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 1–6 of 6 results
Advanced filters: Author: Jesper L. Karlsen Clear advanced filters

  • An X-ray crystal structure of sarcoplasmic reticulum Ca2+-ATPase (SERCA) in the presence of sarcolipin, a SERCA regulator, is presented; the structure shows that sarcolipin traps SERCA in a previously unidentified ‘open’ state in which its high-affinity Ca2+-binding sites are unoccupied, but accessible from the cytoplasm.

    • Anne-Marie L. Winther
    • Maike Bublitz
    • Morten J. Buch-Pedersen
    Research
    Nature
    Volume: 495, P: 265-269

  • Here, authors analyse the structural organisation of the large carbon-phosphorus lyase enzyme from bacteria using electron microscopy and discover that it contains two ATP-binding cassette dimers of PhnK and PhnL and opens upon ATP hydrolysis.

    • Søren K. Amstrup
    • Sui Ching Ong
    • Ditlev E. Brodersen
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12

  • Cryo-EM structures of the yeast P4-ATPase Drs2p–Cdc50p in three different states of activation provide insights into the function of this lipid flippase, including mechanisms of autoinhibition and PI4P-dependent activation.

    • Milena Timcenko
    • Joseph A. Lyons
    • Poul Nissen
    Research
    Nature
    Volume: 571, P: 366-370

  • The detailed interactions of membrane proteins with their lipid environment are poorly understood. Sonntaget al. use low-resolution X-ray crystallographic data and molecular dynamics simulations to study the manner in which the sarcoendoplasmic reticulum Ca2+–ATPase adapts to different membrane environments.

    • Yonathan Sonntag
    • Maria Musgaard
    • Lea Thøgersen
    Research
    Nature Communications
    Volume: 2, P: 1-7

  • In plants and fungi, cellular ion homeostasis is powered by the proton pump, a member of the P-type ATPase family. The first X-ray structure of the H+-ATPase is presented, and insight into the mechanism by which protons are transported against an electrochemical gradient is provided

    • Claus Olesen
    • Martin Picard
    • Poul Nissen
    Research
    Nature
    Volume: 450, P: 1036-1042