Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Ellen H. Reed"'
Autor:
Benjamin S. Schuster, Ellen H. Reed, Ranganath Parthasarathy, Craig N. Jahnke, Reese M. Caldwell, Jessica G. Bermudez, Holly Ramage, Matthew C. Good, Daniel A. Hammer
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Designer organelles with new biochemical functionalities are of great interest in synthetic biology and cellular engineering. Here the authors present a single-protein-based platform for generating synthetic membraneless compartments that is capable
Externí odkaz:
https://doaj.org/article/66e8162a85c44e12a7eb131604d160da
Publikováno v:
Annual Review of Biomedical Engineering. 23:61-87
Cells receive enormous amounts of information from their environment. How they act on this information—by migrating, expressing genes, or relaying signals to other cells—comprises much of the regulatory and self-organizational complexity found ac
Publikováno v:
Handbook of Lipid Membranes ISBN: 9780429194078
Handbook of Lipid Membranes
Handbook of Lipid Membranes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::34b5aa3a7ac257be6a6b603591e459fa
https://doi.org/10.1201/9780429194078-18
https://doi.org/10.1201/9780429194078-18
Protein clusters and condensates are pervasive in mammalian signaling. Yet how the signaling capacity of higher-order assemblies differs from simpler forms of molecular organization is still poorly understood. Here, we present an optogenetic approach
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a61352f509d29e2e42e2d7437e5de50e
https://doi.org/10.1101/2020.10.06.328708
https://doi.org/10.1101/2020.10.06.328708
Publikováno v:
ACS Synth Biol
Protein coacervates serve as hubs to concentrate and sequester proteins and nucleotides and thus function as membrane-less organelles to manipulate cell physiology. We have engineered a coacervating protein to create tunable, synthetic membrane-less
Publikováno v:
Cell reports
SUMMARY Protein clustering is pervasive in cell signaling, yet how signaling from higher-order assemblies differs from simpler forms of molecular organization is still poorly understood. We present an optogenetic approach to switch between oligomers
Autor:
Michael L. Klein, Qi Xiao, Paul A. Heiney, Srujana S. Yadavalli, Sergei A. Vinogradov, Mark Goulian, Daniel A. Hammer, Ellen H. Reed, Tobias Baumgart, Jack D. Rubien, Samantha E. Wilner, Dipankar Sahoo, Virgil Percec, Zhichun Wang
Publikováno v:
Journal of the American Chemical Society. 138:12655-12663
The modular synthesis of a library containing seven self-assembling amphiphilic Janus dendrimers is reported. Three of these molecules contain environmentally friendly chiral-racemic fluorinated dendrons in their hydrophobic part (RF), one contains a
Autor:
Daeyeon Lee, Woo-Sik Jang, Samuel F. Wheeler, Kevin P. Dooley, Daniel A. Hammer, Ellen H. Reed, Seung Chul Park
Publikováno v:
Soft Matter. 12:1014-1020
Polymersomes are robust vesicles made from amphiphilic block co-polymers. Large populations of uniform giant polymersomes with defined, entrapped species can be made by templating of double-emulsions using microfluidics. In the present study, a serie
Autor:
Daniel A. Hammer, Ellen H. Reed
Publikováno v:
Soft matter. 14(31)
Protein engineering enables the creation of materials with designer functionality and tailored responsiveness. Here, we design a protein with two control motifs for its phase separation into micron sized liquid droplets – one driven by a hydrophobi
Autor:
Ranganath Parthasarathy, Craig N. Jahnke, Matthew C. Good, Benjamin S. Schuster, Jessica G. Bermudez, Reese M. Caldwell, Holly Ramage, Ellen H. Reed, Daniel A. Hammer
Publikováno v:
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Many intrinsically disordered proteins self-assemble into liquid droplets that function as membraneless organelles. Because of their biological importance and ability to colocalize molecules at high concentrations, these protein compartments represen