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Showing 1–19 of 19 results
Advanced filters: Author: Wesley I. Sundquist Clear advanced filters

  • Recent NMR structures of bovine immunodeficiency viral TAR RNA–Tat peptide complexes have revealed a new β-hairpin RNA recognition motif. These complexes exhibit intriguing new variations on the recurring themes in nucleic acid recognition.

    • Wesley I. Sundquist
    News & Views
    Nature Structural Biology
    Volume: 3, P: 8-11

  • The microtubule interacting and tarnsport (MIT) domain of Vps4 binds conserved residues in the CHMP1-3 class of ESCRT-III proteins. These results reveal how Vps4 recognises substrates to facilitate membrane fission events required for viral release and endosomal vesicles

    • Melissa D. Stuchell-Brereton
    • Jack J. Skalicky
    • Wesley I. Sundquist
    Research
    Nature
    Volume: 449, P: 740-744

  • Three papers show that Vipp1, a plastid ESCRT-III protein, can form sheets, spirals and regular polygons on flat membranes and tubulate the membranes within stacked rings and helices. This work provides a framework for how Vipp1 can deliver lipids for thylakoid membrane biogenesis and protect and repair the membranes during photosynthesis.

    • John McCullough
    • Wesley I. Sundquist
    News & Views
    Nature Structural & Molecular Biology
    Volume: 32, P: 414-417

  • Affinity tagging, mass spectroscopy and a tailor-made scoring system are used to identify 497 high-confidence interactions between human proteins and human immunodeficiency virus proteins.

    • Stefanie Jäger
    • Peter Cimermancic
    • Nevan J. Krogan
    Research
    Nature
    Volume: 481, P: 365-370

  • The sorting and degradation of cell-surface proteins are essential for cellular homeostasis. The ESCRT-I complex is known to be involved in these events, and new structural findings elucidate its core architecture.

    • Steven L. Alam
    • Wesley I. Sundquist
    News & Views
    Nature
    Volume: 447, P: 921-922

  • Cryo-EM structures of human ESCRT-III proteins forming membrane-bound and membrane-free filaments show how CHMP1B and IST1 polymerize sequentially, driving membrane tubulation, constriction and bilayer thinning, leading to membrane fission.

    • Henry C. Nguyen
    • Nathaniel Talledge
    • Adam Frost
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 392-399

  • ESCRT-III proteins play important roles in multivesicular body (MVB) formation, cytokinesis, and enveloped virus budding. The structure of Ist1, which also functions in cytokinesis and MVB sorting, reveals that it, too, is an ESCRT-III family member and suggests that this protein family uses a common mode of autoinhibition.

    • Monika Bajorek
    • Heidi L Schubert
    • Wesley I Sundquist
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 754-762

  • Two complementary papers demonstrate that the homologous type II transmembrane proteins LAP1 and LULL1 adopt nucleotide-free AAA+ ATPase folds and donate arginine fingers to complete the active sites of Torsin AAA+ ATPases. Activated Torsin complexes appear to function in nuclear and endoplasmic reticulum membrane-remodeling processes, including a nuclear vesiculation pathway that carries large cellular and viral cargoes from the nucleus into the cytoplasm.

    • John McCullough
    • Wesley I Sundquist
    News & Views
    Nature Structural & Molecular Biology
    Volume: 21, P: 1025-1027

  • A powerful arm of the cellular defence against microbial invaders has been characterized. APOBEC3G, a protein that can fight off HIV, works by introducing 'typographical errors' during viral replication.

    • Yapeng Gu
    • Wesley I. Sundquist
    News & Views
    Nature
    Volume: 424, P: 21-22

  • Two new crystal structures of ubiquitin (Ub) in complex with fragments of the endosomal proteins Rabex-5 and HRS show intriguing new modes of Ub binding and reveal that both fragments can bind two Ub molecules simultaneously.

    • Steven L Alam
    • Wesley I Sundquist
    News & Views
    Nature Structural & Molecular Biology
    Volume: 13, P: 186-188