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Ronald L. Goldberg

Researcher at Novartis

Publications -  50
Citations -  1746

Ronald L. Goldberg is an academic researcher from Novartis. The author has contributed to research in topics: Cartilage & Proteoglycan. The author has an hindex of 19, co-authored 50 publications receiving 1712 citations. Previous affiliations of Ronald L. Goldberg include Tulane University & Tufts University.

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Discovery of CGS 27023A, a non-peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits.

TL;DR: In this article, structure-activity relationships of a lead hydroxamic acid inhibitor of recombinant human stromelysin were systematically defined by taking advantage of a concise synthesis that allowed diverse functionality to be explored at each position in a template.
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Hyaluronate inhibition of cell proliferation.

TL;DR: The changes in synovial fluid hyaluronate that are associated with arthropathies may contribute to a favorable environment for rheumatoid pannus expansion.
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An improved method for determining proteoglycans synthesized by chondrocytes in culture.

TL;DR: An improved micro method for measuring sulfated glycosaminoglycans (S-GAG) in chondrocyte cultures using 1,9-Dimethylmethylene Blue (DMB) has been developed and can be used to measure changes in proteoglycan synthesized by chondROcytes.
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Elevated plasma levels of hyaluronate in patients with osteoarthritis and rheumatoid arthritis.

TL;DR: Data support in part the contention that plasma HA may be unique as a marker, in that it may be a reflection of synovial involvement and inflammation, rather than only of inflammation, in arthritis.
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Identification of dipeptidyl nitriles as potent and selective inhibitors of cathepsin B through structure-based drug design.

TL;DR: Inhibitor potency and selectivity were enhanced by tethering a carboxylate functionality from the carbon alpha to the nitrile to interact with this region of the enzyme, resulting in the identification of compound 10, a 7 nM inhibitor of cathepsin B, with excellent selectivity over other cysteine cathepsypsins.