Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Amanda L. Stouffer"'
Autor:
Chunlong Ma, Amanda L. Stouffer, Lawrence H. Pinto, Lidia Cristian, James D. Lear, Yuki Ohigashi, Robert A. Lamb, William F. DeGrado
Publikováno v:
Structure. 16:1067-1076
Summary We explore the interplay between amino acid sequence, thermodynamic stability, and functional fitness in the M2 proton channel of influenza A virus. Electrophysiological measurements show that drug-resistant mutations have minimal effects on
Publikováno v:
Journal of Molecular Biology. 347:169-179
The driving forces behind the folding processes of integral membrane proteins after insertion into the bilayer, is currently under debate. The M2 protein from the influenza A virus is an ideal system to study lateral association of transmembrane heli
Autor:
William F. DeGrado, Arne Schön, Lawrence H. Pinto, Yuki Ohigashi, Robert A. Lamb, Xianghong Jing, Alexei L. Polishchuk, James D. Lear, Chunlong Ma, Ernesto Freire, Emma Magavern, Amanda L. Stouffer
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 106(30)
The influenza A virus M2 protein (A/M2) is a homotetrameric pH-activated proton transporter/channel that mediates acidification of the interior of endosomally encapsulated virus. This 97-residue protein has a single transmembrane (TM) helix, which as
Autor:
Valentina Tereshko, Anna S. Levine, Luigi Di Costanzo, William F. DeGrado, Rudresh Acharya, Vikas Nanda, Cinque Soto, Amanda L. Stouffer, Steven Stayrook, David Salom
Until recently, the pH-gated proton channel of influenza A virus, M2, was effectively targeted by amantadine-based antivirals, but resistance to these drugs is now widespread. Two groups now present structural studies of M2 proton channel. Jason Schn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71006c62f0b1ebe1463cd8fc53b18d4a
http://hdl.handle.net/11588/768610
http://hdl.handle.net/11588/768610
Publikováno v:
Analytical Ultracentrifugation VIII ISBN: 3540296158
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dab934afce38016eaa2118872762ba4b
https://doi.org/10.1007/2882_010
https://doi.org/10.1007/2882_010
Autor:
Amanda L. Stouffer, Rudresh Acharya, David Salom, Anna S. Levine, Luigi Di Costanzo, Cinque S. Soto, Valentina Tereshko, Vikas Nanda, Steven Stayrook, William F. DeGrado
Publikováno v:
Nature. 452:380-380
Publikováno v:
Biophysical Journal. (5):3421-3429
A peptide containing glycine at a and d positions of a heptad motif was synthesized to investigate the possibility that membrane-soluble peptides with a Gly-based, left-handed helical packing motif would associate. Based on analytical ultracentrifuga