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Linda K. Molnar

Researcher at Konkoly Thege Miklós Astronomical Institute

Publications -  11
Citations -  6285

Linda K. Molnar is an academic researcher from Konkoly Thege Miklós Astronomical Institute. The author has contributed to research in topics: Drug delivery & Biodistribution. The author has an hindex of 10, co-authored 11 publications receiving 5806 citations. Previous affiliations of Linda K. Molnar include Eötvös Loránd University & National Institutes of Health.

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Factors Affecting the Clearance and Biodistribution of Polymeric Nanoparticles

TL;DR: These factors have been shown to substantially affect the biodistribution and blood circulation half-life of circulating nanoparticles by reducing the level of nonspecific uptake, delaying opsonization, and increasing the extent of tissue specific accumulation.
Journal Article

Factors Affecting the Clearance and Biodistribution of Polymeric Nanoparticles

TL;DR: In this article, the authors discuss the factors which can influence nanoparticle blood residence time and organ specific accumulation, including interactions with biological barriers and tunable nanoparticle parameters, such as composition, size, core properties, surface modifications (pegylation and surface charge), and targeting ligand functionalization.
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The Identification of EGRET Sources with Flat-Spectrum Radio Sources

TL;DR: In this article, the authors presented a method to assess the reliability of the identification of EGRET sources with extragalactic radio sources and verified that EGRET is detecting the blazar class of active galactic nuclei (AGNs).
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Nanotechnology for cancer diagnostics: promises and challenges.

TL;DR: This review examines the in vitro and in vivo diagnostic applications of nanoparticles, and other nanodevices that are likely to have an impact on the field in the future.
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HER-2-targeted nanoparticle-affibody bioconjugates for cancer therapy.

TL;DR: Development of drug delivery vehicles comprised of polymeric NPs that are surface modified with Affibody ligands that bind to the extracellular domain of the trans-membrane human epidermal growth factor receptor 2 (HER-2) for targeted delivery to cells which over express the HER-2 antigen is reported.