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Kenneth Lundstrom

Researcher at Hoffmann-La Roche

Publications -  183
Citations -  6925

Kenneth Lundstrom is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Semliki Forest virus & Medicine. The author has an hindex of 43, co-authored 145 publications receiving 6083 citations. Previous affiliations of Kenneth Lundstrom include Orion Corporation & Flamel Technologies.

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Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters.

TL;DR: Human genomic DNA fragments containing catechol O-methyltransferase (COMT) sequences were isolated and the exon-intron structure analysed by sequencing, PCR and comparing to the human COMT cDNA sequences, indicating tissue-specific regulation of the COMT gene at transcriptional level.
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A synthetic agonist at the orphanin FQ/nociceptin receptor ORL1: Anxiolytic profile in the rat

TL;DR: These data confirm the notable anxiolytic-like effects observed at low doses with the orphanin FQ/nociceptin neuropeptide given locally into the brain and support a role for orphan in F Q/nOCiceptin in adaptive behavioral fear responses to stress.
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Viral Vectors in Gene Therapy

Kenneth Lundstrom
- 21 May 2018 - 
TL;DR: Applications of viral vectors have found an encouraging new beginning in gene therapy in recent years, and gene silencing generating a reversible effect has become an interesting alternative, and is well-suited for delivery by viral vectors.
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Ionic permeability of, and divalent cation effects on, two ATP‐gated cation channels (P2X receptors) expressed in mammalian cells.

TL;DR: Complementary DNAs for the ATP‐gated ion channel subunits P2x1 and P2X2 were used to express the receptors in human embryonic kidney cells by stable transfection, and in Chinese hamster ovary cells by viral infection.
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Binding of a new Ca2+ sensitizer, levosimendan, to recombinant human cardiac troponin C : A molecular modelling, fluorescence probe, and proton nuclear magnetic resonance study

TL;DR: The binding of a new calcium sensitizer, levosimendan, to human cardiac troponin C (cTnC) is described, and the role of Asp-88 in the binding of the drug to the NH2-terminal domain of cTNC is revealed.