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Arthur Felix
Researcher at Hoffmann-La Roche
Publications - 114
Citations - 3901
Arthur Felix is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Peptide synthesis & Fluorescamine. The author has an hindex of 31, co-authored 114 publications receiving 3864 citations.
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Journal ArticleDOI
Safety and immunogenicity in man of a synthetic peptide malaria vaccine against plasmodium falciparum sporozoites
D A Herrington,David F. Clyde,Genevieve Losonsky,Manuel Cortesia,James R. Murphy,Jonathan R. Davis,Shahida Baqar,Arthur Felix,Edgar P. Heimer,Dieter Gillessen,Elizabeth Nardin,Ruth S. Nussenzweig,Victor Nussenzweig,M. R. Hollingdale,Myron M. Levine +14 more
TL;DR: This first synthetic peptide parenteral vaccine against a communicable disease tested in man is safe and stimulates biologically active antibodies, which encourage the development of improved vaccine formulations which, by enhancing immunogenicity, may lead to practical vaccines to assist in the control of falciparum malaria.
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The Alzheimer's peptide a beta adopts a collapsed coil structure in water
S S. Zhang,K. Iwata,M.J. Lachenmann,J. W. Peng,Shuwei Li,E.R. Stimson,Y.-a. Lu,Arthur Felix,John E. Maggio,Jongsoon Lee +9 more
TL;DR: The self-assembly of the soluble peptide Abeta into Alzheimer's disease amyloid is believed to involve a conformational change and because fibrillization leads to formation of intermolecular beta-sheet secondary structure, a global conformational rearrangement is highly likely.
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Synthesis, biological activity and conformational analysis of cyclic GRF analogs.
Arthur Felix,Edgar P. Heimer,Ching-Tso Wang,Theodore Lambros,Alain Fournier,Thomas F. Mowles,S L Maines,Robert M. Campbell,Bogda Wegrzynski,Voldemar Toome,David C. Fry,Vincent S. Madison +11 more
TL;DR: Conformational analysis (circular dichroism and molecular dynamics calculations based on NOE-derived distance constraints) demonstrated that cyclo8,12[Asp8,Ala15]-GRF(1-29)-NH2 contains a long alpha-helical segment even in aqueous solution.
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Point Substitution in the Central Hydrophobic Cluster of a Human β-Amyloid Congener Disrupts Peptide Folding and Abolishes Plaque Competence†
William P. Esler,Evelyn R. Stimson,Joseph R. Ghilardi,Yi An Lu,Arthur Felix,Harry V. Vinters,Patrick W. Mantyh,Jonathan P. Lee,John E. Maggio +8 more
TL;DR: It is reported here that an active congener, Aβ(10−35)-NH2, displays time dependence, pH−activity profile, and kinetic order of deposition similar to A β(1−40), and is sufficiently soluble for NMR spectroscopy in water under conditions where it actively deposits.
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1H NMR of A beta amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence.
Jongsoon Lee,Evelyn R. Stimson,Ghilardi,Patrick W. Mantyh,Y.-a. Lu,Arthur Felix,William Llanos,Behbin A,Cummings M,Van Criekinge M +9 more
TL;DR: It is demonstrated that no conformations are present in water under conditions where the peptides can adhere to authentic amyloid plaques and a helical conformation is proposed in plaque formation.