies (processing bodies), cellular sites where RNA turnover and, at least in part, miRNA-guided gene regulation occurs. Zeng et al. further show that a member of the MAPK (mitogen-activated protein kinase) signalling pathway phosphorylates Ago2 at Ser387, suggesting that Ago2-mediated gene silencing might be linked to distinct signalling pathways.

APA, Harvard, Vancouver, ISO, and other styles

19

Meister, Gunter. "Argonaute proteins: functional insights and emerging roles." Nature Reviews Genetics 14, no. 7 (June 4, 2013): 447–59. http://dx.doi.org/10.1038/nrg3462.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Djuranovic, Sergej, Michelle Kim Zinchenko, Junho K. Hur, Ali Nahvi, Julie L. Brunelle, Elizabeth J. Rogers, and Rachel Green. "Allosteric regulation of Argonaute proteins by miRNAs." Nature Structural & Molecular Biology 17, no. 2 (January 10, 2010): 144–50. http://dx.doi.org/10.1038/nsmb.1736.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Hutvagner, Gyorgy, and Martin J. Simard. "Argonaute proteins: key players in RNA silencing." Nature Reviews Molecular Cell Biology 9, no. 1 (January 2008): 22–32. http://dx.doi.org/10.1038/nrm2321.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Mallory, Allison, and Hervé Vaucheret. "Form, Function, and Regulation of ARGONAUTE Proteins." Plant Cell 22, no. 12 (December 2010): 3879–89. http://dx.doi.org/10.1105/tpc.110.080671.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Hegge, Jorrit W., Daan C. Swarts, and John van der Oost. "Prokaryotic Argonaute proteins: novel genome-editing tools?" Nature Reviews Microbiology 16, no. 1 (July 24, 2017): 5–11. http://dx.doi.org/10.1038/nrmicro.2017.73.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Jiang, Lixu, Min Yu, Yuwei Zhou, Zhongjie Tang, Ning Li, Juanjuan Kang, Bifang He, and Jian Huang. "AGONOTES: A Robot Annotator for Argonaute Proteins." Interdisciplinary Sciences: Computational Life Sciences 12, no. 1 (November 18, 2019): 109–16. http://dx.doi.org/10.1007/s12539-019-00349-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Nowak, Iwona, and Aishe A. Sarshad. "Argonaute Proteins Take Center Stage in Cancers." Cancers 13, no. 4 (February 13, 2021): 788. http://dx.doi.org/10.3390/cancers13040788.

Full text

Abstract:

Argonaute proteins (AGOs) play crucial roles in RNA-induced silencing complex (RISC) formation and activity. AGOs loaded with small RNA molecules (miRNA or siRNA) either catalyze endoribonucleolytic cleavage of target RNAs or recruit factors responsible for translational silencing and target destabilization. miRNAs are well characterized and broadly studied in tumorigenesis; nevertheless, the functions of the AGOs in cancers have lagged behind. Here, we discuss the current state of knowledge on the role of AGOs in tumorigenesis, highlighting canonical and non-canonical functions of AGOs in cancer cells, as well as the biomarker potential of AGO expression in different of tumor types. Furthermore, we point to the possible application of the AGOs in development of novel therapeutic approaches.

APA, Harvard, Vancouver, ISO, and other styles

26

Jin, Shujuan, Jian Zhan, and Yaoqi Zhou. "Argonaute proteins: structures and their endonuclease activity." Molecular Biology Reports 48, no. 5 (May 2021): 4837–49. http://dx.doi.org/10.1007/s11033-021-06476-w.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

MacRae, Ian. "Structural basis for post-transcriptional gene silencing by human Argonaute-2." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1395. http://dx.doi.org/10.1107/s2053273314086045.

Full text

Abstract:

Argonaute proteins are a unique class of RNases that degrade substrate RNAs in a sequence-specific manner. Argonaute proteins acquire substrate specificity by binding to a small RNA (21 nucleotide), termed the guide RNA, and use the encoded sequence to locate target message RNAs (mRNAs) through base-pairing complementarity. We have determined crystal structures of human Argonaute-2 (Ago2) bound a guide RNA and a variety of complementary target RNAs. The structures reveal how Ago2 uses discrete regions of the guide to scan for targets and the conformational changes associated with target recognition. Using free phenol as a probe, we also identified a constellation of hydrophobic cavities on the surface of Ago2 that we suggest are involved in the recruitment of additional protein factors to target mRNAs upon recognition by Ago2.

