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Showing 1–13 of 13 results
Advanced filters: Author: "Richard Kriwacki" Clear advanced filters
  • Here, the authors use small angle neutron scattering and coarse-grained molecular dynamics simulations to demonstrate that condensates based on the granular components of nucleoli are network fluids.

    • Furqan Dar
    • Samuel R. Cohen
    • Rohit V. Pappu
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-17
  • The cyclin-dependent kinase (Cdk) inhibitor p27Kip1 (p27) folds upon binding to Cdk/cyclin complexes and during cell cycle progression p27 becomes phosphorylated, which triggers its ubiquitination and degradation. Here the authors use an integrated approach and show that Cdk2/cyclin A-bound p27 samples lowly-populated conformations that dynamically anticipate the sequential steps of the signaling cascade.

    • Maksym Tsytlonok
    • Hugo Sanabria
    • Richard Kriwacki
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-13
  • Many fusion oncoproteins (FOs) form condensates, some form in the nucleus and regulate gene expression while others form in the cytoplasm and promote cell signaling. In this work, the authors report the analysis of physicochemical features to enable prediction of FO condensation behavior.

    • Swarnendu Tripathi
    • Hazheen K. Shirnekhi
    • Richard W. Kriwacki
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-25
  • The nucleolus is a membrane-less organelle formed through liquid–liquid phase separation (LLPS). Here the authors use biophysical methods and show that the nucleolar protein nucleophosmin (NPM1) also undergoes LLPS through homotypic, inter-NPM1 interactions and discuss implications for the ribosome biogenesis process.

    • Diana M. Mitrea
    • Jaclyn A. Cika
    • Richard W. Kriwacki
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-13
  • The nucleolus is a membrane-less organelle and both Nucleophosmin (NPM1) and Surfeit locus protein 6 (SURF6) are abundant proteins within the nucleolus. Here the authors employ biophysical methods to study the properties of NPM1-S6N droplets and provide insights into the role of SURF6 in maintaining and modulating the liquid-like structure of the nucleolus.

    • Mylene C. Ferrolino
    • Diana M. Mitrea
    • Richard W. Kriwacki
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11
  • Post-translational modification of residues in an intrinsically disordered region of Bcl-XL promotes interactions with its folded core and allosterically reduces affinity for proapoptotic BH3-domain-containing proteins, resulting in apoptosis.

    • Ariele Viacava Follis
    • Fabien Llambi
    • Richard W. Kriwacki
    Research
    Nature Chemical Biology
    Volume: 14, P: 458-465
  • Tumor suppressor p53 can activate BAX or BAK; this activity is opposed by antiapoptotic protein BCL-xL, which sequesters p53. Now Kriwacki, Green and colleagues characterize the human p53–BCL-xL complex by NMR spectroscopy, thus allowing mutagenesis analyses to dissect p53's nuclear and cytosolic functions and BCL-xL's antiapoptotic mechanisms.

    • Ariele Viacava Follis
    • Fabien Llambi
    • Richard W Kriwacki
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 535-543
  • NMR reveals the dynamic stretching ability of the subdomain LH of the intrinsically disordered p21, providing a physical basis for the binding and functional diversity in its cell cycle regulatory role as a modulator of Cdk–cyclin complexes.

    • Yuefeng Wang
    • John C Fisher
    • Richard W Kriwacki
    Research
    Nature Chemical Biology
    Volume: 7, P: 214-221
  • The dynamic interplay between p53 and Mdm2 triggers cell cycle arrest after DNA damage. A new study reveals that disorder in the transactivation domain of p53 is important for tuning this negative feedback system to ensure normal cellular signaling responses.

    • Richard W Kriwacki
    News & Views
    Nature Chemical Biology
    Volume: 10, P: 987-988