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N6‐methyladenosine and RNA secondary structure affect transcript stability and protein abundance during systemic salt stress in Arabidopsis
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/cpmb.21openalex-snapshot
Protein Interaction Profile Sequencing (PIP‐seq)
inferredcites →https://doi.org/10.1002/pld3.239openalex-snapshot
N6‐methyladenosine and RNA secondary structure affect transcript stability and protein abundance during systemic salt stress in Arabidopsis
inferredcites →https://doi.org/10.1002/wrna.1426openalex-snapshot
RNA structure, binding, and coordination in Arabidopsis
inferredcites →https://doi.org/10.1007/978-1-4939-9045-0_21openalex-snapshot
Using Protein Interaction Profile Sequencing (PIP-seq) to Identify RNA Secondary Structure and RNA–Protein Interaction Sites of Long Noncoding RNAs in Plants
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Computationally Characterizing Protein-Bound Long Noncoding RNAs and Their Secondary Structure Using Protein Interaction Profile Sequencing (PIP-Seq) in Plants
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Functional FRIGIDA allele enhances drought tolerance by regulating the P5CS1 pathway in Arabidopsis thaliana
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Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons
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N6-methyladenosine Modulates Messenger RNA Translation Efficiency
inferredcites →https://doi.org/10.1016/j.cell.2015.10.012openalex-snapshot
5′ UTR m6A Promotes Cap-Independent Translation
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Global Analysis of RNA Secondary Structure in Two Metazoans
inferredcites →https://doi.org/10.1016/j.celrep.2018.10.020openalex-snapshot
N6-Methyladenosine Inhibits Local Ribonucleolytic Cleavage to Stabilize mRNAs in Arabidopsis
inferredcites →https://doi.org/10.1016/j.devcel.2010.05.013openalex-snapshot
A Simple Method for Gene Expression and Chromatin Profiling of Individual Cell Types within a Tissue
inferredcites →https://doi.org/10.1016/j.devcel.2016.06.008openalex-snapshot
N6-Methyladenosine RNA Modification Regulates Shoot Stem Cell Fate in Arabidopsis
inferredcites →https://doi.org/10.1016/j.devcel.2017.03.018openalex-snapshot
A Global View of RNA-Protein Interactions Identifies Post-transcriptional Regulators of Root Hair Cell Fate
inferredcites →https://doi.org/10.1016/j.fob.2013.10.003openalex-snapshot
COLD SHOCK DOMAIN PROTEIN 3 is involved in salt and drought stress tolerance in Arabidopsis
inferredcites →https://doi.org/10.1016/j.molcel.2014.12.004openalex-snapshot
Global Analysis of the RNA-Protein Interaction and RNA Secondary Structure Landscapes of the Arabidopsis Nucleus
inferredcites →https://doi.org/10.1016/j.molcel.2018.01.019openalex-snapshot
N6-Methyladenosine Guides mRNA Alternative Translation during Integrated Stress Response
inferredcites →https://doi.org/10.1016/j.molp.2019.12.007openalex-snapshot
Epigenetic Modifications of mRNA and DNA in Plants
inferredcites →https://doi.org/10.1016/j.pbi.2018.05.010openalex-snapshot
The nucleotides they are a-changin’: function of RNA binding proteins in post-transcriptional messenger RNA editing and modification in Arabidopsis
inferredcites →https://doi.org/10.1016/j.tplants.2005.10.002openalex-snapshot
Developing salt-tolerant crop plants: challenges and opportunities
inferredcites →https://doi.org/10.1016/j.tplants.2012.08.004openalex-snapshot
Plant RNA chaperones in stress response
inferredcites →https://doi.org/10.1016/j.ymeth.2013.07.003openalex-snapshot
Improved genome-wide mapping of uncapped and cleaved transcripts in eukaryotes—GMUCT 2.0
inferredcites →https://doi.org/10.1017/s135583820100108xopenalex-snapshot
The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 5′ secondary structure
inferredcites →https://doi.org/10.1021/ac026117iopenalex-snapshot
Stop and Go Extraction Tips for Matrix-Assisted Laser Desorption/Ionization, Nanoelectrospray, and LC/MS Sample Pretreatment in Proteomics
inferredcites →https://doi.org/10.1038/250546a0openalex-snapshot
Structure of yeast phenylalanine tRNA at 3 Å resolution
inferredcites →https://doi.org/10.1038/nature10887openalex-snapshot
Modular regulatory principles of large non-coding RNAs
inferredcites →https://doi.org/10.1038/nature11013openalex-snapshot
Systematic discovery of structural elements governing stability of mammalian messenger RNAs
inferredcites →https://doi.org/10.1038/nature12730openalex-snapshot
N6-methyladenosine-dependent regulation of messenger RNA stability
inferredcites →https://doi.org/10.1038/nature12756openalex-snapshot
In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features
inferredcites →https://doi.org/10.1038/nature14234openalex-snapshot
N6-methyladenosine-dependent RNA structural switches regulate RNA–protein interactions
inferredcites →https://doi.org/10.1038/nature14263openalex-snapshot
Structural imprints in vivo decode RNA regulatory mechanisms
inferredcites →https://doi.org/10.1038/ncb2902openalex-snapshot
N6-methyladenosine modification destabilizes developmental regulators in embryonic stem cells