APA, Harvard, Vancouver, ISO, and other styles

28

Hauptmann, Judith, Daniel Schraivogel, Astrid Bruckmann, Sudhir Manickavel, Leonhard Jakob, Norbert Eichner, Janina Pfaff, et al. "Biochemical isolation of Argonaute protein complexes by Ago-APP." Proceedings of the National Academy of Sciences 112, no. 38 (September 8, 2015): 11841–45. http://dx.doi.org/10.1073/pnas.1506116112.

Full text

Abstract:

During microRNA (miRNA)-guided gene silencing, Argonaute (Ago) proteins interact with a member of the TNRC6/GW protein family. Here we used a short GW protein-derived peptide fused to GST and demonstrate that it binds to Ago proteins with high affinity. This allows for the simultaneous isolation of all Ago protein complexes expressed in diverse species to identify associated proteins, small RNAs, or target mRNAs. We refer to our method as “Ago protein Affinity Purification by Peptides“ (Ago-APP). Furthermore, expression of this peptide competes for endogenous TNRC6 proteins, leading to global inhibition of miRNA function in mammalian cells.

APA, Harvard, Vancouver, ISO, and other styles

29

Wang, D., Z. Zhang, E. O'Loughlin, T. Lee, S. Houel, D. O'Carroll, A. Tarakhovsky, N. G. Ahn, and R. Yi. "Quantitative functions of Argonaute proteins in mammalian development." Genes & Development 26, no. 7 (April 1, 2012): 693–704. http://dx.doi.org/10.1101/gad.182758.111.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Zhang, Han, Rui Xia, Blake C. Meyers, and Virginia Walbot. "Evolution, functions, and mysteries of plant ARGONAUTE proteins." Current Opinion in Plant Biology 27 (October 2015): 84–90. http://dx.doi.org/10.1016/j.pbi.2015.06.011.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Ameyar-Zazoua, Maya, Christophe Rachez, Mouloud Souidi, Philippe Robin, Lauriane Fritsch, Robert Young, Nadya Morozova, et al. "Argonaute proteins couple chromatin silencing to alternative splicing." Nature Structural & Molecular Biology 19, no. 10 (September 9, 2012): 998–1004. http://dx.doi.org/10.1038/nsmb.2373.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Dueck, A., C. Ziegler, A. Eichner, E. Berezikov, and G. Meister. "microRNAs associated with the different human Argonaute proteins." Nucleic Acids Research 40, no. 19 (July 25, 2012): 9850–62. http://dx.doi.org/10.1093/nar/gks705.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Wu, Jin'en, Jing Yang, William C. Cho, and Yadong Zheng. "Argonaute proteins: Structural features, functions and emerging roles." Journal of Advanced Research 24 (July 2020): 317–24. http://dx.doi.org/10.1016/j.jare.2020.04.017.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Till, Susanne, Erwan Lejeune, Rolf Thermann, Miriam Bortfeld, Michael Hothorn, Daniel Enderle, Constanze Heinrich, Matthias W. Hentze, and Andreas G. Ladurner. "A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain." Nature Structural & Molecular Biology 14, no. 10 (September 23, 2007): 897–903. http://dx.doi.org/10.1038/nsmb1302.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Boone, Erin C., Hua Xiao, Michael M. Vierling, Logan M. Decker, Victor T. Sy, Rana F. Kennedy, Marilyn A. Bonham, et al. "An NCBP3-Domain Protein Mediates Meiotic Silencing by Unpaired DNA." G3: Genes|Genomes|Genetics 10, no. 6 (April 14, 2020): 1919–27. http://dx.doi.org/10.1534/g3.120.401236.

Full text

Abstract:

In the filamentous fungus Neurospora crassa, genes unpaired during meiosis are silenced by a process known as meiotic silencing by unpaired DNA (MSUD). MSUD utilizes common RNA interference (RNAi) proteins, such as Dicer and Argonaute, to target homologous mRNAs for silencing. Previously, we demonstrated that nuclear cap-binding proteins NCBP1 and NCBP2 are involved in MSUD. We report here that SAD-8, a protein similar to human NCBP3, also mediates silencing. Although SAD-8 is not essential for either vegetative or sexual development, it is required for MSUD. SAD-8 localizes predominantly in the nucleus and interacts with both NCBP1 and NCBP2. Similar to NCBP1 and NCBP2, SAD-8 interacts with a component (Argonaute) of the perinuclear meiotic silencing complex (MSC), further implicating the involvement of cap-binding proteins in silencing.

