Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Milton Truong"'
Autor:
Milton Truong, Ivan Hung, David D. Busath, Mukesh Sharma, Huan-Xiang Zhou, Huajun Qin, Yimin Miao, Thach V. Can, Sorin Luca, Timothy A. Cross
Publikováno v:
ResearcherID
M2 is a 97-residue, single-pass membrane protein which functions in a tetrameric state. The tetramer forms a proton channel which has been proven to be a drug target for Influenza A virus (H3N2 and H1N1). However, the M2 protein of this virus has rec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::392bf37ad3018e87cb52a7d95d0bd3fc
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 188(1)
A new two-dimensional scheme is proposed for accurate measurements of high-resolution chemical shifts and heteronuclear dipolar couplings in NMR of aligned samples. Both the (1)H chemical shifts and the (1)H-(15)N dipolar couplings are evolved in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e10316009058dceb7bdc1f93b79572b
https://pubmed.ncbi.nlm.nih.gov/17606394
https://pubmed.ncbi.nlm.nih.gov/17606394
Autor:
Eric D. Gordon, William E. Wieczorek, Breanna S. Vollmar, Myriam Cotten, Mukesh Sharma, Richard W. Pastor, Riqiang Fu, Milton Truong, Richard M. Venable
Publikováno v:
Biophysical Journal. 100:496a
Piscidin, an amphipathic cationic antimicrobial peptide (AMP) active against a broad range of pathogens including multidrug-resistant bacteria and HIV-1, belongs to a large family of vital host-defense peptides that interact, at least initially, with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1cea0d5749e9901ebcaad1c0c5c3215
https://doi.org/10.1016/j.bpj.2010.12.2907
https://doi.org/10.1016/j.bpj.2010.12.2907
Autor:
Milton Truong, Alexander E. Dao, Myriam Cotten, Mukesh Sharma, Riqiang Fu, William E. Wieczorek
Publikováno v:
Biophysical Journal. 100:512a
First discovered in the mast cells of hybrid striped sea bass, piscidin 1 and piscidin 3 (p1 and p3) are two isoforms of the piscidin family of antimicrobial, cationic, and amphipathic peptides (ACAPs) that have demonstrated broad spectrum activity a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b86f0c702286c03c33548abfea482c9
https://doi.org/10.1016/j.bpj.2010.12.2994
https://doi.org/10.1016/j.bpj.2010.12.2994
Publikováno v:
Biophysical Journal. 96:410a
Gramicidin A, an enzymatic product from the bacterium Bacillus brevis, is a fifteen residue peptide that induces cell lysis by forming a transmembrane channel that conducts monovalent cations and water molecules into a cell. The dimer of gramicidin A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bfe7e2d63984d2ce3450b2be7a7fc14
https://doi.org/10.1016/j.bpj.2008.12.2091
https://doi.org/10.1016/j.bpj.2008.12.2091
Autor:
Anna S. Kozlova, Elaina L. Daza, Eric D. Gordon, Mallorie M. Taylor, Riqiang Fu, Jeffrey J. Ditto, Daniel J. Hibbard, Myriam Cotten, Milton Truong
Publikováno v:
Biophysical Journal. 96:390a
Piscidin is an amphipathic cationic antimicrobial peptide that belongs to a large family of versatile host-defense peptides, which interact, at least initially, with cell membranes in order to perform their function. In the research presented here, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51dbedd5b6a8c47e5714936d19f0c987
https://doi.org/10.1016/j.bpj.2008.12.2912
https://doi.org/10.1016/j.bpj.2008.12.2912
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