Reviewed articles

A list by Biophysics Colab

Articles that have been reviewed by Biophysics Colab.

27 articlesLast updated

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  2. TMEM16 scramblases thin the membrane to enable lipid scrambling

    1. Maria E. Falzone
    2. Zhang Feng
    3. Omar E. Alvarenga
    4. Yangang Pan
    5. ByoungCheol Lee
    6. Xiaolu Cheng
    7. Eva Fortea
    8. Simon Scheuring
    9. Alessio Accardi

    • Curated by Biophysics Colab

      Biophysics Colab

      Endorsement statement (11 May 2022)

      Falzone et al. report important new cryo-EM structures of the fungal calcium-activated lipid scramblase afTMEM16, as well as the functional impact of mutations and different lipid membrane compositions on lipid scrambling. Individual lipids are beautifully resolved around the subunit cavity involved in lipid scrambling in one of the highest resolution structures of a TMEM16 protein solved to date, enabling the role of these lipid-interacting residues to be interrogated. Collectively, the results suggest that afTMEM16 catalyzes lipid scrambling by thinning the membrane rather than providing a hydrophilic permeation pathway for lipids. The work represents an important contribution that will be of interest to scientists investigating the mechanisms of lipid scrambling and how membrane proteins interact with their lipid environment.

      (This endorsement by Biophysics Colab refers to the version of record for this work, which is linked to and has been revised from the original preprint following peer review.)

    Reviewed by Biophysics Colab

    3 evaluationsAppears in 2 listsLatest version Latest activity

  4. Fast ATP-Dependent Subunit Rotation in Reconstituted F o F 1 -ATP Synthase Trapped in Solution

    1. Thomas Heitkamp
    2. Michael Börsch

    • Curated by Biophysics Colab

      Endorsement statement (21 September 2021)

      The preprint by Heitkamp and Börsch describes visualization of the fast ATP-dependent subunit rotation in reconstituted FoF1-ATP synthase using single-molecule FRET techniques. Using a highly innovative method for trapping single molecules, the authors were able to see the static and dynamic disorder of enzymes in solution, not possible in previous studies. The work makes important contributions to both understanding the structural dynamics of FoF1-ATP synthase and the development of methodologies to study single-molecule dynamics of other proteins in solution.

      (This endorsement refers to version 5 of this preprint, which was peer reviewed by Biophysics Colab.)

    Reviewed by Biophysics Colab

    2 evaluationsAppears in 3 listsLatest version Latest activity

  5. Mechanism of CFTR correction by type I folding correctors

    1. Karol Fiedorczuk
    2. Jue Chen

    • Curated by Biophysics Colab

      Endorsement statement (27 April 2022)

      The preprint by Fiedorczuk and Chen presents structures of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel in complex with type I correctors, a class of drug currently used to treat cystic fibrosis by targeting CFTR folding and stability. The strength of the paper lies in the consistency of the structural data with maturation and binding assays, as well as with much of the existing literature. Overall, the work represents a rigorous investigation of the mechanism of these drugs, and will be of interest to those who study cystic fibrosis, protein folding, and drug design.

      (This endorsement refers to version 1 of this preprint, which was peer reviewed by Biophysics Colab.)

    Reviewed by Biophysics Colab

    2 evaluationsAppears in 2 listsLatest version Latest activity

  7. Single-molecule imaging with cell-derived nanovesicles reveals early binding dynamics at a cyclic nucleotide-gated ion channel

    1. Vishal R. Patel
    2. Arturo M. Salinas
    3. Darong Qi
    4. Shipra Gupta
    5. David J. Sidote
    6. Marcel P. Goldschen-Ohm

    • Curated by Biophysics Colab

      Endorsement statement (30 August 2021)

      The preprint by Patel et al. describes the development of a single molecule approach for studying individual ligand binding events in membrane proteins within native lipid environments. The approach represents an elegant way to investigate the dynamics of ligand binding, and potential relationships with conformational changes, in molecules embedded within physiological membranes. The work makes an important contribution that will be of interest to scientists working on molecular mechanisms in ion channels and other membrane proteins.

      (This endorsement by Biophysics Colab refers to version 2 of this preprint, which has been revised in response to peer review of version 1.)

    Reviewed by Biophysics Colab

    3 evaluationsAppears in 4 listsLatest version Latest activity