Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Chad Cummings"'
Autor:
Chad Cummings, Amber Lucas, Jonathan S. Minden, Bibifatima Kaupbayeva, Alan J. Russell, Hironobu Murata
Publikováno v:
ACS Applied Polymer Materials. 1:2897-2906
After labeling of proteins with chemical tags, the unconjugated tag that remains in solution must be removed to prevent interference with downstream workflows. Currently, unconjugated tags are remo...
Autor:
Rebecca L. Ball, Hironobu Murata, Alan J. Russell, Kathryn A. Whitehead, Katherine C. Fein, Chad Cummings
Publikováno v:
Journal of Controlled Release. 255:270-278
Despite its patient-friendliness, the oral route is not yet a viable strategy for the delivery of biomacromolecular therapeutics. This is, in part, due to the large size of proteins, which greatly limits their absorption across the intestinal epithel
Publikováno v:
ACS Macro Letters. 5:493-497
While most effective in aqueous environments, enzymes are also able to catalyze reactions in essentially anhydrous organic media. Enzyme activity in organic solvents is limited as a result of inefficient substrate binding, lack of solubility, and ina
Autor:
Chad Cummings, Allie C. Obermeyer
Publikováno v:
Biochemistry. 57(3)
Membraneless organelles, like membrane-bound organelles, are essential to cell homeostasis and provide discrete cellular subcompartments. Unlike classical organelles, membraneless organelles possess no physical barrier but rather arise by phase separ
Autor:
Sheiliza, Carmali, Hironobu, Murata, Chad, Cummings, Krzysztof, Matyjaszewski, Alan J, Russell
Publikováno v:
Methods in enzymology. 590
Atom transfer radical polymerization (ATRP) from the surface of a protein can generate remarkably dense polymer shells that serve as armor and rationally tune protein function. Using straightforward chemistry, it is possible to covalently couple or d
Autor:
Chad Cummings, Stefanie L. Baker, Alan Campbell, Sheiliza Carmali, Hironobu Murata, Alan J. Russell
Publikováno v:
Biomacromolecules. 18(2)
The reduced immunogenicity and increased stability of protein-polymer conjugates has made their use in therapeutic applications particularly attractive. However, the physicochemical interactions between polymer and protein, as well as the effect of t
Atom transfer radical polymerization (ATRP) from the surface of a protein can generate remarkably dense polymer shells that serve as armor and rationally tune protein function. Using straightforward chemistry, it is possible to covalently couple or d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f90879265586263a7f6dccb6b5a777ee
https://doi.org/10.1016/bs.mie.2016.12.005
https://doi.org/10.1016/bs.mie.2016.12.005
Publikováno v:
Biomaterials. 34:7437-7443
Polymer-based protein engineering (PBPE) offers an attractive method to predictably modify and enhance enzyme structure and function. Using polymers that respond to stimuli such as temperature and pH, enzyme activity and stability can be predictably
Publikováno v:
Biomacromolecules. 14:1919-1926
The attachment of inert polymers, such as polyethylene glycol, to proteins has driven the emergence of a multibillion dollar biotechnology industry. In all cases, proteins have been stabilized or altered by covalently coupling the pre-existing polyme
Autor:
David M. Engle, Samuel D. Fuhlendorf, Christopher M. O’Meilia, John R. Weir, D. Chad Cummings
Publikováno v:
Agriculture, Ecosystems & Environment. 132:1-6
Herbicides have been applied extensively on rangelands to reduce forbs that were considered undesirable, which has been assumed to lead to an increase in grass production and ultimately to an improvement in livestock performance. While scores of rese