Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Jed P. Aucoin"'
Autor:
Tim J. Jensen, Cyrus K. Bett, Robin L. McCarley, Jed P. Aucoin, Ted Ajmo, Donna L. Herber, Marcus A. Etienne, David G. Morgan, Robert P. Hammer
Publikováno v:
Understanding Biology Using Peptides ISBN: 9780387265698
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aac836544d0842840ef07ae875c4e09e
https://doi.org/10.1007/978-0-387-26575-9_201
https://doi.org/10.1007/978-0-387-26575-9_201
Autor:
Marcus A, Etienne, Nadia J, Edwin, Jed P, Aucoin, Paul S, Russo, Robin L, McCarley, Robert P, Hammer
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 386
The beta-amyloid peptide aggregates via a nucleation pathway where micellar aggregates propagate to form oligomers (protofibrils), which then polymerize into insoluble fibrils. This fibrillogenic process has been linked to the pathogenesis associated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e8b8cc374eac50621b2728d9ff071e12
https://pubmed.ncbi.nlm.nih.gov/18604947
https://pubmed.ncbi.nlm.nih.gov/18604947
Autor:
Paul S. Russo, Robert P. Hammer, Marcus A. Etienne, Robin L. McCarley, Jed P. Aucoin, Nadia J. Edwin
Publikováno v:
Peptide Characterization and Application Protocols ISBN: 9781588295507
The beta-amyloid peptide aggregates via a nucleation pathway where micellar aggregates propagate to form oligomers (protofibrils), which then polymerize into insoluble fibrils. This fibrillogenic process has been linked to the pathogenesis associated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afdd428ef9df9af165876d584900e475
https://doi.org/10.1007/978-1-59745-430-8_7
https://doi.org/10.1007/978-1-59745-430-8_7
Publikováno v:
Journal of the American Chemical Society. 128:3522-3523
We have prepared two peptides based on the hydrophobic core (Lys-Leu-Val-Phe-Phe) of amyloid beta-protein (Abeta) that contain alpha,alpha-disubstituted amino acids at alternating positions, but differ in the positioning of the oligolysine chain (AMY
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41a47685060d7efef85751c0abbaa394
https://doi.org/10.1021/ja0600678
https://doi.org/10.1021/ja0600678