Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Phillip Gao"'
Autor:
Fei Phillip Gao, Kalena M. Nichol, David R. Corbin, Jorge E. Umana, Kaylee E. Barr, William D. Picking, Edward J. Reyes, Brian C. Kirchhoff, Mark B. Shiflett, Nicole A. Montoya, Eric R. Hartman
Publikováno v:
Kansas Journal of Medicine. 13:6-9
Introduction. It is estimated that 50% of vaccines produced annu- ally are wasted because effectivity is dependent on protein structure and heat exposure disrupts the intermolecular interactions that maintain this structure. Since 90% of vaccines req
Autor:
Ana Rita C. Morais, Lillian L. Higgins, Kaylee E. Barr, Kalena M. Nichol, Brian C. Kirchhoff, Eric R. Hartman, Rhianna E. Roth, Simon Velasquez Morales, Mark B. Shiflett, Jorge E. Umana, Phillip Gao, Channary Ny, Edward J. Reyes, David R. Corbin, William D. Picking, Alan M. Allgeier, Nicole A. Montoya
Publikováno v:
Langmuir : the ACS journal of surfaces and colloids. 36(47)
Approximately half of all vaccines produced annually are wasted because effectivity is dependent on protein structure and heat exposure disrupts the intermolecular interactions needed to maintain the structure. Thus, most vaccines require a temperatu
Autor:
Nicole, Montoya, Kaylee, Barr, Brian, Kirchhoff, Edward, Reyes, Jorge, Umana, Kalena, Nichol, Eric, Hartman, William, Picking, Fei Phillip, Gao, David R, Corbin, Mark B, Shiflett
Publikováno v:
Kansas Journal of Medicine
Introduction It is estimated that 50% of vaccines produced annually are wasted because effectivity is dependent on protein structure and heat exposure disrupts the intermolecular interactions that maintain this structure. Since 90% of vaccines requir
Autor:
Sangeeta B. Joshi, C. Russell Middaugh, Subhashchandra Naik, Divya N. Amin, Elizabeth Lindboe, Phillip Gao, Melissa Cullom, Taylor L. Roop, David B. Volkin, Srivalli Telikepalli, Mark T. Fisher, Ozan S. Kumru
Publikováno v:
Protein Science. 23:1461-1478
The ability of a GroEL-based bio-layer interferometry (BLI) assay to detect structurally altered and/or aggregated species of pharmaceutically relevant proteins is demonstrated. Assay development included optimizing biotinylated-GroEL immobilization
Autor:
Susan R. Brock, R. John Collier, Edward P. Gogol, Wesley Mcginn-Straub, Phillip Gao, Na Zhang, Narahari Akkaladevi, Subhashchandra Naik, Jon Tally, Bradley L. Pentelute, Mark T. Fisher
Publikováno v:
Biochemistry. 52:6335-6347
Domain 2 of the anthrax protective antigen (PA) prepore heptamer unfolds and refolds during endosome acidification to generate an extended 100 Å β barrel pore that inserts into the endosomal membrane. The PA pore facilitates the pH-dependent unfold
Publikováno v:
Current Topics in Medicinal Chemistry. 999:15-21
Correcting aberrant folds that develop during protein folding disease states is now an active research endeavor that is attracting increasing attention from both academic and industrial circles. One particular approach focuses on developing or identi