Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum.
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A Naturally Variable Residue in the S1 Subsite of M1 Family Aminopeptidases Modulates Catalytic Properties and Promotes Functional Specialization3,4-Dihydroxyphenylalanine Peptides as Nonperturbative Quantum Dot Sensors of Aminopeptidase.Sitagliptin does not inhibit the M1 alanyl aminopeptidase from Plasmodium falciparum.Two cap residues in the S1 subsite of a Plasmodium falciparum M1-family aminopeptidase promote broad specificity and enhance catalysis.Evidence for Regulation of Hemoglobin Metabolism and Intracellular Ionic Flux by the Plasmodium falciparum Chloroquine Resistance Transporter
P2860
Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
@zh-hk
2012年論文
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2012年論文
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2012年论文
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2012年论文
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2012年论文
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name
Engagement of the S1, S1' and ...... se from Plasmodium falciparum.
@ast
Engagement of the S1, S1' and ...... se from Plasmodium falciparum.
@en
type
label
Engagement of the S1, S1' and ...... se from Plasmodium falciparum.
@ast
Engagement of the S1, S1' and ...... se from Plasmodium falciparum.
@en
prefLabel
Engagement of the S1, S1' and ...... se from Plasmodium falciparum.
@ast
Engagement of the S1, S1' and ...... se from Plasmodium falciparum.
@en
P2093
P2860
P1476
Engagement of the S1, S1' and ...... se from Plasmodium falciparum.
@en
P2093
Daniel R T Ragheb
Michael Klemba
Seema Dalal
P2860
P356
10.1016/J.MOLBIOPARA.2012.02.003
P577
2012-02-13T00:00:00Z