Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Linda Foit"'
Autor:
Linda Foit, C. Shad Thaxton
Publikováno v:
Biomaterials. 100:67-75
Toll-like receptor 4 (TLR4) plays a critical role in the innate immune system. Stimulation of TLR4 occurs upon binding lipopolysaccharide (LPS), a component of Gram-negative bacterial cell walls. Due to the potency of the induced inflammatory respons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfa8a7799f30af1720dc48665b2a75fc
https://doi.org/10.1016/j.biomaterials.2016.05.021
https://doi.org/10.1016/j.biomaterials.2016.05.021
Autor:
Şerife Akgül, Frederick Stull, Elan Z. Eisenmesser, James C.A. Bardwell, Linda Foit, Sabrina Sayle, M. Claire Cato, Scott Horowitz, Logan S. Ahlstrom, Loïc Salmon, Hashim M. Al-Hashimi
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2018, 430 (1), pp.33-40. ⟨10.1016/j.jmb.2017.11.002⟩
Journal of Molecular Biology, Elsevier, 2018, 430 (1), pp.33-40. ⟨10.1016/j.jmb.2017.11.002⟩
HdeA is a periplasmic chaperone that is rapidly activated upon shifting the pH to acidic conditions. This activation is thought to involve monomerization of HdeA. There is evidence that monomerization and partial unfolding allow the chaperone to bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cccfc673bc7f3f7f34a53d7750b6268e
https://hal.archives-ouvertes.fr/hal-02387272
https://hal.archives-ouvertes.fr/hal-02387272
Publikováno v:
Journal of materials chemistry. B. 4(2)
High-density lipoproteins (HDL) are a class of natural nanostructures found in the blood and are composed of lipids, proteins, and nucleic acids (e.g. microRNA). Their size, which appears to be well-suited for both tissue penetration/retention as wel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f83df32d8bb290a80fe03d2f749608a3
https://pubmed.ncbi.nlm.nih.gov/27069624
https://pubmed.ncbi.nlm.nih.gov/27069624
Autor:
Bharath S. Mamathambika, James C.A. Bardwell, Antje Mueller-Schickert, Linda Foit, Guoping Ren, Caitlyn L. Klaska, Stefan Gleiter
Publikováno v:
Antioxidants & Redox Signaling. 14:973-984
The periplasm provides a strongly oxidizing environment; however, periplasmic expression of proteins with disulfide bonds is often inefficient. Here, we used two different tripartite fusion systems to perform in vivo selections for mutants of the mod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::167649cc3c4afd721991b54e265c51d9
https://doi.org/10.1089/ars.2010.3712
https://doi.org/10.1089/ars.2010.3712
Autor:
Stephan Hofmann, Philipp Koldewey, Guoping Ren, Tim Tapley, Miroslaw Cygler, James C.A. Bardwell, Shu Quan, Nadine Kirsch, Zhaohui Xu, Linda Foit, Karen M. Ruane, Ursula Jakob, Jennifer Pfizenmaier, Rong Shi
Publikováno v:
Nature structural & molecular biology
To optimize the in vivo folding of proteins, we linked protein stability to antibiotic resistance, thereby forcing bacteria to effectively fold and stabilize proteins. When we challenged Escherichia coli to stabilize a very unstable periplasmic prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afd23dced89dc73e74cc7ca94b2f1782
http://europepmc.org/articles/PMC3079333
http://europepmc.org/articles/PMC3079333
Autor:
Maximilian J. Kern, James Titchmarsh, Annekathrin von Hacht, Stuart L. Warriner, Lenz R. Steimer, James C.A. Bardwell, Sheena E. Radford, Linda Foit, Gareth J. Morgan
Publikováno v:
Molecular Cell. 36:861-871
Identifying mutations that stabilize proteins is challenging because most substitutions are destabilizing. In addition to being of immense practical utility, the ability to evolve protein stability in vivo may indicate how evolution has formed today'
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80f3e0faf47fb68ba520f228ec21031e
https://doi.org/10.1016/j.molcel.2009.11.022
https://doi.org/10.1016/j.molcel.2009.11.022
Autor:
Francis J. Giles, C. Shad Thaxton, Nicholas L. Angeloni, Kaylin M. McMahon, Leo I. Gordon, Linda Foit
Publikováno v:
Cancer Treatment and Research ISBN: 9783319165547
High-density lipoproteins (HDL) are diverse natural nanoparticles that carry cholesterol and are best known for the role that they play in cardiovascular disease. However, due to their unique targeting capabilities, diverse molecular cargo, and natur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d60e0603f6f57585ff0b1fe93fc95156
https://europepmc.org/articles/PMC4418545/
https://europepmc.org/articles/PMC4418545/
Publikováno v:
Proceedings of the National Academy of Sciences. 110
Conditionally disordered proteins can alternate between highly ordered and less ordered configurations under physiological conditions. Whereas protein function is often associated with the ordered conformation, for some of these conditionally unstruc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6eb3e28c4759efc421cb5ca1a7af003c
https://doi.org/10.1073/pnas.1222458110
https://doi.org/10.1073/pnas.1222458110
Autor:
Linda, Foit, James C A, Bardwell
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 978
We describe here a genetic selection system that directly links protein stability to antibiotic resistance, allowing one to directly select for mutations that stabilize proteins in vivo. Our technique is based on a tripartite fusion in which the prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d2a0e56b03f8cf3fd538a1168fcea4a3
https://pubmed.ncbi.nlm.nih.gov/23423885
https://pubmed.ncbi.nlm.nih.gov/23423885
Autor:
James C.A. Bardwell, Linda Foit
Publikováno v:
Methods in Molecular Biology ISBN: 9781627032926
We describe here a genetic selection system that directly links protein stability to antibiotic resistance, allowing one to directly select for mutations that stabilize proteins in vivo. Our technique is based on a tripartite fusion in which the prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d0b79a15d3873289c88dc08e17840a3
https://doi.org/10.1007/978-1-62703-293-3_1
https://doi.org/10.1007/978-1-62703-293-3_1