Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of beta-lactamases.
about
Computational Redesign of the SHV-1 β-Lactamase/β-Lactamase Inhibitor Protein InterfaceStructural and Biochemical Evidence That a TEM-1 -Lactamase N170G Active Site Mutant Acts via Substrate-assisted CatalysisRemoval of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric StrainIdentification of residues critical for metallo-beta-lactamase function by codon randomization and selectionNatural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme StabilityWeighted protein residue networks based on joint recurrences between residuesAmino acid sequence determinants of extended spectrum cephalosporin hydrolysis by the class C P99 beta-lactamase.New beta -lactamase inhibitory protein (BLIP-I) from Streptomyces exfoliatus SMF19 and its roles on the morphological differentiation.Design of potent beta-lactamase inhibitors by phage display of beta-lactamase inhibitory protein.Amino acid sequence requirements at residues 69 and 238 for the SME-1 beta-lactamase to confer resistance to beta-lactam antibiotics.Fine mapping of the sequence requirements for binding of beta-lactamase inhibitory protein (BLIP) to TEM-1 beta-lactamase using a genetic screen for BLIP function.Identification and characterization of beta-lactamase inhibitor protein-II (BLIP-II) interactions with beta-lactamases using phage display.Identification of a β-lactamase inhibitory protein variant that is a potent inhibitor of Staphylococcus PC1 β-lactamase.Use of periplasmic target protein capture for phage display engineering of tight-binding protein-protein interactions.An analysis of why highly similar enzymes evolve differentlyA fitness cost associated with the antibiotic resistance enzyme SME-1 beta-lactamaseDeep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations.Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases.Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases.Modeling and fitting protein-protein complexes to predict change of binding energyIdentification of the β-lactamase inhibitor protein-II (BLIP-II) interface residues essential for binding affinity and specificity for class A β-lactamasesProtein-protein docking with multiple residue conformations and residue substitutions.Identification of residues in beta-lactamase critical for binding beta-lactamase inhibitory protein.Binding properties of a peptide derived from beta-lactamase inhibitory protein.THz frequency spectrum of protein-solvent interaction energy using a recurrence plot-based Wiener-Khinchin method.Resistance to beta-lactamase inhibitor protein does not parallel resistance to clavulanic acid in TEM beta-lactamase mutants.Engineering Specificity from Broad to Narrow: Design of a β-Lactamase Inhibitory Protein (BLIP) Variant That Exclusively Binds and Detects KPC β-Lactamase.Role of β-lactamase residues in a common interface for binding the structurally unrelated inhibitory proteins BLIP and BLIP-II.Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1.Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 beta-lactamase with beta-lactamase inhibitory protein.Dissecting the protein-protein interface between beta-lactamase inhibitory protein and class A beta-lactamases.Functional analysis of active site residues of the fosfomycin resistance enzyme FosA from Pseudomonas aeruginosa.Structural and computational characterization of the SHV-1 beta-lactamase-beta-lactamase inhibitor protein interface.Detecting transitions in protein dynamics using a recurrence quantification analysis based bootstrap method.'Light up' protein-protein interaction through bioorthogonal incorporation of a turn-on fluorescent probe into β-lactamase.Efficient production of secretory Streptomyces clavuligerus β-lactamase inhibitory protein (BLIP) in Pichia pastoris.Tackling the Antibiotic Resistance Caused by Class A -Lactamases through the Use of -Lactamase Inhibitory ProteinDifferential active site requirements for NDM-1 β-lactamase hydrolysis of carbapenem versus penicillin and cephalosporin antibiotics
P2860
Q27652020-24BEE3E6-26E6-4761-91E8-A6586616CABFQ27657721-4CECBAEC-8663-4868-8AF8-9CB2727BB509Q27704563-902E72F0-B2FA-41C6-A70D-4CEAD6EEF1B3Q28364522-31B42390-E4A3-44DA-AACE-4F2255DA566DQ28547682-53B0E74D-228E-4ABD-8A00-26181902853FQ30374934-552EC8D8-E5D4-4842-9D0F-DA1284CD8B1CQ30731622-D874520D-BB32-44E0-A2EF-121464983E53Q30854268-28D3943A-69D5-4A13-A4C7-67601ADCF543Q30854317-7E24D98C-F5E0-4FC3-BE3B-F10BF573C3F2Q31133027-038D992A-48BD-468D-A8CF-FB59EF8F5927Q33434215-3CD44E89-E673-4015-BF11-5284562F3383Q33544102-E5AFB0B5-1324-4932-9F39-37F99B2B55E3Q33794586-737BAD47-4F34-4F09-99FC-8177727AA2D4Q34013420-87846BD0-FB1B-45E1-B874-DD527B60BFBFQ34616960-E9CC3AEE-E208-4118-8F68-081E309B8D71Q35945753-40ADF095-11E2-4CC7-A65F-157186FDA106Q36129525-02CB4F42-0D87-4B2F-A34C-F355EE62DDC9Q36158271-CE8D93CF-DD0E-40C2-A7A3-0ABF606240DBQ36298671-9957B510-B64A-444B-AE65-2EB035C8168FQ36898375-3957A2A1-877E-403E-9BA2-DB151AD4BEFFQ36928945-F00B3D90-AD7D-4B9F-B3E0-D574BE625D7FQ38269842-94732914-4597-4512-87C9-2DF9382E57EAQ38327464-9415959C-22C7-4001-9366-45D452276172Q39479019-396CD55E-C3A1-4D52-9B60-9D66F01F826FQ39644236-CBF87F72-F761-4737-8B3E-6A5CA706ED10Q39657859-1AC157A1-4920-44C2-AF81-895DBF9FC171Q40532268-C8BBA6F4-C61C-4230-AB0A-6279A351B40CQ42550799-820AA81A-B4E2-40EB-A592-4705F346E55BQ42949243-8A4CB327-5625-4DAA-A629-11F73A40E14CQ44559371-280DD3A5-8153-422D-81CA-24A8FBEE69C2Q45000448-B890A423-26D8-4840-B74F-9D303A64E220Q45291346-91EB8285-8726-478E-8F52-E4C60AAA308FQ46392280-F8628CA3-DEC2-4A0C-92FD-B26EF5E4E975Q47134706-FF7BC1FE-D615-4E32-895B-BFBBCB6A1BAFQ48310697-81E37341-8953-4EFD-BC49-3A0B95BB0C66Q55322279-DCAB4253-F44B-40EE-9A35-42589A2DB1C0Q57174160-B6B0A644-27B7-4AE8-86B9-939F92CE77A9Q58097719-2448D8F8-028A-43CC-A8E6-DF707691B940
P2860
Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of beta-lactamases.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Contributions of aspartate 49 ...... ry protein of beta-lactamases.
@en
type
label
Contributions of aspartate 49 ...... ry protein of beta-lactamases.
@en
prefLabel
Contributions of aspartate 49 ...... ry protein of beta-lactamases.
@en
P2093
P2860
P356
P1476
Contributions of aspartate 49 ...... ry protein of beta-lactamases.
@en
P2093
Palzkill T
Petrosino J
P2860
P304
P356
10.1074/JBC.274.4.2394
P407
P577
1999-01-01T00:00:00Z