Kinetics of avibactam inhibition against Class A, C, and D β-lactamases - Wikidata - wikimedia - TriplyDB

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

http://www.wikidata.org/entity/Q24617763

about

New β-Lactamase Inhibitors in the Clinic Beyond Susceptible and Resistant, Part III: Treatment of Infections due to Gram-Negative Organisms Producing Carbapenemases Insights into Newer Antimicrobial Agents Against Gram-negative Bacteria The Chemical Biology of Human Metallo-β-Lactamase Fold Proteins Crystal Structure of OXA-58 with the Substrate-Binding Cleft in a Closed State: Insights into the Mobility and Stability of the OXA-58 Structure Avibactam and Class C -Lactamases: Mechanism of Inhibition, Conservation of the Binding Pocket, and Implications for Resistance Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibition OP0595, a new diazabicyclooctane: mode of action as a serine β-lactamase inhibitor, antibiotic and β-lactam 'enhancer'Removal 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 Strain Crystal Structure of the Pseudomonas aeruginosa BEL-1 Extended-Spectrum β-Lactamase and its Complex with Moxalactam and Imipenem Investigations on recyclisation and hydrolysis in avibactam mediated serine β-lactamase inhibition New β-lactamase inhibitors: a therapeutic renaissance in an MDR world.Reclaiming the efficacy of β-lactam-β-lactamase inhibitor combinations: avibactam restores the susceptibility of CMY-2-producing Escherichia coli to ceftazidime.Antibiotics and bacterial resistance in the 21st century.Carbapenemase-producing Klebsiella pneumoniae.Therapy of Infections due to Carbapenem-Resistant Gram-Negative Pathogens Ceftazidime-avibactam: an evidence-based review of its pharmacology and potential use in the treatment of Gram-negative bacterial infections.Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers Interaction of Avibactam with Class B Metallo-β-Lactamases.Unexpected in vivo activity of ceftazidime alone and in combination with avibactam against New Delhi metallo-β-lactamase-producing Enterobacteriaceae in a murine thigh infection model.Effect of asparagine substitutions in the YXN loop of a class C β-lactamase of Acinetobacter baumannii on substrate and inhibitor kinetics.Unexpected challenges in treating multidrug-resistant Gram-negative bacteria: resistance to ceftazidime-avibactam in archived isolates of Pseudomonas aeruginosa.Pharmacokinetics and penetration of ceftazidime and avibactam into epithelial lining fluid in thigh- and lung-infected mice.Variants of β-lactamase KPC-2 that are resistant to inhibition by avibactam.Avibactam and inhibitor-resistant SHV β-lactamases Inhibition of Klebsiella β-Lactamases (SHV-1 and KPC-2) by Avibactam: A Structural Study.Activity of ceftazidime/avibactam against isogenic strains of Escherichia coli containing KPC and SHV β-lactamases with single amino acid substitutions in the Ω-loop.In vitro selection of ceftazidime-avibactam resistance in Enterobacteriaceae with KPC-3 carbapenemase.Characterization of a Carbapenem-Hydrolyzing Enzyme, PoxB, in Pseudomonas aeruginosa PAO1.Role of the Outer Membrane and Porins in Susceptibility of β-Lactamase-Producing Enterobacteriaceae to Ceftazidime-Avibactam Crystal Structures of KPC-2 and SHV-1 β-Lactamases in Complex with the Boronic Acid Transition State Analog S02030 Boronic Acid Transition State Inhibitors Active against KPC and Other Class A β-Lactamases: Structure-Activity Relationships as a Guide to Inhibitor Design β-Lactam Antibiotics Renaissance.In Vitro Susceptibility of Global Surveillance Isolates of Pseudomonas aeruginosa to Ceftazidime-Avibactam (INFORM 2012 to 2014).Carbapenem-Resistant Pseudomonas aeruginosa Bacteremia: Risk Factors for Mortality and Microbiologic Treatment Failure.Cyclic Boronates Inhibit All Classes of β-Lactamases.Fragment-based inhibitor discovery against β-lactamase β-lactam/β-lactamase inhibitor combinations: from then to now.Distinctive Binding of Avibactam to Penicillin-Binding Proteins of Gram-Negative and Gram-Positive Bacteria.Structural and mechanistic insights into the inhibition of class C β-lactamases through the adenylylation of the nucleophilic serine.

