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  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Link.springer.com Make Money
  6. Keywords
  7. Topics
  8. Questions
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We are analyzing https://link.springer.com/article/10.1007/s00018-016-2217-y.

Title:
Nucleoside modifications in the regulation of gene expression: focus on tRNA | Cellular and Molecular Life Sciences
Description:
Both, DNA and RNA nucleoside modifications contribute to the complex multi-level regulation of gene expression. Modified bases in tRNAs modulate protein translation rates in a highly dynamic manner. Synonymous codons, which differ by the third nucleoside in the triplet but code for the same amino acid, may be utilized at different rates according to codon–anticodon affinity. Nucleoside modifications in the tRNA anticodon loop can favor the interaction with selected codons by stabilizing specific base pairs. Similarly, weakening of base pairing can discriminate against binding to near-cognate codons. mRNAs enriched in favored codons are translated in higher rates constituting a fine-tuning mechanism for protein synthesis. This so-called codon bias establishes a basic protein level, but sometimes it is necessary to further adjust the production rate of a particular protein to actual requirements, brought by, e.g., stages in circadian rhythms, cell cycle progression or exposure to stress. Such an adjustment is realized by the dynamic change of tRNA modifications resulting in the preferential translation of mRNAs coding for example for stress proteins to facilitate cell survival. Furthermore, tRNAs contribute in an entirely different way to another, less specific stress response consisting in modification-dependent tRNA cleavage that contributes to the general down-regulation of protein synthesis. In this review, we summarize control functions of nucleoside modifications in gene regulation with a focus on recent findings on protein synthesis control by tRNA base modifications.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Science
  • Telecommunications

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

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

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

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


Based on our best estimate, this website will receive around 7,643,078 visitors per month in the current month.

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How Does Link.springer.com Make Money? {💸}

We see no obvious way the site makes money.

Websites don't always need to be profitable; some serve as platforms for education or personal expression. Websites can serve multiple purposes. And this might be one of them. Link.springer.com might be making money, but it's not detectable how they're doing it.

Keywords {🔍}

pubmed, article, google, scholar, cas, trna, central, modifications, rna, translation, modification, trnas, wobble, protein, mitochondrial, cell, stress, base, position, codons, biol, mrna, nucleoside, codon, anticodon, mol, modified, human, mrnas, acids, methylation, res, chem, function, synthesis, proteins, control, halves, cells, structure, yeast, suzuki, nucleic, binding, genet, regulation, specific, cleavage, found, gene,

Topics {✒️}

article download pdf false watson–crick pairings histone acetyltransferase sin3/elp3 mto1 mediates tissue-specificity identical donor/acceptor pattern widespread post-transcriptional modifications von kleist-retzow jc post-transcriptionally modified nucleosides post-transcriptional modification steps growth phase-dependent alteration trna-derived rna fragments codon–anticodon affinity regulate transcriptome-wide mapping rapid transfer-rna deactivation rna epigenetics-chemical messages spring-loaded base modification trna-derived fragments contribute trna 5-methylaminomethyl-2-thiouridylate methyltransferase post-transcriptional modifications located base modification-mediated strengthening stabilizing codon–anticodon interactions purine-ending codons nna promotes cap-independent translation trm9-catalyzed trna modifications electron withdrawing/donating properties telomeric gene silencing intra-molecular cross-regulation modification-dependent trna cleavage gene expression affects prevailing mcm5h2u-trna product mitochondrial-trna modifier mto1 intrinsic codon–anticodon strength rna structure-specific manner ragged-red fiber disease cognate aminoacyl-trna synthetases mt-trna biochemical functions full size image n6-methyladenosine-dependent regulation 5′-cap-independent translation depends commonly base-methylated purines stress-induced cleavage rna-binding protein ybx1 3′utr-mediated translational control mt-trnas bearing ser mitochondria-specific 5-substituted pyrimidines cdk5rap1-mediated 2-methylthio modification codon–anticodon binding affinity murphy fv 4th correct mt-trna folding prevent frame-shift mutations

Questions {❓}

  • Belostotsky R, Frishberg Y, Entelis N (2012) Human mitochondrial tRNA quality control in health and disease: a channelling mechanism?
  • Grewal SS (2015) Why should cancer biologists care about tRNAs?
  • How does this work?
  • Lightowlers RN, Taylor RW, Turnbull DM (2015) Mutations causing mitochondrial disease: what is new challenges remain?

