ArticleBioorganic & medicinal chemistry letters2016
Exploration of GGTase-I substrate requirements. Part 2: Synthesis and biochemical analysis of novel saturated geranylgeranyl diphosphate analogs.
Article in Bioorganic & medicinal chemistry letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Sesquiterpene Backbones Generated by Sesquiterpene Cyclases: Formation ofOrganic letters · 2023Article
- Amides as bioisosteres of triazole-based geranylgeranyl diphosphate synthase inhibitors.Bioorganic & medicinal chemistry · 2020Article
- SmgGDS-607 Regulation of RhoA GTPase Prenylation Is Nucleotide-Dependent.Biochemistry · 2018Article
- Bishomoisoprenoid triazole bisphosphonates as inhibitors of geranylgeranyl diphosphate synthase.Bioorganic & medicinal chemistry · 2017Article
- Synthesis of Non-natural, Frame-Shifted Isoprenoid Diphosphate Analogues.Organic letters · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Protein prenylation is a type of post-translational modification that aids certain proteins in localizing to the plasma member where they activate cell signaling. To better understand the isoprenoid requirements and differences of FTase and GGTase-I, a series of saturated geranylgeranyl diphosphate analogs were synthesized and screened against both mammalian FTase and GGTase-I. Of our library of compounds, several analogs proved to be substrates of GGTase-I, with 11d having a krel=0.95 when compared to GGPP (krel=1.0).
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