Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Erin N. Heim"'
Autor:
Li He, Helena Steinocher, Ashish Shelar, Emily B Cohen, Erin N Heim, Birthe B Kragelund, Gevorg Grigoryan, Daniel DiMaio
Publikováno v:
eLife, Vol 6 (2017)
Transmembrane domains (TMDs) engage in protein-protein interactions that regulate many cellular processes, but the rules governing the specificity of these interactions are poorly understood. To discover these principles, we analyzed 26-residue model
Externí odkaz:
https://doaj.org/article/0c943039475e4f7da16907be3642d2a5
Publikováno v:
Cell reports
SUMMARY During virus entry, human papillomaviruses are sorted by the cellular trafficking complex, called retromer, into the retrograde transport pathway to traffic from the endosome to downstream cellular compartments, but regulation of retromer act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d7bd5f78912d4fb0f80dc56e76fe10f
http://europepmc.org/articles/PMC7339955
http://europepmc.org/articles/PMC7339955
Autor:
Daniel DiMaio, Helena Steinocher, Erin N. Heim, Birthe B. Kragelund, Emily B. Cohen, Gevorg Grigoryan, Ashish Shelar, Li He
Publikováno v:
eLife
eLife, Vol 6 (2017)
He, L, Steinocher, H, Shelar, A, Cohen, E B, Heim, E N, Kragelund, B B, Grigoryan, G & DiMaio, D 2017, ' Single methyl groups can act as toggle switches to specify transmembrane protein-protein interactions ', eLife, vol. 6, e27701 . https://doi.org/10.7554/eLife.27701
eLife, Vol 6 (2017)
He, L, Steinocher, H, Shelar, A, Cohen, E B, Heim, E N, Kragelund, B B, Grigoryan, G & DiMaio, D 2017, ' Single methyl groups can act as toggle switches to specify transmembrane protein-protein interactions ', eLife, vol. 6, e27701 . https://doi.org/10.7554/eLife.27701
Transmembrane domains (TMDs) engage in protein-protein interactions that regulate many cellular processes, but the rules governing the specificity of these interactions are poorly understood. To discover these principles, we analyzed 26-residue model
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36e3396c9e305fa216beb4c663637e14
https://pubmed.ncbi.nlm.nih.gov/28869036
https://pubmed.ncbi.nlm.nih.gov/28869036
Autor:
Lisa M. Petti, Donald M. Engelman, Erin N. Heim, Ross S. Federman, Alexander G. Karabadzhak, Anne P. B. Edwards, Daniel DiMaio, Jez L. Marston
Publikováno v:
Proceedings of the National Academy of Sciences. 112
We have constructed 26-amino acid transmembrane proteins that specifically transform cells but consist of only two different amino acids. Most proteins are long polymers of amino acids with 20 or more chemically distinct side-chains. The artificial t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::007c7b1e7570da244a9d28d303560373
https://doi.org/10.1073/pnas.1514230112
https://doi.org/10.1073/pnas.1514230112