Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Robert E. Jefferson"'
Autor:
Robert E. Jefferson, Aurélien Oggier, Andreas Füglistaler, Nicolas Camviel, Mahdi Hijazi, Ana Rico Villarreal, Caroline Arber, Patrick Barth
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
Abstract Engineering protein biosensors that sensitively respond to specific biomolecules by triggering precise cellular responses is a major goal of diagnostics and synthetic cell biology. Previous biosensor designs have largely relied on binding st
Externí odkaz:
https://doaj.org/article/6b49ba1051634d6fb46147418a7f26b1
Autor:
Justine S. Paradis, Xiang Feng, Brigitte Murat, Robert E. Jefferson, Badr Sokrat, Martyna Szpakowska, Mireille Hogue, Nick D. Bergkamp, Franziska M. Heydenreich, Martine J. Smit, Andy Chevigné, Michel Bouvier, Patrick Barth
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
Computational modeling and design of G Protein-Coupled Receptor quaternary structures reveals a signaling bias switch at the receptor dimer interface that selectively controls G protein vs β-arrestin activation.
Externí odkaz:
https://doaj.org/article/c0d899ae8609439f8ce39b8bdc95e8a4
Publikováno v:
Protein Science. 25:1535-1544
Manipulating single molecules and systems of molecules with mechanical force is a powerful technique to examine their physical properties. Applying force requires attachment of the target molecule to larger objects using some sort of molecular tether
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d6ba8ecc1281a732889520321cb56a4a
https://doi.org/10.1002/pro.2952
https://doi.org/10.1002/pro.2952
Autor:
Mark A. Arbing, Duyoung Min, Robert E. Jefferson, Jing Yang Wang, James U. Bowie, Yifei Qi, Wonpil Im
Publikováno v:
Nature chemical biology, vol 14, iss 5
ClC chloride channels and transporters are important for chloride homeostasis in species from bacteria to human. Mutations in ClC proteins cause genetically inherited diseases, some of which are likely to involve folding defects. The ClC proteins pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c479a5fb3ef09349f94c6ca03b50541d
https://escholarship.org/uc/item/1zd598w0
https://escholarship.org/uc/item/1zd598w0
Publikováno v:
Journal of molecular biology, vol 430, iss 4
Protein folding is a fundamental life process with many implications throughout biology and medicine. Consequently, there have been enormous efforts to understand how proteins fold. Almost all of this effort has focused on water-soluble proteins, how
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fae291e0c9bbe79921500bb831728832
https://escholarship.org/uc/item/7pr2z0gn
https://escholarship.org/uc/item/7pr2z0gn
Publikováno v:
Nature Chemical Biology. 11:981-987
Membrane proteins are designed to fold and function in a lipid membrane, yet folding experiments within a native membrane environment are challenging to design. Here we show that single-molecule forced unfolding experiments can be adapted to study he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8aa14844ec35e8e31d6c1fd3e0db196e
https://doi.org/10.1038/nchembio.1939
https://doi.org/10.1038/nchembio.1939
Publikováno v:
Protein science : a publication of the Protein Society. 25(8)
Manipulating single molecules and systems of molecules with mechanical force is a powerful technique to examine their physical properties. Applying force requires attachment of the target molecule to larger objects using some sort of molecular tether
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d4610e3942f45fd7cad632bdcaa1e027
https://pubmed.ncbi.nlm.nih.gov/27222403
https://pubmed.ncbi.nlm.nih.gov/27222403
Autor:
Robert E. Jefferson, Yifei Qi, James U. Bowie, Wonpil Im, Jing Yang Wang, Mark A. Arbing, Duyoung Min
Publikováno v:
Biophysical Journal. 114:244a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::42126d98f89f4d8bd3b6f0d279d22b86
https://doi.org/10.1016/j.bpj.2017.11.1358
https://doi.org/10.1016/j.bpj.2017.11.1358
Publikováno v:
Biophysical Journal. 110:396a
Our understanding of membrane proteins has been severely hindered by a dearth of techniques to investigate membrane protein folding and stability in lipid bilayers. Our lab has developed a technique to drive membrane protein unfolding under native co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3473c86bd9f1339aa086a0a5c73fc4e7
https://doi.org/10.1016/j.bpj.2015.11.2138
https://doi.org/10.1016/j.bpj.2015.11.2138
Autor:
Todd O. Yeates, Thomas A. Bobik, Shouqiang Cheng, Robert E. Jefferson, Yu Liu, Christopher S. Crowley, Chenguang Fan, Cristina M. Escobar
Hundreds of bacterial species produce proteinaceous microcompartments (MCPs) that act as simple organelles by confining the enzymes of metabolic pathways that have toxic or volatile intermediates. A fundamental unanswered question about bacterial MCP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8dd3fc36d639365fa3bde71545561c19
https://europepmc.org/articles/PMC2867708/
https://europepmc.org/articles/PMC2867708/