Zobrazeno 1 - 10
of 222
pro vyhledávání: '"T Eger"'
Publikováno v:
PLoS ONE, Vol 12, Iss 1, p e0169390 (2017)
The seasonal profession of wildland fire fighting in Canada requires individuals to work in harsh environmental conditions that are physically demanding. The purpose of this study was to use novel technologies to evaluate the physiological demands an
Externí odkaz:
https://doaj.org/article/85fe06f58471472dbc30362849d13ea3
Akademický článek
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Akademický článek
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Akademický článek
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Autor:
D. von Stetten, Takefumi Morizumi, Saeed Oghbaey, Henrike M. Müller-Werkmeister, Pedram Mehrabi, Robin L. Owen, Friedjof Tellkamp, D.A. Sherrell, Robert Bücker, Danny Axford, R.J.D. Miller, H. Schikora, Gleb Bourenkov, Eric Schulz, S. Meier, O. Pare´-Labrosse, Emil F. Pai, Wei-Lin Ou, Oliver P. Ernst, A. Kuo, Bryan T. Eger, Andreas Marx, Antoine Sarracini, Jessica E. Besaw, Helen M. Ginn
Publikováno v:
Science Advances
Science advances 7(12), eabf1380-(2021). doi:10.1126/sciadv.abf1380
Science advances 7(12), eabf1380-(2021). doi:10.1126/sciadv.abf1380
Science advances 7(12), eabf1380 - (2021). doi:10.1126/sciadv.abf1380
For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) an
For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff5316a54ce9be7c377c486856d487d9
https://pubmed.ncbi.nlm.nih.gov/33731353
https://pubmed.ncbi.nlm.nih.gov/33731353
Autor:
Antoine Sarracini, Olivier Paré-Labrosse, Jessica E. Besaw, Henrike M. Müller-Werkmeister, Takefumi Morizumi, D. von Stetten, R.J.D. Miller, Pedram Mehrabi, H. Schikora, Wei-Lin Ou, Robert Bücker, Robin L. Owen, Emil F. Pai, Friedjof Tellkamp, Helen M. Ginn, Oliver P. Ernst, Gleb Bourenkov, Eric Schulz, A. Kuo, Bryan T. Eger, S. Meier, Andreas Marx, Danny Axford, D.A. Sherrell, Saeed Oghbaey
For the two proteins myoglobin (MB) and fluoroacetate dehalogenase (FAcD), we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize compara
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91de657e1f6629615ba8764c9dae49b2
https://doi.org/10.1101/2020.08.21.257170
https://doi.org/10.1101/2020.08.21.257170
Autor:
Andrew Harris, Bryan T. Eger, Jessica H.Y. Chu, R. J. Dwayne Miller, Wei-Lin Ou, Takefumi Morizumi, Jessica E. Besaw, Leonid S. Brown, Oliver P. Ernst, Juan Diego Sanchez Vasquez
Publikováno v:
J Biol Chem
Microbial rhodopsins are versatile and ubiquitous retinal-binding proteins that function as light-driven ion pumps, light-gated ion channels, and photosensors, with potential utility as optogenetic tools for altering membrane potential in target cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21ce416815b5bb82cce3c57e8a5de1d3
https://pubmed.ncbi.nlm.nih.gov/32703899
https://pubmed.ncbi.nlm.nih.gov/32703899
Autor:
Jennings Luu, Christopher L. Sander, MinSoung Kang, Ho-Jun Lee, Hui-Woog Choe, Krzysztof Palczewski, Philip D. Kiser, Oliver P. Ernst, Joerg Reichenwallner, Bryan T. Eger, Kiyoung Jang, Yong Ju Kim, Kyumhyuk Kim, Dorothea Fiedler, David Furkert
Publikováno v:
Structure (London, England : 1993), vol 30, iss 2
Structure
Structure
Summary Visual arrestin (Arr1) terminates rhodopsin signaling by blocking its interaction with transducin. To do this, Arr1 translocates from the inner to the outer segment of photoreceptors upon light stimulation. Mounting evidence indicates that in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb806005f63ebd872a964016fd740dcf
https://doi.org/10.1016/j.str.2021.10.002
https://doi.org/10.1016/j.str.2021.10.002
Publikováno v:
Der Nervenarzt. 90:503-508
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e6dce7f00831daa283dd3dad5adfff7
https://doi.org/10.1007/s00115-018-0570-9
https://doi.org/10.1007/s00115-018-0570-9
Autor:
Siavash Vahidi, Elisa Leung, Emil F. Pai, Bryan T. Eger, Sadhna Phanse, Yu-Qian Mao, Vaibhav Bhandari, Mark F. Mabanglo, Jin Lin Zhou, Marim M Barghash, Robert A. Batey, Mohan Babu, Kamran Rizzolo, Thiago V. Seraphim, Steve Bryson, Walid A. Houry, Carlos H.I. Ramos, Lewis E. Kay, Leandro R.S. Barbosa, Jordan D. Goodreid
Publikováno v:
Communications Biology
Communications Biology, Vol 2, Iss 1, Pp 1-14 (2019)
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Communications Biology, Vol 2, Iss 1, Pp 1-14 (2019)
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Bacterial ClpP is a highly conserved, cylindrical, self-compartmentalizing serine protease required for maintaining cellular proteostasis. Small molecule acyldepsipeptides (ADEPs) and activators of self-compartmentalized proteases 1 (ACP1s) cause dys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a967e1194914b15faf9c871e9f024bbf
https://doi.org/10.1038/s42003-019-0656-3
https://doi.org/10.1038/s42003-019-0656-3