Identification of the β-lactamase inhibitor protein-II (BLIP-II) interface residues essential for binding affinity and specificity for class A β-lactamases
about
Weighted protein residue networks based on joint recurrences between residuesMolecular basis for the catalytic specificity of the CTX-M extended-spectrum β-lactamases.Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases.Engineering Specificity from Broad to Narrow: Design of a β-Lactamase Inhibitory Protein (BLIP) Variant That Exclusively Binds and Detects KPC β-Lactamase.BLIP-II Employs Differential Hotspot Residues To Bind Structurally Similar Staphylococcus aureus PBP2a and Class A β-Lactamases.Role of β-lactamase residues in a common interface for binding the structurally unrelated inhibitory proteins BLIP and BLIP-II.
P2860
Identification of the β-lactamase inhibitor protein-II (BLIP-II) interface residues essential for binding affinity and specificity for class A β-lactamases
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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2013年论文
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2013年论文
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name
Identification of the β-lactam ...... icity for class A β-lactamases
@en
type
label
Identification of the β-lactam ...... icity for class A β-lactamases
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prefLabel
Identification of the β-lactam ...... icity for class A β-lactamases
@en
P2093
P2860
P356
P1476
Identification of the β-lactam ...... icity for class A β-lactamases
@en
P2093
Dar-Chone Chow
Kevin E Ruprecht
Nicholas G Brown
Timothy Palzkill
P2860
P304
17156-17166
P356
10.1074/JBC.M113.463521
P407
P577
2013-04-27T00:00:00Z