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Alan J. Waring

Researcher at University of California, Los Angeles

Publications -  202
Citations -  9129

Alan J. Waring is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Pulmonary surfactant & Peptide. The author has an hindex of 55, co-authored 198 publications receiving 8568 citations. Previous affiliations of Alan J. Waring include Charles R. Drew University of Medicine and Science & Los Angeles Biomedical Research Institute.

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Journal ArticleDOI

Membrane thinning effect of the beta-sheet antimicrobial protegrin.

TL;DR: Results suggest that PG-1 has the same concentration-gated mechanism of action as alamethicin and the S state is adsorbed in the headgroup region of the lipid bilayer, where the peptide is in an inactive state.
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Anti-inflammatory apoA-I-mimetic peptides bind oxidized lipids with much higher affinity than human apoA-I

TL;DR: The results indicate that specific mimetic peptides have an increased binding affinity for oxidized phospholipids, compared with the parent nonoxidized phosphoattractant protein-1 (MCP-1) whereas full-length human apoA-I binds oxidized and nonoxids phospholIPids similarly.
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Activity of alpha- and theta-defensins against primary isolates of HIV-1.

TL;DR: The relationship between carbohydrate-binding and the antiviral properties of α- and θ-defensins is compared and it is shown that the lectin-like behavior of defensins may contribute to many other activities of these multifunctional peptides.
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Effects of Lung Surfactant Proteins, SP-B and SP-C, and Palmitic Acid on Monolayer Stability

TL;DR: Langmuir isotherms and fluorescence and atomic force microscopy images of synthetic model lung surfactants were used to determine the influence of palmitic acid and synthetic peptides based on the surfactant-specific proteins SP-B and SP-C on the morphology and function of surfactan monolayers.
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CotH3 mediates fungal invasion of host cells during mucormycosis

TL;DR: Together, these data indicate that CotH3 and CotH2 function as invasins that interact with host cell GRP78 to mediate pathogenic host-cell interactions and identify CotH as a promising therapeutic target for mucormycosis.