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We began analyzing https://www.tandfonline.com/doi/abs/10.4161/rna.25194, but it redirected us to https://www.tandfonline.com/doi/abs/10.4161/rna.25194. The analysis below is for the second page.

Title[redir]:
Full article: Identification of LIN28B-bound mRNAs reveals features of target recognition and regulation
Description:
Post-transcriptional gene regulation is elicited through a complex network of RNA-binding proteins (RBPs) and miRNA-containing ribonucleoprotein complexes that target defined sequence elements with...

Matching Content Categories {πŸ“š}

  • Science
  • Education
  • Dating & Relationships

Content Management System {πŸ“}

What CMS is doi.org built with?

Custom-built

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

Traffic Estimate {πŸ“ˆ}

What is the average monthly size of doi.org audience?

πŸ™οΈ Massive Traffic: 50M - 100M visitors per month


Based on our best estimate, this website will receive around 80,486,609 visitors per month in the current month.

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How Does Doi.org Make Money? {πŸ’Έ}

We can't figure out the monetization strategy.

Many websites are intended to earn money, but some serve to share ideas or build connections. Websites exist for all kinds of purposes. This might be one of them. Doi.org has a secret sauce for making money, but we can't detect it yet.

Keywords {πŸ”}

open, linb, science, pmid, windowgoogle, scholar, cell, windowpubmed, windowweb, protein, lin, binding, sites, fig, parclip, cells, target, rna, sequence, csd, zkd, clusters, proteins, targets, motif, lina, genes, mrna, transcripts, experiments, human, observed, acids, expression, analysis, regulation, crosslinking, studies, rnabinding, mrnas, gene, bound, domain, knockdown, data, stem, amino, top, molecular, cycle,

Topics {βœ’οΈ}

/flag/ha-dest destination vectorcitation7 matrix-assisted laser desorption/ionization flag/ha-tagged lin28b protein lin28-mediated post-transcriptional regulation expressing flag/ha-lin28b flag/ha-lin28b expressing full-length ido-par-clips social care medicine cold-shock protein cspb medical systems biology post-transcriptional events inducible flag/ha-lin28b post-transcriptional gene regulation recombinant flag/ha-lin28b lin28b par-clip-binding sites csd ido-par-clip data c-terminally tagged lin28b insulin-pi3k-mtor pathway single cold-shock domain inducible lin28b-expressing cells genome-wide studies reveal elute full-length lin28b semi-dry blotting apparatus lc/ms sample pretreatment οΏ½medium-heavy”-labeled silac medium dna-mod zoops-minsites 20 par-clip data sets develop ido-par-clip developed ido-par-clip full-length lin28b protein c-terminally truncated lin28b ido-par-clip data individual domain par-clip full-length lin28b proteins d-mem high glucose counteract false-positive signals additional material acknowledgments anti-flag m2 antibody lin28b par-clip data post-transcriptional regulation g-rich binding motif protein-rna complex migrating neural stem-cell commitment single-stranded dna binding hrp-conjugated secondary antibody ido-par-clip approach n-terminal flag-tag transition-centered binding sites transcriptome-wide view rna-binding protein hur

Questions {❓}

  • How does Lin28 let-7 control development and disease?
  • Why publish with us?

Schema {πŸ—ΊοΈ}

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            name:Identification of LIN28B-bound mRNAs rev ....
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      articleSection:Research Paper
      name:Identification of LIN28B-bound mRNAs reveals features of target recognition and regulation
      headline:Identification of LIN28B-bound mRNAs reveals features of target recognition and regulation
      abstract:The conserved human LIN28 RNA-binding proteins function in development, maintenance of pluripotency and oncogenesis. We used PAR-CLIP and a newly developed variant of this method, iDo-PAR-CLIP, to identify LIN28B targets as well as sites bound by the individual RNA-binding domains of LIN28B in the human transcriptome at nucleotide resolution. The position of target binding sites reflected the known structural relative orientation of individual LIN28B-binding domains, validating iDo-PAR-CLIP. Our data suggest that LIN28B directly interacts with most expressed mRNAs and members of the let-7 microRNA family. The Lin28-binding motif detected in pre-let-7 was enriched in mRNA sequences bound by LIN28B. Upon LIN28B knockdown, cell proliferation and the cell cycle were strongly impaired. Quantitative shotgun proteomics of LIN28B depleted cells revealed significant reduction of protein synthesis from its RNA targets. Computational analyses provided evidence that the strength of protein synthesis reduction correlated with the location of LIN28B binding sites within target transcripts.
      description:The conserved human LIN28 RNA-binding proteins function in development, maintenance of pluripotency and oncogenesis. We used PAR-CLIP and a newly developed variant of this method, iDo-PAR-CLIP, to identify LIN28B targets as well as sites bound by the individual RNA-binding domains of LIN28B in the human transcriptome at nucleotide resolution. The position of target binding sites reflected the known structural relative orientation of individual LIN28B-binding domains, validating iDo-PAR-CLIP. Our data suggest that LIN28B directly interacts with most expressed mRNAs and members of the let-7 microRNA family. The Lin28-binding motif detected in pre-let-7 was enriched in mRNA sequences bound by LIN28B. Upon LIN28B knockdown, cell proliferation and the cell cycle were strongly impaired. Quantitative shotgun proteomics of LIN28B depleted cells revealed significant reduction of protein synthesis from its RNA targets. Computational analyses provided evidence that the strength of protein synthesis reduction correlated with the location of LIN28B binding sites within target transcripts.
      author:
            type:Person
            name:Nikolaus Rajewsky
            type:Person
            name:Florian Mayr
            type:Person
            name:Guido Mastrobuoni
            type:Person
            name:Mathias Munschauer
            type:Person
            name:Nikolaus Rajewsky
            type:Person
            name:Stefan Kempa
            type:Person
            name:Udo Heinemann
            type:Person
            name:Robin Graf
            type:Person
            name:Nikolaus Rajewsky
            type:Person
            name:Nikolaus Rajewsky
            type:Person
            name:Nikolaus Rajewsky
            type:Person
            name:Nikolaus Rajewsky
            type:Person
            name:Nikolaus Rajewsky
            type:Person
            name:Markus Landthaler
      keywords:post-transcriptional regulation, RNA-binding protein, CLIP, stem cell
      pageStart:1146
      pageEnd:1159
      datePublished:2013-05-29
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      name:Stefan Kempa
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      name:Nikolaus Rajewsky
      name:Nikolaus Rajewsky
      name:Nikolaus Rajewsky
      name:Nikolaus Rajewsky
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