Efficient One-Step Knockout by Electroporation of Ribonucleoproteins Into Zona-Intact Bovine Embryos [PDF]
Frontiers in Genetics, 2020 Somatic cell nuclear transfer or cytoplasm microinjection have been used to generate genome-edited farm animals; however, these methods have several drawbacks that reduce their efficiency. This study aimed to develop electroporation conditions that allow
Luiz Sergio Almeida Camargo +3 more
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The TROVE module: A common element in Telomerase, Ro and Vault ribonucleoproteins
BMC Bioinformatics, 2003 Background Ribonucleoproteins carry out a variety of important tasks in the cell. In this study we show that a number of these contain a novel module, that we speculate mediates RNA-binding. Results The TROVE module – Telomerase, Ro and Vault module – is
Bateman Alex, Kickhoefer Valerie
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Membrane permeabilizing amphiphilic peptide delivers recombinant transcription factor and CRISPR-Cas9/Cpf1 ribonucleoproteins in hard-to-modify cells. [PDF]
PLoS ONE, 2018 Delivery of recombinant proteins to therapeutic cells is limited by a lack of efficient methods. This hinders the use of transcription factors or Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) ribonucleoproteins to develop cell ...
Thomas Del'Guidice +12 more
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Activation of Peptidylarginine Deiminase in the Salivary Glands of Balb/c Mice Drives the Citrullination of Ro and La Ribonucleoproteins [PDF]
Journal of Immunology Research, 2017 The goal of the present study was to determine whether peptidylarginine deiminase PAD2 and PAD4 enzymes are present in Balb/c mouse salivary glands and whether they are able to citrullinate Ro and La ribonucleoproteins.
Mayra Rodríguez-Rodríguez +7 more
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The World of Stable Ribonucleoproteins and Its Mapping With Grad-Seq and Related Approaches
Frontiers in Molecular Biosciences, 2021 Macromolecular complexes of proteins and RNAs are essential building blocks of cells. These stable supramolecular particles can be viewed as minimal biochemical units whose structural organization, i.e., the way the RNA and the protein interact with each
Milan Gerovac +4 more
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Ro60 and La ribonucleoproteins become self-aggregated by cell stress
Reumatismo, 2011 Ro is a cellular particle composed by three ribonucleoproteins of 60, 54 and 52 kDa (1-3). Ro60 forms a complex with one of the 1-5 hYRNAs (4). Antigenic properties of Ro were described by Clark in 1969 using autoimmune sera (5), and it is broadly ...
E. Avalos-Díaz +3 more
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New insights into trypanosomatid U5 small nuclear ribonucleoproteins [PDF]
Memorias do Instituto Oswaldo Cruz, 2011 Several protozoan parasites exist in the Trypanosomatidae family, including various agents of human diseases. Multiple lines of evidence suggest that important differences are present between the translational and mRNA processing (trans splicing) systems
Marco Túlio A da Silva +8 more
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Diverse roles of heterogeneous nuclear ribonucleoproteins in viral life cycle
Frontiers in Virology, 2022 Understanding the host-virus interactions helps to decipher the viral replication strategies and pathogenesis. Viruses have limited genetic content and rely significantly on their host cell to establish a successful infection.
Krishna Bhattarai, Martin Holcik
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Collaborative interactions of heterogenous ribonucleoproteins contribute to transcriptional regulation of sterol metabolism in mice [PDF]
Nature Communications, 2020 Heterogeneous nuclear ribonucleoproteins (hnRNPs) play critical roles in the biogenesis, localization and transport of RNA. Here authors investigate a role for hnRNPs in sterol metabolism in mice and provide insights into their role in selective promoter
Zhengyi Zhang +14 more
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Influenza A virus ribonucleoproteins form liquid organelles at endoplasmic reticulum exit sites [PDF]
Nature Communications, 2019 Influenza A virus forms cytosolic inclusions containing viral ribonucleoproteins. Here, the authors show that viral inclusions form juxtaposed the endoplasmic reticulum and have liquid properties, likely constituting sites of assembly of epidemic and ...
Marta Alenquer +5 more
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