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Showing 1–6 of 6 results
Advanced filters: Author: Krishnananda Chattopadhyay Clear advanced filters

  • Sannigrahi et al. discuss conformational switching that allows proteins to alter their conformation, aiding in pathogenesis by enabling cellular entry of viruses and bacterial toxins. Focussing on fusion domain of the Spike glycoprotein of SARS COV2 virus, they identify similar “switching sequences” present in diverse pathogen derived proteins.

    • Achinta Sannigrahi
    • Nayan De
    • Krishnananda Chattopadhyay
    ReviewsOpen Access
    Communications Biology
    Volume: 3, P: 1-6

  • Chakraborty et al. present biophysical and structural insights into fibril-forming oligomers of alpha-synuclein stabilized by heme. They show that heme targets the His50 residue of the oligomers and locks the protein into a different conformation which leads to non-toxic, non-fibrillating oligomer formation, therefore addressing a very important issue in the field of structure of transient oligomers.

    • Ritobrita Chakraborty
    • Sandip Dey
    • Krishnananda Chattopadhyay
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-14

  • Although liquid-liquid phase separation (LLPS) has been extensively studied in various cellular and organismal contexts, the link between functional influence of a genetic mutation and LLPS with respect to human diseases is poorly understood. A recent article by Mensah et al. looks at a rare genetic disease to identify a frameshift mutation, which triggered aberrant phase separation and nucleolar dysregulation, linking genetic variants to a dysregulation of biomolecular condensates.

    • Sumangal Roychowdhury
    • Krishnananda Chattopadhyay
    Research HighlightsOpen Access
    Communications Biology
    Volume: 6, P: 1-2

  • Protein aggregation and phase separation appear to play important roles in diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia (FTLD), but the interplay between different participating molecular events-which may facilitate or inhibit one another-can be difficult to study by conventional ensemble methods. In a recent study, Kevin Rhine and co-workers make use of point mutations to demonstrate the contrasting behaviour of condensates arising from Glycine and Arginine FUS mutants using single molecules fluorescence measurements.

    • Krishnananda Chattopadhyay
    Research HighlightsOpen Access
    Communications Biology
    Volume: 4, P: 1-2