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We are analyzing https://www.nature.com/articles/nrd.2018.71.

Title:
RNA-modifying proteins as anticancer drug targets | Nature Reviews Drug Discovery
Description:
Covalent modifications of RNA β€” mediated by RNA-modifying proteins (RMPs) β€” affect RNA stability and translation to proteins, and some of these RMPs have been implicated in cancer. Here, Copeland and colleagues review the current understanding of RNA modifications with a focus on mRNA methylation and assess the potential of RMPs as novel anticancer targets. All major biological macromolecules (DNA, RNA, proteins and lipids) undergo enzyme-catalysed covalent modifications that impact their structure, function and stability. A variety of covalent modifications of RNA have been identified and demonstrated to affect RNA stability and translation to proteins; these mechanisms of translational control have been termed epitranscriptomics. Emerging data suggest that some epitranscriptomic mechanisms are altered in human cancers as well as other human diseases. In this Review, we examine the current understanding of RNA modifications with a focus on mRNA methylation, highlight their possible roles in specific cancer indications and discuss the emerging potential of RNA-modifying proteins as therapeutic targets.
Website Age:
30 years and 10 months (reg. 1994-08-11).

Matching Content Categories {πŸ“š}

  • Education
  • Science
  • Business & Finance

Content Management System {πŸ“}

What CMS is nature.com built with?

Custom-built

No common CMS systems were detected on Nature.com, and no known web development framework was identified.

Traffic Estimate {πŸ“ˆ}

What is the average monthly size of nature.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
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How Does Nature.com Make Money? {πŸ’Έ}


Display Ads {🎯}


The website utilizes display ads within its content to generate revenue. Check the next section for further revenue estimates.

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google.com, pmc.com, doceree.com, yourbow.com, audienciad.com, onlinemediasolutions.com, advibe.media, aps.amazon.com, getmediamx.com, onomagic.com

Reseller Advertisers (38)
conversantmedia.com, rubiconproject.com, pubmatic.com, appnexus.com, openx.com, smartadserver.com, lijit.com, sharethrough.com, video.unrulymedia.com, google.com, yahoo.com, triplelift.com, onetag.com, sonobi.com, contextweb.com, 33across.com, indexexchange.com, media.net, themediagrid.com, adform.com, richaudience.com, sovrn.com, improvedigital.com, freewheel.tv, smaato.com, yieldmo.com, amxrtb.com, adyoulike.com, adpone.com, criteo.com, smilewanted.com, 152media.info, e-planning.net, smartyads.com, loopme.com, opera.com, mediafuse.com, betweendigital.com

How Much Does Nature.com Make? {πŸ’°}


Display Ads {🎯}

$63,100 per month
Our estimates place Nature.com's monthly online earnings from display ads at $42,042 to $115,616.

Keywords {πŸ”}

pubmed, article, google, scholar, cas, central, rna, cell, cancer, biol, chem, nature, human, methylation, protein, nat, res, proteins, methyltransferase, structure, mrna, enzymes, mol, family, nucleic, fto, trna, acids, dna, modifications, domain, structural, nmethyladenosine, basis, drug, discovery, modification, mettl, alkb, med, breast, cells, complex, access, methyltransferases, inhibitors, gene, reveals, binding, recognition,

Topics {βœ’οΈ}

permissions reprints nature portfolio journals privacy policy fe2+β€”Ξ±-kg-dependent dioxygenase superfamily targeting fto/m6a/myc/cebpa signaling nature portfolio body mass index sah s-adenosyl-l-homocysteine adar rna editing advertising posttranscriptional m6a editing cross-linked protein-dna system cell-type-specific methylation patterns nol1/nop2/sun domain family social media hypoxia-inducible microrna-210 regulates mediates myc-induced proliferation alkbh2 mutants cross-linked s-adenosyl-l-methionine high-resolution mapping reveals pi3k/akt signaling pathway guide rna-protein interactions mettl3-mediated m6a modification n6-methyladenosine rna demethylase single-nucleotide-resolution mapping china chem eif4e mrna-cap interaction il-7/stat5/socs pathways protein-protein interaction inhibitors n6-methyladenosine demethylase fto a-dependent translation control editing dna-repair protein alkb n6-methyladenosine-dependent regulation sam-dependent methyltransferase catalysis alkali-stable dinucleotide sequences dimt1-irf4 oncogenic axis oxygen-sensing prolyl hydroxylases /alpha-ketoglutarate-dependent dioxygenases alpha-ketoglutarate-dependent dioxygenases n6-methylated adenosine modification article boriack-sjodin acute mega-karyoblastic leukemia reverse dna/rna damage eif4e cap-binding protein alkbhs-facilitated rna modifications genome-wide meta-analyses m7g-cap-binding mode n6-methyladenosine reader proteins x-ray crystal structural

Questions {❓}

  • Eukaryotic stand-alone pseudouridine synthases β€” RNA modifying enzymes and emerging regulators of gene expression?

Schema {πŸ—ΊοΈ}

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         description:Covalent modifications of RNA Ҁ” mediated by RNA-modifying proteins (RMPs) Ҁ” affect RNA stability and translation to proteins, and some of these RMPs have been implicated in cancer. Here, Copeland and colleagues review the current understanding of RNA modifications with a focus on mRNA methylation and assess the potential of RMPs as novel anticancer targets. All major biological macromolecules (DNA, RNA, proteins and lipids) undergo enzyme-catalysed covalent modifications that impact their structure, function and stability. A variety of covalent modifications of RNA have been identified and demonstrated to affect RNA stability and translation to proteins; these mechanisms of translational control have been termed epitranscriptomics. Emerging data suggest that some epitranscriptomic mechanisms are altered in human cancers as well as other human diseases. In this Review, we examine the current understanding of RNA modifications with a focus on mRNA methylation, highlight their possible roles in specific cancer indications and discuss the emerging potential of RNA-modifying proteins as therapeutic targets.
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