Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Joshua W. Wilkerson"'
Autor:
Kristen M. Wilding, Bradley C. Bundy, Addison K. Smith, Joshua W. Wilkerson, Thomas A. Knotts
Publikováno v:
Journal of Chemical Information and Modeling. 60:5117-5125
Functionalization is often needed to harness the power of proteins for beneficial use but can cause losses to stability and/or activity. State of the art methods to limit these deleterious effects accomplish this by substituting an amino acid in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::212ef0a8cc0109af155c630c6b45eb18
https://doi.org/10.1021/acs.jcim.0c00725
https://doi.org/10.1021/acs.jcim.0c00725
Autor:
Thomas A. Knotts, Emily Long Zhao, Brandon D Timmerman, Bradley C. Bundy, Joshua W. Wilkerson, Mehran Soltani, Addison K. Smith
Publikováno v:
The Journal of chemical physics. 154(7)
PEGylated and surface-tethered proteins are used in a variety of biotechnological applications, but traditional methods offer little control over the placement of the functionalization sites on the protein. Fortunately, recent experimental methods fu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d386a6abdc75fa53e48993bb9b06a840
https://pubmed.ncbi.nlm.nih.gov/33607875
https://pubmed.ncbi.nlm.nih.gov/33607875
Autor:
Joshua W, Wilkerson, Addison K, Smith, Kristen M, Wilding, Bradley C, Bundy, Thomas A, Knotts
Publikováno v:
Journal of chemical information and modeling. 60(10)
Functionalization is often needed to harness the power of proteins for beneficial use but can cause losses to stability and/or activity. State of the art methods to limit these deleterious effects accomplish this by substituting an amino acid in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4ded0727177f33d5591ef6d9f6c72966
https://pubmed.ncbi.nlm.nih.gov/32966074
https://pubmed.ncbi.nlm.nih.gov/32966074
Publikováno v:
The journal of physical chemistry. A. 124(30)
Recent new methods to functionalize proteins at specific amino acid locations use unnatural amino acids that contain azido and alkynyl groups. This capability is unprecedented and enables the creation of site-specific protein devices. Because of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfd127f2110ce477b5a40f71d3dd1812
https://pubmed.ncbi.nlm.nih.gov/32614187
https://pubmed.ncbi.nlm.nih.gov/32614187
Autor:
Bradley C. Bundy, Kristen M. Wilding, Addison K. Smith, Joshua W. Wilkerson, Derek B. Bush, Thomas A. Knotts
Publikováno v:
ACS synthetic biology. 7(2)
Although polyethylene glycol (PEG) is commonly used to improve protein stability and therapeutic efficacy, the optimal location for attaching PEG onto proteins is not well understood. Here, we present a cell-free protein synthesis-based screening pla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02a8e7b839bd14be1ca5b9ee08d2d24a
https://pubmed.ncbi.nlm.nih.gov/29295615
https://pubmed.ncbi.nlm.nih.gov/29295615
Publikováno v:
New biotechnology. 44
Enzyme-mediated biocatalysis is generally more selective and environmentally friendly and requires less energy than chemocatalysis. However, factors such as temperature, acidity and the presence of proteases can negate enzyme activity. Encapsulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::529cc09645213435c84b1cb5f7bf4b47
https://pubmed.ncbi.nlm.nih.gov/29702249
https://pubmed.ncbi.nlm.nih.gov/29702249
Autor:
Joshua W. Wilkerson, Rebecca L. Swensen, Michael L. Christian, Bradley C. Bundy, John Hunt, Parker J. Funk, William C. Carver, Kristen M. Wilding
Publikováno v:
Biotechnology Journal. 14:1800271
Approximately one third of protein therapeutics are produced in Escherichia coli, targeting a wide variety of diseases. However, due to immune recognition of endotoxin (a lipid component in the E. coli cell membrane), these protein products must be e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2b4f809c16a735c5bfdf8bea53044e3
https://doi.org/10.1002/biot.201800271
https://doi.org/10.1002/biot.201800271