Schema {🗺️}

WebPage:
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         headline:Nucleoside modifications in the regulation of gene expression: focus on tRNA
         description:Both, DNA and RNA nucleoside modifications contribute to the complex multi-level regulation of gene expression. Modified bases in tRNAs modulate protein translation rates in a highly dynamic manner. Synonymous codons, which differ by the third nucleoside in the triplet but code for the same amino acid, may be utilized at different rates according to codon–anticodon affinity. Nucleoside modifications in the tRNA anticodon loop can favor the interaction with selected codons by stabilizing specific base pairs. Similarly, weakening of base pairing can discriminate against binding to near-cognate codons. mRNAs enriched in favored codons are translated in higher rates constituting a fine-tuning mechanism for protein synthesis. This so-called codon bias establishes a basic protein level, but sometimes it is necessary to further adjust the production rate of a particular protein to actual requirements, brought by, e.g., stages in circadian rhythms, cell cycle progression or exposure to stress. Such an adjustment is realized by the dynamic change of tRNA modifications resulting in the preferential translation of mRNAs coding for example for stress proteins to facilitate cell survival. Furthermore, tRNAs contribute in an entirely different way to another, less specific stress response consisting in modification-dependent tRNA cleavage that contributes to the general down-regulation of protein synthesis. In this review, we summarize control functions of nucleoside modifications in gene regulation with a focus on recent findings on protein synthesis control by tRNA base modifications.
         datePublished:2016-04-19T00:00:00Z
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            Modified nucleosides
            Stress signaling
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            Translation rate
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            Biomedicine
            general
            Life Sciences
            Biochemistry
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      headline:Nucleoside modifications in the regulation of gene expression: focus on tRNA
      description:Both, DNA and RNA nucleoside modifications contribute to the complex multi-level regulation of gene expression. Modified bases in tRNAs modulate protein translation rates in a highly dynamic manner. Synonymous codons, which differ by the third nucleoside in the triplet but code for the same amino acid, may be utilized at different rates according to codon–anticodon affinity. Nucleoside modifications in the tRNA anticodon loop can favor the interaction with selected codons by stabilizing specific base pairs. Similarly, weakening of base pairing can discriminate against binding to near-cognate codons. mRNAs enriched in favored codons are translated in higher rates constituting a fine-tuning mechanism for protein synthesis. This so-called codon bias establishes a basic protein level, but sometimes it is necessary to further adjust the production rate of a particular protein to actual requirements, brought by, e.g., stages in circadian rhythms, cell cycle progression or exposure to stress. Such an adjustment is realized by the dynamic change of tRNA modifications resulting in the preferential translation of mRNAs coding for example for stress proteins to facilitate cell survival. Furthermore, tRNAs contribute in an entirely different way to another, less specific stress response consisting in modification-dependent tRNA cleavage that contributes to the general down-regulation of protein synthesis. In this review, we summarize control functions of nucleoside modifications in gene regulation with a focus on recent findings on protein synthesis control by tRNA base modifications.
      datePublished:2016-04-19T00:00:00Z
      dateModified:2016-04-19T00:00:00Z
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         Regulation of gene expression
         Modified nucleosides
         Stress signaling
         tRNA
         Translation rate
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
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      name:Lodz University of Technology
      address:
         name:Institute of Organic Chemistry, Lodz University of Technology, Lodz, Poland
         type:PostalAddress
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               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Grażyna Leszczyńska
      affiliation:
            name:Lodz University of Technology
            address:
               name:Institute of Organic Chemistry, Lodz University of Technology, Lodz, Poland
               type:PostalAddress
            type:Organization
      name:Elzbieta Sochacka
      affiliation:
            name:Lodz University of Technology
            address:
               name:Institute of Organic Chemistry, Lodz University of Technology, Lodz, Poland
               type:PostalAddress
            type:Organization
      name:Barbara Nawrot
      affiliation:
            name:Polish Academy of Sciences
            address:
               name:Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Lodz, Poland
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Lodz, Poland
      name:Institute of Organic Chemistry, Lodz University of Technology, Lodz, Poland
      name:Institute of Organic Chemistry, Lodz University of Technology, Lodz, Poland
      name:Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Lodz, Poland

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