APA, Harvard, Vancouver, ISO, and other styles

36

Basu, Protip, Sayak Ganguli, Sohini Gupta, and Abhijit Datta. "Exploring Computational Protein Fishing (CPF) to Identify Argonaute Proteins from Sequenced Crop Genomes." International Letters of Natural Sciences 33 (January 2015): 27–36. http://dx.doi.org/10.18052/www.scipress.com/ilns.33.27.

Full text

Abstract:

Plant RNA interference has been a very well studied phenomenon since its discovery. We are well versed with the types of small noncoding RNAs that are prevalent in the plant systems and their pathways of biogenesis and subsequent actions. However, apart from model plant systems such as Arabidopsis and Oryza, very little information is available regarding the other members of the RNA interference machinery; specially Argonaute proteins which acts as the major stabilizing factor for execution of the interference. This work focuses on the exploration of the sequenced crop genomes available on the web using a hybrid approach of computational protein fishing and genome mining. The results indicate that this hybrid approach was successful in the identification of argonaute proteins in the crop genomes under study.

APA, Harvard, Vancouver, ISO, and other styles

37

Niaz, Saife. "The AGO proteins: an overview." Biological Chemistry 399, no. 6 (May 24, 2018): 525–47. http://dx.doi.org/10.1515/hsz-2017-0329.

Full text

Abstract:

AbstractSmall RNAs govern almost every biological process in eukaryotes associating with the Argonaute (AGO) proteins to form the RNA-induced silencing complex (mRISC). AGO proteins constitute the core of RISCs with different members having variety of protein-binding partners and biochemical properties. This review focuses on the AGO subfamily of the AGOs that are ubiquitously expressed and are associated with small RNAs. The structure, function and role of the AGO proteins in the cell is discussed in detail.

APA, Harvard, Vancouver, ISO, and other styles

38

Lewis, Alexandra, Ahmet C. Berkyurek, Andre Greiner, Ahilya N. Sawh, Ajay Vashisht, Stephanie Merrett, Mathieu N. Flamand, et al. "A Family of Argonaute-Interacting Proteins Gates Nuclear RNAi." Molecular Cell 78, no. 5 (June 2020): 862–75. http://dx.doi.org/10.1016/j.molcel.2020.04.007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Rüdel, Sabine, Yanli Wang, René Lenobel, Roman Körner, He-Hsuan Hsiao, Henning Urlaub, Dinshaw Patel, and Gunter Meister. "Phosphorylation of human Argonaute proteins affects small RNA binding." Nucleic Acids Research 39, no. 6 (November 10, 2010): 2330–43. http://dx.doi.org/10.1093/nar/gkq1032.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Mescalchin, A., A. Detzer, U. Weirauch, M. J. Hahnel, C. Engel, and G. Sczakiel. "Antisense tools for functional studies of human Argonaute proteins." RNA 16, no. 12 (October 8, 2010): 2529–36. http://dx.doi.org/10.1261/rna.2204610.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Schürmann, Nina, Leonardo G. Trabuco, Christian Bender, Robert B. Russell, and Dirk Grimm. "Molecular dissection of human Argonaute proteins by DNA shuffling." Nature Structural & Molecular Biology 20, no. 7 (June 9, 2013): 818–26. http://dx.doi.org/10.1038/nsmb.2607.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Batsché, Eric, and Maya Ameyar-Zazoua. "The influence of Argonaute proteins on alternative RNA splicing." Wiley Interdisciplinary Reviews: RNA 6, no. 1 (September 25, 2014): 141–56. http://dx.doi.org/10.1002/wrna.1264.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Kobayashi, Hotaka, and Yukihide Tomari. "RISC assembly: Coordination between small RNAs and Argonaute proteins." Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1859, no. 1 (January 2016): 71–81. http://dx.doi.org/10.1016/j.bbagrm.2015.08.007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Lapinaite, Audrone, Jennifer A. Doudna, and Jamie H. D. Cate. "Programmable RNA recognition using a CRISPR-associated Argonaute." Proceedings of the National Academy of Sciences 115, no. 13 (March 12, 2018): 3368–73. http://dx.doi.org/10.1073/pnas.1717725115.