P2860

Q26747150-FD65D6FB-1F6B-4B69-839C-7241CDF6FA22 Q26747580-056343E0-B5D8-4D6E-8F7C-492662DCA012 Q26751255-09B66FD4-1464-407F-80B4-766C14F2BD38 Q26775167-F307CF37-B585-4167-A9D4-FD68A4F3C160 Q27333834-5551AFBD-E017-4201-8F45-372487E3C710 Q27684678-3A5D04C6-3778-4701-A069-55B17D39BDFB Q27696197-3EE9E5DD-BF42-4D26-BF21-0B177025998B Q27701037-08C7A052-C18E-40F7-B0F6-1AC7BCD4BC69 Q27704563-C6F8D595-9E77-4CBC-8455-273C87DF195F Q27728123-EB21631E-6D02-4773-8999-FEE113E94809 Q28834096-E59ECCF8-D442-44C1-9080-465EAA3C77C6 Q33622976-FFC29B4B-F6F8-4E6C-B37F-9CF140BA62F3 Q34058217-1CB96C9B-712C-4B41-86C6-3056A7B17B53 Q34156349-80D94C23-5869-4F22-B847-CFB43A510AFA Q34201937-BA4B402E-C7B3-479E-81B1-5B9FF51E7BFC Q34303970-37438711-6150-48F1-979F-7122245EB3C0 Q34402134-F14C909B-58D0-4C53-859C-14FE1E990B61 Q34498607-017562C1-255E-4ED4-A1DC-3604D235BDDD Q34533834-D31482A0-9B4D-4F59-A2D7-7D14F8906CFE Q34596918-2928E1CE-7572-4ED5-B5D9-BFE81F705730 Q35076850-57A9CFB0-1DB1-4D34-B156-347F50FB8D50 Q35105960-2154D7A8-7702-45F3-8F50-8B9387F8919C Q35168955-27E21A6A-6E7C-4018-BEC2-0F478E222BFE Q35746006-EA2DEE56-DC3D-47F0-B8C1-7D4474A3D97C Q35746285-11BCEA2D-80A7-4812-810E-CEF38C3E0A67 Q35764780-4B457064-1400-47CA-AF3D-4E8B9CFDBA02 Q35847267-8916177C-47DC-4BD4-BC0F-A377AB9C5A1D Q35960745-C7668262-E626-407C-AFE3-1E7A85D136D7 Q36571851-9D173F63-8CEC-4291-9D25-379430191523 Q36644679-D1C919F8-CF2A-4327-A539-3A9D4B7B10B7 Q36644761-08C4855E-FE44-487C-8601-193B3E9AB089 Q36644892-3AF8E725-0DBC-484B-B9EA-72C0B01B054A Q36683689-E6F2A1BF-65B5-4464-84A1-46FA9A55AFBC Q37120019-9357571E-A397-484D-9E03-76A2B538E340 Q37538614-7772D9A8-A511-4FE1-A78F-184030C028C4 Q37720801-09041D5C-0A63-45DE-BDF7-F243BBC3C4E2 Q38196443-0111504C-EFCD-4285-AD01-3E373A521B8A Q38264182-8855896E-378D-4141-B05D-DE23D8474AAB Q38367722-D3D80459-150A-4B41-A7E7-C311CED98BE7 Q38407413-8753938A-74C1-4DE6-A996-D53D5A60C2A0

