Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Marcus A. Etienne"'
Publikováno v:
Cell Transplantation, Vol 17 (2008)
Previous studies have shown that 17,19,21-tri-N-methyl-Aβ16-22 peptide (Aβ16-22m), and a peptide analogue containing α,α-disubsituted amino acids (ααAA) in the hydrophobic core domain of Aβ, termed AMY-1, effectively inhibited full-length Aβ
Externí odkaz:
https://doaj.org/article/271076578dfb4e8ea5a9701eb2530e53
Autor:
Jaroslav Zajicek, Michael L. Kostochka, Joseph A. Fuselier, Marcus A. Etienne, David H. Coy, Lichun Sun
Publikováno v:
Journal of Heterocyclic Chemistry. 52:1723-1730
Magnetic Resonance Research Center, Department of Chemistry and Biochemistry, University of Notre Dame,Notre Dame 46556, Indiana, USA*E-mail: mkostochka@yahoo.comAdditional Supporting Information may be found in the online version of this article.Rec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::51ebd9526795f7f5e69580832a9957da
https://doi.org/10.1002/jhet.2263
https://doi.org/10.1002/jhet.2263
Publikováno v:
Amino Acids. 42:1727-1733
A more convenient and facile approach for the synthesis and production of camptothecin-amino acids carbamate linkers, that can be used in the synthesis of bioconjugate peptides JF-10-81, JF-10-71, and other peptide analogs designed to target somatost
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30dfe5944e05cf799badde0f8fe6f952
https://doi.org/10.1007/s00726-011-0884-4
https://doi.org/10.1007/s00726-011-0884-4
Autor:
Fernando Porcelli, George Barany, Gianluigi Veglia, Robert P. Hammer, Larry R. Masterson, Marcus A. Etienne
Publikováno v:
Biopolymers. 88:746-753
The use of alpha,alpha-disubstituted amino acids represents a valuable strategy to exercise conformational control in peptides. Incorporation of the nonstereogenic alpha-aminoisobutyryl-glycyl (Aib-Gly) dipeptidyl sequence into i+1 and i+2 positions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df3ba6c1319c8ebb0e6be7c9b434c3e0
https://doi.org/10.1002/bip.20738
https://doi.org/10.1002/bip.20738
Publikováno v:
Understanding Biology Using Peptides ISBN: 9780387265698
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::993c68912871364f707b1a57f60a1032
https://doi.org/10.1007/978-0-387-26575-9_317
https://doi.org/10.1007/978-0-387-26575-9_317
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:
Kyle D. Dukes, Robin K. Lammi, Lyndsey R. Powell, Marcus A. Etienne, Robert P. Hammer, Cyrus K. Bett
Publikováno v:
Biophysical Journal. 96(3)
Alzheimer's disease (AD) is linked to the self-association of amyloid-β peptide (Aβ), a protein of 39-43 amino acids that is normally soluble in the plasma and cerebrospinal fluid. Although large, fibrillar aggregates were long thought to be the pa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::830237baa14702ca094b65a37a4537a6
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
Publikováno v:
Cell transplantation. 17(4)
Previous studies have shown that 17,19,21-tri-N-methyl-Abeta16-22 peptide (Abeta16-22m), and a peptide analogue containing alpha,alpha-disubstituted amino acids (alphaalpha AA) in the hydrophobic core domain of Abeta, termed AMY-1, effectively inhibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::12ecbd4740f47bef4a682ddfe6ca703b
https://pubmed.ncbi.nlm.nih.gov/18522242
https://pubmed.ncbi.nlm.nih.gov/18522242
Autor:
Robert P. Hammer, Joohyun Kim, Timothy A. Keiderling, Vladimir Setnička, Rong Huang, Marcus A. Etienne, Jan Kubelka
Publikováno v:
Journal of the American Chemical Society. 129(44)
Isotope-edited IR spectroscopy was used to study a series of singly and doubly 13C=O-labeled beta-hairpin peptides stabilized by an Aib-Gly turn sequence. The double-labeled peptides have amide I' IR spectra that show different degrees of vibrational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46d2f7979f16745115a1df7fd9c45819
https://pubmed.ncbi.nlm.nih.gov/17929810
https://pubmed.ncbi.nlm.nih.gov/17929810