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Identification of Distinct Amino Acid Composition of Human Cruciform Binding Proteins

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17310%2F19%3AA20020ZY" target="_blank" >RIV/61988987:17310/19:A20020ZY - isvavai.cz</a>

  • Alternative codes found

    RIV/68081707:_____/19:00510902

  • Result on the web

    <a href="https://link.springer.com/article/10.1134%2FS0026893319010023" target="_blank" >https://link.springer.com/article/10.1134%2FS0026893319010023</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1134/S0026893319010023" target="_blank" >10.1134/S0026893319010023</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Identification of Distinct Amino Acid Composition of Human Cruciform Binding Proteins

  • Original language description

    Cruciform structures are preferential targets for many architectural and regulatory proteins, as well as a number of DNA binding proteins with weak sequence specificity. Some of these proteins are also capable of inducing the formation of cruciform structures upon DNA binding. In this paper we analyzed the amino acid composition of eighteen cruciform binding proteins of Homo sapiens. Comparison with general amino acid frequencies in all human proteins revealed unique differences, with notable enrichment for lysine and serine and/or depletion for alanine, glycine, glutamine, arginine, tyrosine and tryptophan residues. Based on bootstrap resampling and fuzzy cluster analysis, multiple molecular mechanisms of interaction with cruciform DNA structures could be suggested, including those involved in DNA repair, transcription and chromatin regulation. The proteins DEK, HMGB1 and TOP1 in particular formed a very distinctive group. Nonetheless, a strong interaction network connecting nearly all the cruciform binding proteins studied was demonstrated. Data reported here will be very useful for future prediction of new cruciform binding proteins or even construction of predictive tool/web-based application.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2019

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Molecular Biology

  • ISSN

    0026-8933

  • e-ISSN

  • Volume of the periodical

    53

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    RU - RUSSIAN FEDERATION

  • Number of pages

    9

  • Pages from-to

    97-106

  • UT code for WoS article

    000468512300012

  • EID of the result in the Scopus database