Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–14 of 14 results
Advanced filters: Author: Alberto Bartesaghi Clear advanced filters

  • MiLoPYP is a two-step, dataset-specific contrastive learning-based method for fast and accurate detection and localization of a diverse range of target structures in cryo-electron tomography data, enabling improved in situ structural biology.

    • Qinwen Huang
    • Ye Zhou
    • Alberto Bartesaghi
    ResearchOpen Access
    Nature Methods
    Volume: 21, P: 1863-1872

  • The hexagonal immature capsid lattice of human endogenous retrovirus K is determined at 3.2 Å resolution, which is an assembly of small molecule-stabilized hexamers via dimer and trimer interfaces, a highly conserved mechanism among retroviruses.

    • Anna-Sophia Krebs
    • Hsuan-Fu Liu
    • Peijun Zhang
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-11

  • Kumar and colleagues report cryo-EM structures of Arabidopsis O-fucosyltransferase SPINDLY in its apo and GDP-fucose bound states, revealing distinct active-site features enabling GDP-fucose recognition and surprisingly dynamic conformations that regulate its enzymatic activity.

    • Shivesh Kumar
    • Yan Wang
    • Pei Zhou
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12

  • nextPYP is a turn-key framework for single-particle cryo-electron tomography that streamlines complex data analysis pipelines, from pre-processing of tilt series to high-resolution refinement, for efficient analysis and visualization of large datasets.

    • Hsuan-Fu Liu
    • Ye Zhou
    • Alberto Bartesaghi
    ResearchOpen Access
    Nature Methods
    Volume: 20, P: 1909-1919

  • Tomographic reconstructions of cryopreserved specimens enable in-situ structural studies. Here, the authors present the beam image-shift electron cryo-tomography (BISECT) approach that accelerates data collection speed and improves the map resolution compared to earlier approaches and present the in vitro structure of a 300 kDa protein complex that was solved at 3.6 Å resolution as a test case.

    • Jonathan Bouvette
    • Hsuan-Fu Liu
    • Alberto Bartesaghi
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11

  • In this study, Henderson and Zhou et al. visualize the development of a HIV-1 broadly neutralizing antibody (bnAb) from germline to maturity by determining cryo-EM structures of HIV-1 Envelope (Env) proteins bound to Fab fragments of antibodies at different stages of development of a Env V3-glcyan supersite targeting bnAb clone.

    • Rory Henderson
    • Ye Zhou
    • Priyamvada Acharya
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • This paper investigates the structure of the HIV glycoprotein gp120 by cryo-electron tomography and molecular modelling. gp120 is analysed in an unliganded state, complexed with a neutralizing antibody and in a CD4 liganded state. The analysis provides insight into the conformational changes that occur with ligand binding.

    • Jun Liu
    • Alberto Bartesaghi
    • Sriram Subramaniam
    Research
    Nature
    Volume: 455, P: 109-113

  • Cryo-electron microscopy and crystal structures of Arabidopsis NPR1—a bird-shaped homodimer—and its complex with the transcription factor TGA3 provide an explanation for a direct role of salicylic acid and enhanceosome assembly in regulating NPR1-dependent gene expression.

    • Shivesh Kumar
    • Raul Zavaliev
    • Pei Zhou
    Research
    Nature
    Volume: 605, P: 561-566

  • Here, using cryo-EM and smFRET, Henderson et al. show how tryptophan 571 in the HIV-1 Env acts as a conformational switch during receptor-mediated viral entry and design HIV-1 Env proteins that cannot undergo conformational changes. This has important implications for HIV-1 vaccine design.

    • Rory Henderson
    • Maolin Lu
    • S. Munir Alam
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-14

  • Cryo-electron microscopy is used to visualize the AMPA receptor GluA2 and the kainate receptor GluK2 in several functional states — having access to so many different structural states has enabled the authors to propose a molecular model for the gating cycle of glutamate receptors.

    • Joel R. Meyerson
    • Janesh Kumar
    • Sriram Subramaniam
    Research
    Nature
    Volume: 514, P: 328-334

  • HIV-1 Env glycoprotein binds receptors on the host cells, triggering a conformational change from a closed to an open state. Now single-particle cryo-EM analysis of a soluble, trimeric Env construct reveals the structure of the closed state at ∼6-Å resolution. The structure features three gp41 helices at the center of the trimer, thus indicating that HIV-1 and influenza viruses use similar mechanisms to enter the cell.

    • Alberto Bartesaghi
    • Alan Merk
    • Sriram Subramaniam
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1352-1357