Literature DB >> 17270439

Novel hydroxamic acid-related phosphinates: inhibition of neutral aminopeptidase N (APN).

Marcin Drag1, Renata Grzywa, Jozef Oleksyszyn.   

Abstract

Here we describe the inhibitory activity toward neutral aminopeptidase of three new families of phosphinate inhibitors related in structure to hydroxamic acids. These compounds, even as racemic mixtures, are good inhibitors of APN and show strong structure activity relationship (SAR) depending on the substituents in P1 and P1' positions.

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Year:  2007        PMID: 17270439     DOI: 10.1016/j.bmcl.2007.01.028

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  3 in total

1.  P-C bond formation via P-H addition of a fluoroaryl phosphinic acid to ketones.

Authors:  Andreas Orthaber; Jörg H Albering; Ferdinand Belaj; Rudolf Pietschnig
Journal:  J Fluor Chem       Date:  2010-10       Impact factor: 2.050

2.  Aminopeptidase fingerprints, an integrated approach for identification of good substrates and optimal inhibitors.

Authors:  Marcin Drag; Matthew Bogyo; Jonathan A Ellman; Guy S Salvesen
Journal:  J Biol Chem       Date:  2009-11-30       Impact factor: 5.157

Review 3.  Metallo-aminopeptidase inhibitors.

Authors:  Artur Mucha; Marcin Drag; John P Dalton; Paweł Kafarski
Journal:  Biochimie       Date:  2010-05-10       Impact factor: 4.079

  3 in total

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