Development of bestatin-based activity-based probes for metallo-aminopeptidases.
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Synthesis of New (−)-Bestatin-Based Inhibitor Libraries Reveals a Novel Binding Mode in the S1 Pocket of the Essential Malaria M1 MetalloaminopeptidaseBestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidasesStrategies in the design of small-molecule fluorescent probes for peptidases.From crystal to compound: structure-based antimalarial drug discovery.Recent developments and applications of clickable photoprobes in medicinal chemistry and chemical biology.Sitagliptin does not inhibit the M1 alanyl aminopeptidase from Plasmodium falciparum.
P2860
Development of bestatin-based activity-based probes for metallo-aminopeptidases.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Development of bestatin-based activity-based probes for metallo-aminopeptidases.
@en
Development of bestatin-based activity-based probes for metallo-aminopeptidases.
@nl
type
label
Development of bestatin-based activity-based probes for metallo-aminopeptidases.
@en
Development of bestatin-based activity-based probes for metallo-aminopeptidases.
@nl
prefLabel
Development of bestatin-based activity-based probes for metallo-aminopeptidases.
@en
Development of bestatin-based activity-based probes for metallo-aminopeptidases.
@nl
P2093
P2860
P1476
Development of bestatin-based activity-based probes for metallo-aminopeptidases.
@en
P2093
Doron C Greenbaum
Geetha Velmourougane
Gilana Reiss
Michael B Harbut
P2860
P304
P356
10.1016/J.BMCL.2008.09.021
P407
P577
2008-09-10T00:00:00Z