Jacek Czub - Publications - Bridge of Knowledge

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Year 2011
Year 2021
  • Two bacterial small heat shock proteins, IbpA and IbpB, form a functional heterodimer
    Publication

    - JOURNAL OF MOLECULAR BIOLOGY - Year 2021

    Small heat shock proteins (sHsps) are a conserved class of ATP-independent chaperones which in stress conditions bind to unfolded protein substrates and prevent their irreversible aggregation. Substrates trapped in sHsps-containing aggregates are efficiently refolded into native structures by ATP-dependent Hsp70 and Hsp100 chaperones. Most γ-proteobacteria possess a single sHsp (IbpA), while in a subset of Enterobacterales, as...

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Year 2020
  • Two-step mechanism of J-domain action in driving Hsp70 function
    Publication
    • B. Tomiczek
    • W. Delewski
    • Ł. Nierzwicki
    • M. Stolarska
    • I. Grochowina
    • B. Schilke
    • R. Dutkiewicz
    • M. A. Uzarska
    • S. Ciesielski
    • J. Czub... and 2 others

    - PLoS Computational Biology - Year 2020

    J-domain proteins (JDPs), obligatory Hsp70 cochaperones, play critical roles in protein homeostasis. They promote key allosteric transitions that stabilize Hsp70 interaction with substrate polypeptides upon hydrolysis of its bound ATP. Although a recent crystal structure revealed the physical mode of interaction between a J-domain and an Hsp70, the structural and dynamic consequences of J-domain action once bound and how Hsp70s...

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Year 2024
  • Why Are Left-Handed G-Quadruplexes Scarce?

    G-quadruplexes (G4s) are nucleic acid structures crucial for the regulation of gene expression and genome maintenance. While they hold promise as nanodevice components, achieving desired G4 folds requires understanding the interplay between stability and structural properties, like helicity. Although right-handed G4 structures dominate the experimental data, the molecular basis for this preference over left-handed helicity is unclear....

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Year 2019

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