Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Björn O. Forsberg"'
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract Cryo electron microscopy (cryo-EM) is used by biological research to visualize biomolecular complexes in 3D, but the heterogeneity of cryo-EM reconstructions is not easily estimated. Current processing paradigms nevertheless exert great effo
Externí odkaz:
https://doaj.org/article/68f9eef138814e649491e4b4f49f129d
Publikováno v:
IUCrJ, Vol 4, Iss 6, Pp 723-727 (2017)
The introduction of direct detectors and the automation of data collection in cryo-EM have led to a surge in data, creating new opportunities for advancing computational processing. In particular, on-the-fly workflows that connect data collection wit
Externí odkaz:
https://doaj.org/article/9ac30ee046bb42b0bb374c25ac6bd725
Autor:
Jasenko Zivanov, Takanori Nakane, Björn O Forsberg, Dari Kimanius, Wim JH Hagen, Erik Lindahl, Sjors HW Scheres
Publikováno v:
eLife, Vol 7 (2018)
Here, we describe the third major release of RELION. CPU-based vector acceleration has been added in addition to GPU support, which provides flexibility in use of resources and avoids memory limitations. Reference-free autopicking with Laplacian-of-G
Externí odkaz:
https://doaj.org/article/75a3cbbc12fd49f7b6239eb7c778a385
Autor:
Pranav N.M. Shah, James B. Gilchrist, Björn O. Forsberg, Alister Burt, Andrew Howe, Shyamal Mosalaganti, William Wan, Julika Radecke, Yuriy Chaban, Geoff Sutton, David I. Stuart, Mark Boyce
Publikováno v:
Cell Host & Microbe. 31:604-615.e4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::adc7befdec20e0e6a58655db07b163c1
https://doi.org/10.1016/j.chom.2023.03.004
https://doi.org/10.1016/j.chom.2023.03.004
Publikováno v:
eLife, Vol 5 (2016)
By reaching near-atomic resolution for a wide range of specimens, single-particle cryo-EM structure determination is transforming structural biology. However, the necessary calculations come at large computational costs, which has introduced a bottle
Externí odkaz:
https://doaj.org/article/1431a1ad2d13425b881afbedce1a6fa5
Autor:
Urska Rovsnik, Björn O. Forsberg, Linnea Yvonnesdotter, Rebecca J. Howard, Yuxuan Zhuang, Marta Carroni, Erik Lindahl
Publikováno v:
Life Science Alliance
Cryo-EM structures and molecular simulations of a pentameric ligand-gated ion channel, GLIC, in resting and activating conditions implicate protonation sites and altered dynamics in sequential gating.
Ligand-gated ion channels are critical media
Ligand-gated ion channels are critical media
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e849371350bf1bec49e4319280c89e5
http://europepmc.org/articles/PMC8326787
http://europepmc.org/articles/PMC8326787
The pyruvate dehydrogenase complex (PDC) is a central component of all aerobic respiration, connecting glycolysis to mitochondrial oxidation of pyruvate. Despite its central metabolic role, its precise composition and means of regulation remain unkno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0111f0c496f058e4a8dac754ee8e18d6
https://doi.org/10.1101/2020.08.13.232140
https://doi.org/10.1101/2020.08.13.232140
Autor:
Linnea S. Axelsson, Urska Rovsnik, Rebecca J. Howard, Victoria T. Lim, Björn O. Forsberg, Christian Blau, Marta Carroni, Erik Lindahl, Yuxuan Zhuang
Ligand-gated ion channels are critical mediators of electrochemical signal transduction across evolution. Biophysical and pharmacological development in this family relies on high-quality structural data in multiple, subtly distinct functional states
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::864880c6bf2b05da2f3df0aca12fc418
https://doi.org/10.1101/2020.06.19.161356
https://doi.org/10.1101/2020.06.19.161356
Autor:
Linnea S. Axelsson, Urska Rovsnik, Rebecca J. Howard, Christian Blau, Marta Carroni, Erik Lindahl, Björn O. Forsberg, Yuxuan Zhuang
Publikováno v:
Biophysical Journal. 120:192a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c62feb604a670cbaba4af8053b9ff4d6
https://doi.org/10.1016/j.bpj.2020.11.1321
https://doi.org/10.1016/j.bpj.2020.11.1321
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
Nature Communications
Nature Communications
The pyruvate dehydrogenase complex (PDC) is a multienzyme complex central to aerobic respiration, connecting glycolysis to mitochondrial oxidation of pyruvate. Similar to the E3-binding protein (E3BP) of mammalian PDC, PX selectively recruits E3 to t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb63feb15fc0b16c9db4e958d2075eb9
https://doi.org/10.1016/j.bpj.2020.11.1225
https://doi.org/10.1016/j.bpj.2020.11.1225