Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Patrick Cosme"'
Publikováno v:
Molecular pharmaceutics. 15(3)
Cell-penetrating peptides (CPPs) are promising vectors for the intracellular delivery of a variety of membrane-impermeable bioactive compounds. The mechanisms by which CPPs cross the cell membrane, and the effects that CPPs may have on cell function,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd154b472b6fc39b9e5f868a1ec716de
https://pubmed.ncbi.nlm.nih.gov/29397737
https://pubmed.ncbi.nlm.nih.gov/29397737
Autor:
Sabrina Amar, Gregg B. Fields, Patrick Cosme, Michal Tokmina-Roszyk, Andrew C. Terentis, Yury Gogotsi, Vadym Mochalin, Dorota Tokmina-Roszyk, Anna M. Knapinska
Publikováno v:
Peptide Science. 104:186-195
Nanodiamonds (NDs) have received considerable attention as potential drug delivery vehicles. NDs are small (∼5 nm diameter), can be surface modified in a controllable fashion with a variety of functional groups, and have little observed toxicity in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cc68355193f79e5d488d7cd76adafc4
https://doi.org/10.1002/bip.22636
https://doi.org/10.1002/bip.22636
Autor:
Elijah J. St.Germain, Pradip Maity, Edith Nagy, Salvatore D. Lepore, Patrick Cosme, Andrew C. Terentis
Publikováno v:
Chemical communications (Cambridge, England). 52(11)
The addition of carbamate nitrogen to a non-conjugated carbon–carbon triple bond is catalyzed by an ammonium salt leading to a cyclic product. Studies in homogeneous systems suggest that the ammonium agent facilitates nitrogen–carbon bond formati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8635fa83046a809e79bbf820d851ee75
https://pubmed.ncbi.nlm.nih.gov/26728333
https://pubmed.ncbi.nlm.nih.gov/26728333
Autor:
Ewa P. Wojcikiewicz, Nelson Rivera, Patrick Cosme, Rolando Oyola, Andrew C. Terentis, Deguo Du, Walter G. Gonzalez, Jaroslava Miksovska, Haiyang Liu, Carlos Andino, Richard Lantz
Publikováno v:
Chemical communications (Cambridge, England). 51(32)
We identify distinct site-specific dynamics over the time course of Aβ1-23 amyloid formation by using an unnatural amino acid, p-cyanophenylalanine, as a sensitive fluorescent and Raman probe. Our results also suggest the key role of an edge-to-face
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89ecef916abd4f61959c0b25beded3b6
https://pubmed.ncbi.nlm.nih.gov/25801393
https://pubmed.ncbi.nlm.nih.gov/25801393
Autor:
Rolando Oyola, Richard Lantz, Haiyang Liu, Patrick Cosme, Ewa P. Wojcikiewicz, Deguo Du, Andrew C. Terentis
Publikováno v:
Biophysical Journal. (2):64a
Amyloid diseases, such as Alzheimer's and Parkinson's, are linked to a poorly understood progression of protein misfolding and aggregation that form tissue-selective fibrillar deposits. Elucidation of site-specific dynamics of protein aggregation is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b42badd4a8dabb60e44cdc1a9b1b322d