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Showing 1–14 of 14 results
Advanced filters: Author: Gregory Effantin Clear advanced filters

  • Cilia are composed of microtubule doublets, but how they assemble is unclear. Here, the authors show that the brain-specific MAP6d1, found in neuronal primary cilia, assembles doublet microtubules and forms protofilaments inside microtubules.

    • Dharshini Gopal
    • Juliette Wu
    • Isabelle Arnal
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Human adenoviruses (HAd) cause respiratory, gastrointestinal and ocular infections. Here, the authors provide insights into the early stages of adenovirus infection by determining the cryo-EM structure of the trimeric HAd type 3 fibre knob bound to its cellular receptor human desmoglein 2, which reveals residues critical for HAd-receptor interactions.

    • Emilie Vassal-Stermann
    • Gregory Effantin
    • Pascal Fender
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-7

  • Only praziquantel is available for treating schistosomiasis, a disease affecting >200 million people. Here, the authors identify compounds active against schistosome infections meeting the criteria for lead progression indicated by WHO with better activity against juvenile worms than praziquantel.

    • Valentina Z. Petukhova
    • Sammy Y. Aboagye
    • Pavel A. Petukhov
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • RNA-dependent RNA polymerases from segmented negative stranded RNA viruses catalyze genome replication and viral transcription. Here, the authors present the cryo-EM structure of full-length La Crosse virus polymerase and structurally characterize the pre-initiation and elongation states, which is of interest for the development of polymerase inhibitors.

    • Benoît Arragain
    • Grégory Effantin
    • Hélène Malet
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • The cryo-EM structures of ESCRT-III CHMP2A and CHMP3 filaments reveal their mode of polymerization and interaction with negatively curved membrane. VPS4 constricts and cleaves the ESCRT-III CHMP2A–CHMP3 membrane tubes, thus acting as a minimal membrane fission machinery.

    • Kimi Azad
    • Delphine Guilligay
    • Winfried Weissenhorn
    Research
    Nature Structural & Molecular Biology
    Volume: 30, P: 81-90

  • Host cell recognition is mediated by the phage tail tip proteins, which then triggers viral genome delivery via the phage tail. Here, the authors combine crystallography and cryoEM to structurally characterise the bacteriophage T5 tail tube structure before and after interaction with its host receptor.

    • Charles-Adrien Arnaud
    • Grégory Effantin
    • Cécile Breyton
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-9

  • Here the authors report the cryo-EM structure of a triple-mutant of the anti-microbial peptide plectasin, PPI42, assembling in a pH- and concentration dependent manner into helical non-amyloid fibrils. The fibrils formation is reversible, and follows a sigmoidal kinetics. The fibrils adopt a right-handed helical superstructure composed by two protofilaments, stabilized by an outer hydrophobic ring and an inner hydrophobic centre. These findings reveal that α/β proteins can natively assemble into fibrils.

    • Christin Pohl
    • Gregory Effantin
    • Pernille Harris
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-15

  • NMR structure determination is challenging for proteins with a molecular weight above 30 kDa and atomic-resolution structure determination from cryo-EM data is currently not the rule. Here the authors describe an integrated structure determination approach that simultaneously uses NMR and EM data and allows them to determine the structure of the 468 kDa dodecameric aminopeptidase TET2 complex.

    • Diego F. Gauto
    • Leandro F. Estrozi
    • Jerome Boisbouvier
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12

  • Vps4 is a AAA+ family protein involved in the disassembly of ESCRT-III polymers during membrane fission events such as occur during HIV budding. Here the authors propose a structure-based model of how the conformational flexibility of Vps4 can be translated into mechanical forces to disassemble ESCRT-III during membrane fission.

    • Christophe Caillat
    • Pauline Macheboeuf
    • Patricia Renesto
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-12

  • The retromer is a complex of Vacuolar protein sorting proteins that mediate retrieval of lysosomal hydrolases from endosomes to the trans golgi network. The human retromer complex can be separated into two smaller complexes, a membrane targeting sorting nexin dimer and a heterotrimeric cargo recognition complex. New and previously solved structures, bioinformatics, interaction studies, molecular modelling and electron microscopy of the entire complex are combined to develop a structural model of the complex.

    • Aitor Hierro
    • Adriana L. Rojas
    • James H. Hurley
    Research
    Nature
    Volume: 449, P: 1063-1067