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: Tristan I. Croll Clear advanced filters

  • An analysis of AlphaFold protein structure predictions shows that while in many cases the predictions are highly accurate, there are also many instances where the predicted structures or parts of predicted structures do not agree with experimentally resolved data. Therefore, care must be taken when using these predictions for informing structural hypotheses.

    • Thomas C. Terwilliger
    • Dorothee Liebschner
    • Paul D. Adams
    ResearchOpen Access
    Nature Methods
    Volume: 21, P: 110-116

  • This paper presents an iterative procedure where AlphaFold models are automatically rebuilt on the basis of experimental density maps and the rebuilt models are used as templates in new AlphaFold predictions.

    • Thomas C. Terwilliger
    • Billy K. Poon
    • Paul D. Adams
    ResearchOpen Access
    Nature Methods
    Volume: 19, P: 1376-1382

  • YenTcA is the pore-forming and membrane binding subunit of the ABC toxin YenTc, which is produced by the insect pathogen Yersinia entomophaga. Here authors present cryo-EM structures of YenTcA purified from the native source which implicate associated endochitinases in host cell recognition.

    • Sarah J Piper
    • Lou Brillault
    • Michael J Landsberg
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12

  • MAL and MyD88 are downstream adaptors of Toll-like receptors (TLR) and the MAL TIR domain forms filaments in vitro, which in turn nucleate the assembly of crystalline arrays of the MyD88 TIR domain. Here, the authors present the structure of these MyD88 TIR crystalline arrays solved by both microcrystal electron diffraction and serial femtosecond crystallography, and they show with mutagenesis experiments that MyD88 interface residues are important for TLR4 signaling in vivo.

    • Max T. B. Clabbers
    • Susannah Holmes
    • Thomas Ve
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • Cryo-electron microscopy structures of the luteinizing hormone–choriogonadotropin receptor (LHCGR), in complex with Gs and in various states of activation, reveal a distinct mechanism of receptor activation, with implications for drug discovery.

    • Jia Duan
    • Peiyu Xu
    • H. Eric Xu
    Research
    Nature
    Volume: 598, P: 688-692

  • Here, the authors evaluate the performance of AlphaFold2 and its predicted structures on common structural biological applications, including missense variants, function and ligand binding site prediction, modeling of interactions and modeling of experimental structural data.

    • Mehmet Akdel
    • Douglas E. V. Pires
    • Pedro Beltrao
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 1056-1067

  • The catalytic domains in nonribosomal peptide synthetases (NRPSs) are responsible for a choreography of events that elongates substrates into natural products. Here, the authors present cryo-EM structures of a siderophore-producing dimeric NRPS elongation module in multiple distinct conformations, which provides insight into the mechanisms of catalytic trajectory.

    • Jialiang Wang
    • Dandan Li
    • Zhijun Wang
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • A survey of SARS-CoV-2 RBD antibodies identifies those with activity against diverse SARS-CoV-2 variants and SARS-related coronaviruses, highlighting epitopes and features to prioritize in antibody and vaccine development.

    • Tyler N. Starr
    • Nadine Czudnochowski
    • Gyorgy Snell
    Research
    Nature
    Volume: 597, P: 97-102

  • Structural insight into TIR-domain interactions, which are essential for the recruitment of signaling adapters to Toll-like receptors during innate immune responses, demonstrates a conserved interaction mode involved in both TLR and IL-1R signaling.

    • Thomas Ve
    • Parimala R Vajjhala
    • Bostjan Kobe
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 743-751

  • Structural biology plays a crucial role in the fight against COVID-19, permitting us to ‘see’ and understand SARS-CoV-2. However, the macromolecular structures of SARS-CoV-2 proteins that were solved with great speed and urgency can contain errors that may hinder drug design. The Coronavirus Structural Task Force has been working behind the scenes to evaluate and improve these structures, making the results freely available at https://insidecorona.net/.

    • Tristan I. Croll
    • Kay Diederichs
    • Andrea Thorn
    Comments & Opinion
    Nature Structural & Molecular Biology
    Volume: 28, P: 404-408