Full text

Abstract:

Argonaute proteins (Agos) are present in all domains of life. Although the physiological function of eukaryotic Agos in regulating gene expression is well documented, the biological roles of many of their prokaryotic counterparts remain enigmatic. In some bacteria, Agos are associated with CRISPR (clustered regularly interspaced short palindromic repeats) loci and use noncanonical 5′-hydroxylated guide RNAs (gRNAs) for nucleic acid targeting. Here we show that using 5-bromo-2′-deoxyuridine (BrdU) as the 5′ nucleotide of gRNAs stabilizes in vitro reconstituted CRISPR-associated Marinitoga piezophila Argonaute–gRNA complexes (MpAgo RNPs) and significantly improves their specificity and affinity for RNA targets. Using reconstituted MpAgo RNPs with 5′-BrdU-modified gRNAs, we mapped the seed region of the gRNA and identified the nucleotides of the gRNA that play the most significant role in targeting specificity. We also show that these MpAgo RNPs can be programmed to distinguish between substrates that differ by a single nucleotide, using permutations at the sixth and seventh positions in the gRNA. Using these specificity features, we employed MpAgo RNPs to detect specific adenosine-to-inosine–edited RNAs in a complex mixture. These findings broaden our mechanistic understanding of the interactions of Argonautes with guide and substrate RNAs, and demonstrate that MpAgo RNPs with 5′-BrdU-modified gRNAs can be used as a highly specific RNA-targeting platform to probe RNA biology.

APA, Harvard, Vancouver, ISO, and other styles

45

Grentzinger, Thomas, Stefan Oberlin, Gregory Schott, Dominik Handler, Julia Svozil, Veronica Barragan-Borrero, Adeline Humbert, Sandra Duharcourt, Julius Brennecke, and Olivier Voinnet. "A universal method for the rapid isolation of all known classes of functional silencing small RNAs." Nucleic Acids Research 48, no. 14 (June 4, 2020): e79-e79. http://dx.doi.org/10.1093/nar/gkaa472.

Full text

Abstract:

Abstract Diverse classes of silencing small (s)RNAs operate via ARGONAUTE-family proteins within RNA-induced-silencing-complexes (RISCs). Here, we have streamlined various embodiments of a Q-sepharose-based RISC-purification method that relies on conserved biochemical properties of all ARGONAUTEs. We show, in multiple benchmarking assays, that the resulting 15-min benchtop extraction procedure allows simultaneous purification of all known classes of RISC-associated sRNAs without prior knowledge of the samples-intrinsic ARGONAUTE repertoires. Optimized under a user-friendly format, the method – coined ‘TraPR’ for Trans-kingdom, rapid, affordable Purification of RISCs – operates irrespectively of the organism, tissue, cell type or bio-fluid of interest, and scales to minute amounts of input material. The method is highly suited for direct profiling of silencing sRNAs, with TraPR-generated sequencing libraries outperforming those obtained via gold-standard procedures that require immunoprecipitations and/or lengthy polyacrylamide gel-selection. TraPR considerably improves the quality and consistency of silencing sRNA sample preparation including from notoriously difficult-to-handle tissues/bio-fluids such as starchy storage roots or mammalian plasma, and regardless of RNA contaminants or RNA degradation status of samples.

APA, Harvard, Vancouver, ISO, and other styles

46

Hu, Yang, Jan Stenlid, Malin Elfstrand, and Åke Olson. "Evolution of RNA interference proteins dicer and argonaute in Basidiomycota." Mycologia 105, no. 6 (November 1, 2013): 1489–98. http://dx.doi.org/10.3852/13-171.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Valdmanis, Paul N., Shuo Gu, Nina Schüermann, Praveen Sethupathy, Dirk Grimm, and Mark A. Kay. "Expression determinants of mammalian argonaute proteins in mediating gene silencing." Nucleic Acids Research 40, no. 8 (December 30, 2011): 3704–13. http://dx.doi.org/10.1093/nar/gkr1274.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Moshkovich, Nellie, and Elissa P. Lei. "HP1 Recruitment in the Absence of Argonaute Proteins in Drosophila." PLoS Genetics 6, no. 3 (March 12, 2010): e1000880. http://dx.doi.org/10.1371/journal.pgen.1000880.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Hauptmann, Judith, Anne Dueck, Simone Harlander, Janina Pfaff, Rainer Merkl, and Gunter Meister. "Turning catalytically inactive human Argonaute proteins into active slicer enzymes." Nature Structural & Molecular Biology 20, no. 7 (May 12, 2013): 814–17. http://dx.doi.org/10.1038/nsmb.2577.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Baumberger, Nicolas, Ching-Hsui Tsai, Miranda Lie, Ericka Havecker, and David C. Baulcombe. "The Polerovirus Silencing Suppressor P0 Targets ARGONAUTE Proteins for Degradation." Current Biology 17, no. 18 (September 2007): 1609–14. http://dx.doi.org/10.1016/j.cub.2007.08.039.

Full text

APA, Harvard, Vancouver, ISO, and other styles

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