inferredcites →https://doi.org/10.1038/nprot.2008.211openalex-snapshot
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
inferredcites →https://doi.org/10.1038/s41467-019-13317-9openalex-snapshot
m6A in mRNA coding regions promotes translation via the RNA helicase-containing YTHDC2
inferredcites →https://doi.org/10.1038/s41594-018-0091-zopenalex-snapshot
Analyses of mRNA structure dynamics identify embryonic gene regulatory programs
inferredcites →https://doi.org/10.1038/s41594-019-0200-7openalex-snapshot
RNA structure maps across mammalian cellular compartments
inferredcites →https://doi.org/10.1038/srep29766openalex-snapshot
The RNA-binding protein repertoire of Arabidopsis thaliana
inferredcites →https://doi.org/10.1042/bj2290001openalex-snapshot
Structure and function of ribosomal RNA
inferredcites →https://doi.org/10.1046/j.1365-313x.1995.07050751.xopenalex-snapshot
Correlation between the induction of a gene for Δ1‐pyrroline‐5‐carboxylate synthetase and the accumulation of proline in Arabidopsis thaliana under osmotic stress
inferredcites →https://doi.org/10.1073/pnas.1610670114openalex-snapshot
Light affects salt stress-induced transcriptional memory of P5CS1 in Arabidopsis
inferredcites →https://doi.org/10.1073/pnas.1908052116openalex-snapshot
mRNA structure regulates protein expression through changes in functional half-life
inferredcites →https://doi.org/10.1080/07352689.2011.605739openalex-snapshot
Gene Expression Profiling of Plants under Salt Stress
inferredcites →https://doi.org/10.1093/jxb/eraa031openalex-snapshot
Duplication and functional divergence of a calcium sensor in the Brassicaceae
inferredcites →https://doi.org/10.1093/nar/gki760openalex-snapshot
Specific roles of 5' RNA secondary structures in stabilizing transcripts in chloroplasts
inferredcites →https://doi.org/10.1093/nar/gkl1172openalex-snapshot
The structure and function of small nucleolar ribonucleoproteins
inferredcites →https://doi.org/10.1104/pp.008532openalex-snapshot
Transcriptome Changes for Arabidopsis in Response to Salt, Osmotic, and Cold Stress,
inferredcites →https://doi.org/10.1104/pp.18.01400openalex-snapshot
Linking Duplication of a Calcium Sensor to Salt Tolerance in Eutrema salsugineum
inferredcites →https://doi.org/10.1105/tpc.112.104232openalex-snapshot
Regulatory Impact of RNA Secondary Structure across the Arabidopsis Transcriptome
inferredcites →https://doi.org/10.1105/tpc.15.00591openalex-snapshot
Chemical Modifications Mark Alternatively Spliced and Uncapped Messenger RNAs in Arabidopsis
inferredcites →https://doi.org/10.1105/tpc.16.00562openalex-snapshot
In Planta Determination of the mRNA-Binding Proteome of Arabidopsis Etiolated Seedlings
inferredcites →https://doi.org/10.1111/j.1365-313x.2007.03318.xopenalex-snapshot
Duplicated P5CS genes of Arabidopsis play distinct roles in stress regulation and developmental control of proline biosynthesis
inferredcites →https://doi.org/10.1111/j.1469-8137.2005.01487.xopenalex-snapshot
Genes and salt tolerance: bringing them together
inferredcites →https://doi.org/10.1126/science.1192002openalex-snapshot
Long Noncoding RNA as Modular Scaffold of Histone Modification Complexes
inferredcites →https://doi.org/10.1126/science.185.4149.435openalex-snapshot
Three-Dimensional Tertiary Structure of Yeast Phenylalanine Transfer RNA
inferredcites →https://doi.org/10.1128/mcb.8.7.2737openalex-snapshot
Leader Length and Secondary Structure Modulate mRNA Function under Conditions of Stress
inferredcites →https://doi.org/10.1146/annurev-arplant-043015-111754openalex-snapshot
The Conservation and Function of RNA Secondary Structure in Plants
inferredcites →https://doi.org/10.1146/annurev.arplant.59.032607.092911openalex-snapshot
Mechanisms of Salinity Tolerance
inferredcites →https://doi.org/10.1186/1471-2164-15-431openalex-snapshot
Genome-wide analysis of alternative splicing of pre-mRNA under salt stress in Arabidopsis
inferredcites →https://doi.org/10.1186/gb-2014-15-1-r3openalex-snapshot
RNase-mediated protein footprint sequencing reveals protein-binding sites throughout the human transcriptome
inferredcites →https://doi.org/10.1186/s12859-016-1071-0openalex-snapshot
A comprehensive database of high-throughput sequencing-based RNA secondary structure probing data (Structure Surfer)
inferredcites →https://doi.org/10.1186/s13059-014-0550-8openalex-snapshot
Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2
inferredcites →https://doi.org/10.1261/rna.072850.119openalex-snapshot
Tissue-specific changes in the RNA structurome mediate salinity response in Arabidopsis
inferredcites →https://doi.org/10.1371/journal.pone.0088222openalex-snapshot
Secondary Structures of rRNAs from All Three Domains of Life
inferredcites →https://doi.org/10.3389/fphys.2018.01201openalex-snapshot
Long Non-coding RNA Structure and Function: Is There a Link?
inferredcites →https://doi.org/10.3389/fpls.2018.00671openalex-snapshot
New Era of Studying RNA Secondary Structure and Its Influence on Gene Regulation in Plants
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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