Novel Tools in Determining the Physiological Demands and Nutritional Practices of Ontario FireRangers during Fire Deployments.

Autor: A H Robertson, C Larivière, C R Leduc, Z McGillis, T Eger, A Godwin, M Larivière, S C Dorman

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

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Serial femtosecond and serial synchrotron crystallography yield data of equivalent quality: a systematic comparison

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

Structural evidence for visual arrestin priming via complexation of phosphoinositols

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

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

ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores

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

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