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AggreProt: a web server for predicting and engineering aggregation prone regions in proteins

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F24%3A00081379" target="_blank" >RIV/00159816:_____/24:00081379 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14310/24:00136705 RIV/61989100:27740/24:10255789

  • Result on the web

    <a href="https://pmc.ncbi.nlm.nih.gov/articles/PMC11223854/pdf/gkae420.pdf" target="_blank" >https://pmc.ncbi.nlm.nih.gov/articles/PMC11223854/pdf/gkae420.pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/nar/gkae420" target="_blank" >10.1093/nar/gkae420</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    AggreProt: a web server for predicting and engineering aggregation prone regions in proteins

  • Original language description

    Recombinant proteins play pivotal roles in numerous applications including industrial biocatalysts or therapeutics. Despite the recent progress in computational protein structure prediction, protein solubility and reduced aggregation propensity remain challenging attributes to design. Identification of aggregation-prone regions is essential for understanding misfolding diseases or designing efficient protein-based technologies, and as such has a great socio-economic impact. Here, we introduce AggreProt, a user-friendly webserver that automatically exploits an ensemble of deep neural networks to predict aggregation-prone regions (APRs) in protein sequences. Trained on experimentally evaluated hexapeptides, AggreProt compares to or outperforms state-of-the-art algorithms on two independent benchmark datasets. The server provides per-residue aggregation profiles along with information on solvent accessibility and transmembrane propensity within an intuitive interface with interactive sequence and structure viewers for comprehensive analysis. We demonstrate AggreProt efficacy in predicting differential aggregation behaviours in proteins on several use cases, which emphasize its potential for guiding protein engineering strategies towards decreased aggregation propensity and improved solubility. The webserver is freely available and accessible at https://loschmidt.chemi.muni.cz/aggreprot/. Graphical Abstract

  • 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

Others

  • Publication year

    2024

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nucleic Acids Research

  • ISSN

    0305-1048

  • e-ISSN

    1362-4962

  • Volume of the periodical

    52

  • Issue of the periodical within the volume

    W1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    11

  • Pages from-to

    "W159"-"W169"

  • UT code for WoS article

    001233323700001

  • EID of the result in the Scopus database