Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Sai Hari A. Gandham"'
Publikováno v:
Biochemical and Biophysical Research Communications. 448:45-49
Inclusion bodies (IBs) are commonly formed in Escherichia coli due to over expression of recombinant proteins in non-native state. Isolation, denaturation and refolding of these IBs is generally performed to obtain functional protein. However, during
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83927ec332904fe57ce1e4cb49bd13e1
https://doi.org/10.1016/j.bbrc.2014.04.049
https://doi.org/10.1016/j.bbrc.2014.04.049
Publikováno v:
Journal of Analytical Sciences, Methods and Instrumentation. :173-178
NF-κB plays a crucial role in regulating various biological processes including innate and adaptive immunity, inflammation, stress responses, B-cell development, and lymphoid organogenesis. Currently, several assays like electrophoretic mobility shi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::221b2a0eceb0b600107733994b7c2e03
https://doi.org/10.4236/jasmi.2013.33022
https://doi.org/10.4236/jasmi.2013.33022
Autor:
Alan D.T. Barrett, David E. Volk, Anjenique Anderson, David G. Gorenstein, Sai Hari A. Gandham, Jana J. von Lindern, Fiona J. May, David W.C. Beasley
Publikováno v:
Virology. 394(1):12-18
The structure of recombinant domain III of the envelope protein (rED3) of yellow fever virus (YFV), containing the major neutralization site, was determined using NMR spectroscopy. The amino acid sequence and structure of the YFV-rED3 shows differenc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbdfcb7f8b3b44b16f6e606b7b03dc38
Autor:
David E. Volk, Ganesh L.R. Lokesh, Muniasamy Neerathilingam, David G. Gorenstein, Sai Hari A. Gandham
Publikováno v:
Biochemical and biophysical research communications. 453(3)
Thioaptamers targeting the dengue-2 virus (DENV-2) envelope protein domain III (EDIII) were developed. EDIII, which contains epitopes for binding neutralizing antibodies, is the putative host-receptor binding domain and is thus an attractive target f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d29b885fa818a8394c5ea86608f0a446
https://pubmed.ncbi.nlm.nih.gov/25261724
https://pubmed.ncbi.nlm.nih.gov/25261724
Autor:
Li Li, Fiona J. May, David G. Gorenstein, David E. Volk, David W.C. Beasley, Kurtis M. Anderson, Sai Hari A. Gandham, Alan D.T. Barrett
Nearly complete backbone and side chain resonance assignments have been obtained for the third domain, residues M289-K400, of the envelope protein from the sylvatic strain (P72-1244) of the dengue 1 virus, containing mutations N336S and E370K, using
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fac77bebde4f159d70e912b3147f4b0
https://europepmc.org/articles/PMC2593834/
https://europepmc.org/articles/PMC2593834/
Autor:
Anjenique Anderson, Fiona J. May, David E. Volk, David G. Gorenstein, Sai Hari A. Gandham, Alan D.T. Barrett
Publikováno v:
Biomolecular NMR Assignments. 1:49-50
Nearly complete backbone and sidechain resonance assignments have been obtained for the third domain, residues S288-K398, of the envelope protein from the Asibi strain of yellow fever virus using double- and triple-resonance spectroscopy.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::198cf5c13e654809398dde72d9c59494
https://doi.org/10.1007/s12104-007-9000-9
https://doi.org/10.1007/s12104-007-9000-9
Publikováno v:
Journal of Analytical Science and Technology. 6(1)
Background Rotor-Gene Q instrument was used to perform high-resolution protein thermal melt studies to characterize protein-small-molecule interaction. Fluorescent dye (1-anilino-8-naphthalenesulfonate (1,8-ANS)) is used as a reporter of protein unfo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::130d28ccf130f38d3b497d15dff89abb