P2860

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

http://www.wikidata.org/entity/Q24617763

description

2013 nî lūn-bûn

@nan

2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@ast

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@en

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@nl

type

label

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@ast

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@en

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@nl

prefLabel

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@ast

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@en

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@nl

P1433

Q24617763-A0DB42EE-53B7-4A92-AB28-CDDDD992B196

P1476

Q24617763-8E760CE6-4066-49E5-9B65-9D4866E43E12

P2093

Q24617763-1888901B-70C3-4359-8E55-5439162E384A

Q24617763-2000E611-D3F5-4DAC-A346-23534B0D5B1D

Q24617763-2050B7DB-847A-444C-956D-7828BC9CDC06

Q24617763-22FCD392-ABD8-4423-AAFA-A6BC066E0081

Q24617763-2FAA95CF-A078-4E48-BAED-D7F40A84E389

Q24617763-454CAA68-BE8E-4DCA-AB8D-CF6D1131CB61

Q24617763-4551201A-6FCA-4448-9521-45FC112CA586

Q24617763-5C02AB44-AA83-44F4-8651-50F5504AFCAE

Q24617763-6B1B638A-CAAC-4121-BE35-1ED48B696C2A

Q24617763-83A1EE06-A875-4443-8337-14F6338719BB

P2860

Q24617763-03DC4F2F-4946-4BBB-BDAB-E3A8696298F0

Q24617763-060F9952-9F2F-4228-9621-0A2023600D1D

Q24617763-0BAA6527-EAD9-447B-A6C9-5CCB96DCC707

Q24617763-153BF02E-684B-4AE6-A105-8E4DADE834E2

Q24617763-1C6204DC-1028-453F-AF41-F1FA49891903

Q24617763-1FCA8834-5589-4F30-90CE-216E088E252C

Q24617763-36394B5D-EA32-4FC5-B237-212DE85090E9

Q24617763-396D1782-AB75-4E78-8C3C-0DFB59C6AB57

Q24617763-450D2AC6-EE15-4CCE-A612-D1AFB022CF33

Q24617763-59345F41-32A9-4028-8489-BBD219FB955B

P304

Q24617763-7743D644-CB9A-4073-8D35-CE4FE2AAA7FB

P31

Q24617763-84D2D579-453B-480D-AD32-7C4023504C78

P3181

Q24617763-750443BA-BF11-4BEC-A7F5-003F29291B2D

P356

Q24617763-BE0BAB86-9057-4D15-BE60-BB376B4D845B

P407

Q24617763-92FEBE17-F37F-4F51-8773-178125F44FFC

P433

Q24617763-C5AB0421-0624-44A9-B8BB-2AE5A4CBE941

P478

Q24617763-17FEB96E-5449-4BF8-9412-BED099C7CB6F

P577

Q24617763-382AD334-57F8-48C3-AC22-473823E8CA7E

P698

Q24617763-1797CC3E-7AD9-42BB-B05A-BC9FCDC73DF9

P921

Q24617763-255903AF-0C57-4DED-BE6F-EEB169C5076A

P932

Q24617763-5D114166-9523-40E8-80B3-72F5CBCEAE0E

P3181

P356

JBC.M113.485979

P1433

Journal of Biological Chemistry

P1476

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

@en

P2093

David E Ehmann

http://www.w3.org/2001/XMLSchema#string

Grant K Walkup

http://www.w3.org/2001/XMLSchema#string

Haris Jahic

http://www.w3.org/2001/XMLSchema#string

Jason Thresher

http://www.w3.org/2001/XMLSchema#string

Jun Hu

http://www.w3.org/2001/XMLSchema#string

Ning Gao

http://www.w3.org/2001/XMLSchema#string

Philip L Ross

http://www.w3.org/2001/XMLSchema#string

Rong-Fang Gu

http://www.w3.org/2001/XMLSchema#string

Stephania Livchak

http://www.w3.org/2001/XMLSchema#string

Stewart L Fisher

http://www.w3.org/2001/XMLSchema#string

P2860

"Stormy waters ahead": global emergence of carbapenemases

Updated functional classification of beta-lactamases

Three decades of beta-lactamase inhibitors

Critical involvement of a carbamylated lysine in catalytic function of class D -lactamases

Evolution to carbapenem-hydrolyzing activity in noncarbapenemase class D -lactamase OXA-10 by rational protein design

Structural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC -Lactamases

NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis

One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase

Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes

Inhibitor resistance in the KPC-2 beta-lactamase, a preeminent property of this class A beta-lactamase.

P304

27960-71

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2343163

http://www.w3.org/2001/XMLSchema#string

P356

10.1074/JBC.M113.485979

http://www.w3.org/2001/XMLSchema#string

P407

P433

39

http://www.w3.org/2001/XMLSchema#string

P478

288

http://www.w3.org/2001/XMLSchema#string

P577

2013-09-27T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

23913691

http://www.w3.org/2001/XMLSchema#string

P921

P932

3784710

http://www.w3.org/2001/XMLSchema#string