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Showing 1–14 of 14 results
Advanced filters: Author: Samuel H. Gellman Clear advanced filters

  • The X-ray crystal structure of the human β2 adrenergic receptor, a G-protein-coupled receptor, in an agonist-bound 'active' state is solved. Comparison of this structure with a previously published structure of the same GPCR in an inactive state indicates that minor changes in the binding pocket of the protein lead to major changes elsewhere — there is a large outward movement of the cytoplasmic end of one of the transmembrane segments and rearrangements of two other transmembrane segments. This structure provides insights into the process of agonist binding and activation.

    • Søren G. F. Rasmussen
    • Hee-Jung Choi
    • Brian K. Kobilka
    Research
    Nature
    Volume: 469, P: 175-180

  • Current parathyroid hormone (PTH) peptides have limited efficacy due to rapid clearance and short receptor binding. Here, the authors show that lipidation strategies can extend circulation time and receptor engagement, enhancing PTH peptide efficacy in vitro and in vivo

    • Jakob Höppner
    • Hiroshi Noda
    • Thomas J. Gardella
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16

  • Chemical force microscopy measurements show that the immobilization of specific cationic groups near non-polar domains produces pronounced changes in the domains’ hydrophobic interaction strengths: charged ammonium groups double interaction strengths, whereas guanidinium groups eliminate measurable interactions.

    • C. Derek Ma
    • Chenxuan Wang
    • Nicholas L. Abbott
    Research
    Nature
    Volume: 517, P: 347-350

  • A new 20-residue peptide represents the smallest example to date of cooperatively folded tertiary structure. This achievement provides a new tool for elucidating protein conformational preferences. The mini-protein should serve as a fruitful platform for protein design.

    • Samuel H. Gellman
    • Derek N. Woolfson
    News & Views
    Nature Structural Biology
    Volume: 9, P: 408-410

  • Parathyroid hormone/parathyroid hormone-related peptide receptor (PTHR1) is a family B G-protein-coupled receptor and is involved in the regulation of skeletal development, bone turnover and mineral ion homeostasis. This Review discusses fundamental aspects of ligand-binding and signalling mechanisms at PTHR1, highlighting the relationship between ligand structural modification and variation in PTHR1 signalling responses. The action of these signalling mechanisms in disease states in which PTHR1 function has an important role are also discussed.

    • Ross W. Cheloha
    • Samuel H. Gellman
    • Thomas J. Gardella
    Reviews
    Nature Reviews Endocrinology
    Volume: 11, P: 712-724

  • An integrated analysis of over 100 single-cell and single-nucleus transcriptomics studies illustrates severe acute respiratory syndrome coronavirus 2 viral entry gene coexpression patterns across different human tissues, and shows association of age, smoking status and sex with viral entry gene expression in respiratory cell populations.

    • Christoph Muus
    • Malte D. Luecken
    • Xiaohui Zhang
    Research
    Nature Medicine
    Volume: 27, P: 546-559

  • The X-ray crystal structure of the human β2 adrenergic receptor, a G-protein-coupled receptor (GPCR), covalently bound to a small-molecule agonist is solved. Comparison of this structure with structures of this GPCR in an inactive state and in an antibody-stabilized active state reveals how binding events at both the extracellular and intracellular surfaces stabilize the active conformation of the receptor. Molecular dynamics simulations suggest that the agonist-bound active state spontaneously relaxes to an inactive-like state in the absence of a G protein.

    • Daniel M. Rosenbaum
    • Cheng Zhang
    • Brian K. Kobilka
    Research
    Nature
    Volume: 469, P: 236-240