Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Jonathan Khao"'
Autor:
Tara C. Marcink, Thomas Kicmal, Emily Armbruster, Zhening Zhang, Gillian Zipursky, Kate L. Golub, Mohab Idris, Jonathan Khao, Jennifer Drew-Bear, Gael McGill, Tom Gallagher, Matteo Porotto, Amédée des Georges, Anne Moscona
Publikováno v:
Science advances. 8(33)
SARS-CoV-2 cell entry is completed after viral spike (S) protein–mediated membrane fusion between viral and host cell membranes. Stable prefusion and postfusion S structures have been resolved by cryo–electron microscopy and cryo–electron tomog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3c0dd7eb0cf7e1adfe8f67a97eb05eb
https://pubmed.ncbi.nlm.nih.gov/35984891
https://pubmed.ncbi.nlm.nih.gov/35984891
Autor:
Rory D. de Vries, Sander Herfst, Barry Rockx, Camilla Predella, Rik L. de Swart, Kyle Stearns, Jonathan Khao, Samuel H. Gellman, Anne Moscona, Danny Noack, Gaël McGill, Bart L. Haagmans, N. Valerio Dorrello, Matteo Porotto, Francesca T. Bovier, Christopher A. Alabi, Sudipta Biswas, Jennifer Drew-Bear, Katharina S. Schmitz
Publikováno v:
Science, 371(6536), 1379-1382. American Association for the Advancement of Science
Science (New York, N.y.)
Science (New York, N.y.)
Halting transmission The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S) glycoprotein binds to host cells and initiates membrane fusion and cell infection. This stage in the virus life history is currently a target for drug inh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb3ce9eda821bff8423c3e97ae255580
https://doi.org/10.1126/science.abf4896
https://doi.org/10.1126/science.abf4896
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2017, 1859 (1), pp.126-134. ⟨10.1016/j.bbamem.2016.10.014⟩
Biochimica et Biophysica Acta:Biomembranes, 2017, 1859 (1), pp.126-134. ⟨10.1016/j.bbamem.2016.10.014⟩
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2017, 1859 (1), pp.126-134. ⟨10.1016/j.bbamem.2016.10.014⟩
Biochimica et Biophysica Acta:Biomembranes, 2017, 1859 (1), pp.126-134. ⟨10.1016/j.bbamem.2016.10.014⟩
International audience; Understanding how membrane proteins interact with their environment is fundamental to the understanding of their structure, function and interactions. We have performed coarse-grained molecular dynamics simulations on a series
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acb46512ae6afccba952ebd004bf12a5
https://doi.org/10.1016/j.bbamem.2016.10.014
https://doi.org/10.1016/j.bbamem.2016.10.014
Autor:
Pierre Hubert, James N. Sturgis, Paul Sawma, Jean-Pierre Duneau, Jonathan Khao, Dominique Bagnard, Jélerôme Hénin
Publikováno v:
Cell Adhesion & Migration. 4:313-324
As a whole, integral membrane proteins represent about one third of sequenced genomes, and more than 50% of currently available drugs target membrane proteins, often cell surface receptors. Some membrane protein classes, with a defined number of tran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c71ae243e047ba1d377041b1e8280f16
https://doi.org/10.4161/cam.4.2.12430
https://doi.org/10.4161/cam.4.2.12430
Autor:
Mohamed Husain, Ignacio Casuso, Jean-Pierre Duneau, Simon Scheuring, James N. Sturgis, Perrine Paul-Gilloteaux, Jonathan Khao, Henning Stahlberg, Mohamed Chami
Publikováno v:
Nature Nanotechnology
Nature Nanotechnology, Nature Publishing Group, 2012, pp.525-529. ⟨10.1038/nnano.2012.109⟩
Nature Nanotechnology, 2012, 7, pp.525-529. ⟨10.1038/nnano.2012.109⟩
Nature nanotechnology
Nature Nanotechnology, Nature Publishing Group, 2012, pp.525-529. ⟨10.1038/nnano.2012.109⟩
Nature Nanotechnology, 2012, 7, pp.525-529. ⟨10.1038/nnano.2012.109⟩
Nature nanotechnology
International audience; For cells to function properly, membrane proteins must be able to diffuse within biological membranes. The functions of these membrane proteins depend on their position and also on protein-protein and protein-lipid interaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10c4dca3ace1eb2d2f16a0c1195558b3
https://www.hal.inserm.fr/inserm-01363192/file/Casusoetal_NatNanotechnologies.pdf
https://www.hal.inserm.fr/inserm-01363192/file/Casusoetal_NatNanotechnologies.pdf
Publikováno v:
Eur. Biophys. J.
Eur. Biophys. J., 2011, 40 (10), pp.1143--55. ⟨10.1007/s00249-011-0745-9⟩
Eur. Biophys. J., 2011, 40 (10), pp.1143--55. ⟨10.1007/s00249-011-0745-9⟩
International audience; Despite the major interest in membrane proteins at functional, genomic, and therapeutic levels, their biochemical and structural study remains challenging, as they require, among other things, solubilization in detergent micel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::653d86a48f52caa6169a00db5ee8affc
https://hal.archives-ouvertes.fr/hal-01458282
https://hal.archives-ouvertes.fr/hal-01458282
Publikováno v:
Biophysical Journal. 96(3)
It is now well known that membrane proteins have a great quantitative and qualitative importance. Their stabilization in detergent micelles, which mimic their natural environment, is an essential step in their structural and functional study. The det
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e48d05f333b5268873fda3224b8235f
Autor:
Ignacio Casuso, Jean-Pierre Duneau, Mohamed Chami, Simon Scheuring, Mohamed Husain, Perrine Paul-Gilloteaux, Jonathan Khao, James N. Sturgis, Henning Stahlberg
Publikováno v:
Biophysical Journal
Biophysical Journal, Biophysical Society, 2012, 102 (3), pp.413a-414a. ⟨10.1016/j.bpj.2011.11.2261⟩
Biophysical Journal, 2012, 102 (3), pp.413a-414a. ⟨10.1016/j.bpj.2011.11.2261⟩
Biophysical Journal, Biophysical Society, 2012, 102 (3), pp.413a-414a. ⟨10.1016/j.bpj.2011.11.2261⟩
Biophysical Journal, 2012, 102 (3), pp.413a-414a. ⟨10.1016/j.bpj.2011.11.2261⟩
Membrane-mediated protein-protein and protein-lipid interactions, membrane protein localization, and related dynamics, modulate membrane protein function. So far membrane structure and dynamics could not be studied altogether lacking the technique th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bb5e46a085cbcad37efdc0b76edee45
https://infoscience.epfl.ch/record/274453
https://infoscience.epfl.ch/record/274453