Non‐thiol Farnesyltransferase Inhibitors: Utilization of the Far Aryl Binding Site by 5‐Cinnamoylaminobenzophenones | Zendy

Mitsch Andreas | Zendy; Wißner Pia | Zendy; Böhm Markus | Zendy; Silber Katrin | Zendy; Klebe Gerhard | Zendy; Sattler Isabel | Zendy; Schlitzer Martin | Zendy

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Non‐thiol Farnesyltransferase Inhibitors: Utilization of the Far Aryl Binding Site by 5‐Cinnamoylaminobenzophenones

Author(s) -

Mitsch Andreas,

Wißner Pia,

Böhm Markus,

Silber Katrin,

Klebe Gerhard,

Sattler Isabel,

Schlitzer Martin

Publication year - 2004

Publication title -

archiv der pharmazie

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.468

H-Index - 61

eISSN - 1521-4184

pISSN - 0365-6233

DOI - 10.1002/ardp.200400871

Subject(s) - farnesyltransferase , aryl , benzophenone , chemistry , farnesyl diphosphate farnesyltransferase , peptidomimetic , substituent , stereochemistry , binding site , combinatorial chemistry , organic chemistry , biochemistry , enzyme , prenylation , peptide , alkyl

We recently described two novel aryl binding sites of farnesyltransferase. In this study, the cinnamoyl residue was designed as an appropriate substituent for our benzophenone‐based AAX‐peptidomimetic compound capable of occupying the far aryl binding site.

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