Zobrazeno 1 - 10
of 15
pro vyhledávání: '"L. Miya Fujimoto"'
Autor:
Kyungsoo Shin, James E. Kent, Alexander E. Aleshin, Ye Tian, L. Miya Fujimoto, Chandan Singh, Francesca M. Marassi
Publikováno v:
Biophysical Journal. 122:467a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40c22e52e83d39c96708f03d797dca23
https://doi.org/10.1016/j.bpj.2022.11.2504
https://doi.org/10.1016/j.bpj.2022.11.2504
Autor:
Francesca M. Marassi, Stanley J. Opella, Sang Ho Park, Samit Kumar Dutta, Yong Yao, Ratan Kumar Rai, L. Miya Fujimoto, Andrey A. Bobkov
Publikováno v:
Journal of Biomolecular NMR. 67:179-190
The outer membrane protein Ail (Adhesion invasion locus) is one of the most abundant proteins on the cell surface of Yersinia pestis during human infection. Its functions are expressed through interactions with a variety of human host proteins, and a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19830e1741747183ef7440926fbedc2a
https://doi.org/10.1007/s10858-017-0094-9
https://doi.org/10.1007/s10858-017-0094-9
Autor:
Kyungsoo Shin, Andrey A. Bobkov, Wonpil Im, Alexander E. Aleshin, James E. Kent, Ye Tian, Francesca M. Marassi, L. Miya Fujimoto
Publikováno v:
Biophysical Journal. 120:202a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ecee5961440e63ffb0fa87956239b33f
https://doi.org/10.1016/j.bpj.2020.11.1384
https://doi.org/10.1016/j.bpj.2020.11.1384
Autor:
Yong Yao, Kyungsoo Shin, Chandan Singh, James E. Kent, L. Miya Fujimoto, Francesca M. Marassi
Publikováno v:
Biophysical Journal. 118:210a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a0ed01e577e216febf1014aabb377685
https://doi.org/10.1016/j.bpj.2019.11.1257
https://doi.org/10.1016/j.bpj.2019.11.1257
Autor:
Yong Yao, Ye Tian, L. Miya Fujimoto, Francesca M. Marassi, Chandan Singh, Kyungsoo Shin, Luz M. Meneghini
Publikováno v:
Biophysical Journal. 116:474a-475a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6aafec0408e463cbe9b7a46278dc6d35
https://doi.org/10.1016/j.bpj.2018.11.2562
https://doi.org/10.1016/j.bpj.2018.11.2562
Autor:
Vishal Jain, Gregory V. Plano, Sara Schesser Bartra, Francesca M. Marassi, L. Miya Fujimoto, Joshua G. Ring, Yi Ding, Sanjay Ram
Publikováno v:
Microbiology. 161:2174-2183
Yersinia pestis, the agent of plague, requires the Ail (attachment invasion locus) outer membrane protein to survive in the blood and tissues of its mammalian hosts. Ail is important for both attachment to host cells and for resistance to complement-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63e1315dd182b5d572d45e6bf063a5ea
https://doi.org/10.1099/mic.0.000179
https://doi.org/10.1099/mic.0.000179
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1848:712-720
The surrounding environment has significant consequences for the structural and functional properties of membrane proteins. While native structure and function can be reconstituted in lipid bilayer membranes, the detergents used for protein solubiliz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e4ecf6c7c288258973e48120655dc10
https://doi.org/10.1016/j.bbamem.2014.11.021
https://doi.org/10.1016/j.bbamem.2014.11.021
Publikováno v:
Journal of Biomolecular NMR. 61:275-286
Solid-state NMR studies of sedimented soluble proteins has been developed recently as an attractive approach for overcoming the size limitations of solution NMR spectroscopy while bypassing the need for sample crystallization or precipitation (Bertin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d24959840cc8baa249ad82b11203e830
https://doi.org/10.1007/s10858-014-9893-4
https://doi.org/10.1007/s10858-014-9893-4
Publikováno v:
Biophysical Journal. 114:403a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9690a9c211a86982fdfcf4171e29d239
https://doi.org/10.1016/j.bpj.2017.11.2236
https://doi.org/10.1016/j.bpj.2017.11.2236
Publikováno v:
Traffic. 1:161-171
Three cell-permeant compounds, cytochalasin D, latrunculin A and jasplakinolide, which perturb intracellular actin dynamics by distinct mechanisms, were used to probe the role of filamentous actin and actin assembly in clathrin-mediated endocytosis i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::267c6785695b3746a83feca1dda0e73d
https://doi.org/10.1034/j.1600-0854.2000.010208.x
https://doi.org/10.1034/j.1600-0854.2000.010208.x