Simon Goodman
Merck & Co.
37 Papers
173 Citations
Simon Goodman is an academic researcher from Merck & Co.. The author has contributed to research in topics: Integrin & Amino acid. The author has an hindex of 10, co-authored 37 publications. Previous affiliations of Simon Goodman include Technische Universität München.
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Papers
N-Methylated cyclic RGD peptides as highly active and selective alpha(V)beta(3) integrin antagonists.
Michael A. Dechantsreiter,Eckart Planker,Barbara Mathä,Elisabeth Lohof,Günter Hölzemann,Alfred Jonczyk,Simon Goodman,Horst Kessler +7 more
TL;DR: Cyclo(RGDf-N(Me)V-) (P5) was found to be even more active than L1 and is one of the most active and selective compounds in inhibiting vitronectin binding to the alpha(V)beta(3) integrin.
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Structural and Functional Aspects of RGD-Containing Cyclic Pentapeptides as Highly Potent and Selective Integrin αVβ3 Antagonists
Roland Haubner,Rainer Gratias,Beate Diefenbach,Simon Goodman,and Alfred Jonczyk,Horst Kessler +5 more
TL;DR: The design of low-molecular-mass αVβ3 antagonists by “spatial screening” led to the highly active peptides c( RGDFV) and c(RGDFV), and the influence of the amino acids in positions 4 and 5 flanking the RGD-sequence on the inhibition of vitronectin and fibrinogen binding to the isolated αV β3 and αIIbβ3 receptors was investigated.
609
Nanomolar Small Molecule Inhibitors for αvβ6, αvβ5, and αvβ3 Integrins
TL;DR: Low molecular weight inhibitors are characterized for their ability to specifically inhibit αvβ6 integrin, a fibronectin/tenascin receptor, and several classes of inhibitors with different selectivities are found.
207
Stereoisomerism and Biological Activity of the Selective and Superactive αvβ3 Integrin Inhibitor cyclo(-RGDfV-) and Its Retro-Inverso Peptide
TL;DR: The cyclic pentapeptide cyclo(-Arg-Gly-Asp-d-Phe-Val-) is a highly potent and selective inhibitor for the αvβ3 integrin and is a prospective anticancer drug by acting to inhibit angiogenesis and by...
146
Novel Solid-Phase Synthesis of Azapeptides and Azapeptoides via Fmoc-Strategy and Its Application in the Synthesis of RGD-Mimetics
TL;DR: An efficient method for the solid-phase synthesis and biological evaluation of linear RGD-mimetics containing an azaamino acid instead of glycine are described, which meet all requirements of the one-bead−one-compound concept.
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