Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Susanne F. Fenz"'
Publikováno v:
Communications Physics, Vol 6, Iss 1, Pp 1-10 (2023)
Abstract The narrow escape theory (NET) predicts the escape time distribution of Brownian particles confined to a domain with reflecting borders except for one small window. Applications include molecular activation events in cell biology and biophys
Externí odkaz:
https://doaj.org/article/9f6e5971f6ad4c9790152501b9fd599a
Autor:
Andreas J. W. Hartel, Marius Glogger, Nicola G. Jones, Wasim Abuillan, Christopher Batram, Anne Hermann, Susanne F. Fenz, Motomu Tanaka, Markus Engstler
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
How molecular crowding affects membrane protein diffusion and function is not known. Here the authors measure diffusion of variant surface glycoprotein on trypanosomes and discover a molecular crowding threshold that limits diffusion, and find that N
Externí odkaz:
https://doaj.org/article/831b8d33c8d54ce4a633cf358d818285
Autor:
Ana-Sunčana Smith, Kheya Sengupta, Udo Seifert, Timo Bihr, Susanne F. Fenz, Rudolf Merkel, Erich Sackmann
Publikováno v:
Biophysical Journal. 107(11):L33-L36
Thus far, understanding how the confined cellular environment affects the lifetime of bonds, as well as the extraction of complexation rates, has been a major challenge in studies of cell adhesion. Based on a theoretical description of the growth cur
Publikováno v:
Biophysical journal. 112(11)
Molecular recruitment into functional domains in the cell plasma membrane is an important prerequisite for many cellular processes, such as cell signaling, cell-matrix adhesion, or the formation of synapses. High precision measurements of the origin
Autor:
Rudolf Merkel, Udo Seifert, Susanne F. Fenz, Ana-Sunčana Smith, Timo Bihr, Kheya Sengupta, Daniel Schmidt
Publikováno v:
Nature physics 13, 906–913 (2017). doi:10.1038/nphys4138
Nature Physics
Nature Physics, 2017, 13 (9), pp.906-913. ⟨10.1038/NPHYS4138⟩
Nature Physics, Nature Publishing Group, 2017, 13 (9), pp.906-913. ⟨10.1038/NPHYS4138⟩
Nature Physics
Nature Physics, 2017, 13 (9), pp.906-913. ⟨10.1038/NPHYS4138⟩
Nature Physics, Nature Publishing Group, 2017, 13 (9), pp.906-913. ⟨10.1038/NPHYS4138⟩
The integrity of living tissues is maintained by adhesion domains of trans-bonds formed between cadherin proteins residing on opposing membranes of neighbouring cells. These domains are stabilized by lateral cis-interactions between the cadherins on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf095a3df5deda05b77b9a13a1167140
https://hdl.handle.net/2128/15921
https://hdl.handle.net/2128/15921
Autor:
Susanne F. Fenz, Marius Glogger, Jochen Kuper, Nicola G. Jones, Thomas Bartossek, Mark Carrington, Mislav Cvitković, Christin Schäfer, Ana-Sunčana Smith, Markus Engstler, Helen R. Mott, Martha Brennich, Caroline Kisker
The most prominent defence of the unicellular parasite Trypanosoma brucei against the host immune system is a dense coat that comprises a variant surface glycoprotein (VSG). Despite the importance of the VSG family, no complete structure of a VSG has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80b0978de91ea62bd23dc6d22ee7e898
https://doi.org/10.1038/s41564-017-0013-6
https://doi.org/10.1038/s41564-017-0013-6
Autor:
Marius Glogger, Motomu Tanaka, Anne Hermann, Andreas Hartel, Markus Engstler, Christopher Batram, Susanne F. Fenz, Nicola G. Jones, Wasim Abuillan
Publikováno v:
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
The protein density in biological membranes can be extraordinarily high, but the impact of molecular crowding on the diffusion of membrane proteins has not been studied systematically in a natural system. The diversity of the membrane proteome of mos
Autor:
Kheya Sengupta, Susanne F. Fenz, Udo Seifert, Daniel Schmidt, Ana-Sunčana Smith, Timo Bihr, Rudolf Merkel
Publikováno v:
Biophysical Journal
Biophysical Journal, Biophysical Society, 2016, 110 (3, 1), pp.190A. ⟨10.1016/j.bpj.2015.11.1058⟩
Biophysical Journal, 2016, 110 (3, 1), pp.190A. ⟨10.1016/j.bpj.2015.11.1058⟩
Biophysical Journal, Biophysical Society, 2016, 110 (3, 1), pp.190A. ⟨10.1016/j.bpj.2015.11.1058⟩
Biophysical Journal, 2016, 110 (3, 1), pp.190A. ⟨10.1016/j.bpj.2015.11.1058⟩
Cadherins are major cell-cell adhesion molecules in vertebrate tissue. They play a vital role in the development and maintenance of multicellular organisms. Cadherins show homophilic as well as heterophilic binding to members of their subfamily with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39689fdbc8c90dd290d3b097e00b80d0
https://hal.archives-ouvertes.fr/hal-01452673
https://hal.archives-ouvertes.fr/hal-01452673
Publikováno v:
Biophysical Journal. 114:537a
Autor:
Gernot Guigas, Nicola G. Jones, Susanne F. Fenz, Matthias Weiss, Andreas Hartel, Markus Engstler, Marius Glogger
Publikováno v:
Scientific Reports
A plethora of proteins undergo random and passive diffusion in biological membranes. While the contribution of the membrane-embedded domain to diffusion is well established, the potential impact of the extra-membrane protein part has been largely neg