β-Lactamase inhibition by avibactam in Mycobacterium abscessus. - Wikidata - wikimedia - TriplyDB

β-Lactamase inhibition by avibactam in Mycobacterium abscessus.

β-Lactamase inhibition by avibactam in Mycobacterium abscessus.

http://www.wikidata.org/entity/Q38927000

about

Impact of β-lactamase inhibition on the activity of ceftaroline against Mycobacterium tuberculosis and Mycobacterium abscessus.Hydrolysis of clavulanate by Mycobacterium tuberculosis β-lactamase BlaC harboring a canonical SDN motif.Deletion of a dehydratase important for intracellular growth and cording renders rough Mycobacterium abscessus avirulent The distinct fate of smooth and rough Mycobacterium abscessus variants inside macrophages.Secretome Prediction of Two M. tuberculosis Clinical Isolates Reveals Their High Antigenic Density and Potential Drug Targets.The Diverse Cellular and Animal Models to Decipher the Physiopathological Traits of Mycobacterium abscessus Infection.Combinations of avibactam and carbapenems exhibit enhanced potencies against drug-resistant Mycobacterium abscessus.β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.Spotlight on ceftazidime/avibactam: a new option for MDR Gram-negative infections.Deciphering and Imaging Pathogenesis and Cording of Mycobacterium abscessus in Zebrafish Embryos.Bedaquiline inhibits the ATP synthase in Mycobacterium abscessus and is effective in infected zebrafish.Inhibition of the β-Lactamase BlaMab by Avibactam Improves the In Vitro and In Vivo Efficacy of Imipenem against Mycobacterium abscessus.Bactericidal and intracellular activity of β-lactams against Mycobacterium abscessus.Controlling Extra- and Intramacrophagic Mycobacterium abscessus by Targeting Mycolic Acid Transport Mycobacterium abscessus Complex Infections in Children: A Review.Inhibition by Avibactam and Clavulanate of the β-Lactamases KPC-2 and CTX-M-15 Harboring the Substitution N132G in the Conserved SDN Motif.galK-based suicide vector mediated allelic exchange in Mycobacterium abscessus.Establishment and validation of Galleria mellonella as a novel model organism to study Mycobacterium abscessus infection, pathogenesis and treatment.Inhibition of β-lactamases of mycobacteria by avibactam and clavulanate.Mechanistic and Structural Insights Into the Unique TetR-Dependent Regulation of a Drug Efflux Pump in Mycobacterium abscessus.NTM drug discovery: status, gaps and the way forward.Nontuberculous Mycobacteria in Cystic Fibrosis.Glycopeptidolipids, a Double-Edged Sword of the Mycobacterium abscessus Complex.Teicoplanin - Tigecycline Combination Shows Synergy Against Mycobacterium abscessus.and β-Lactams: Emerging Insights and Potential Opportunities The Role of Antibiotic-Target-Modifying and Antibiotic-Modifying Enzymes in Drug Resistance

P2860

Q35385697-8FB73CCA-F745-4669-952E-A1383D2CAF03 Q35960711-6D76C4D5-1251-4AEF-AD9B-9DD8BEB2CC45 Q37126863-AF5FD8F9-F7C1-41AB-9AF2-6FEED26BACBC Q37464141-7778053B-4A92-4552-8E2D-DF5AAF5376BB Q37627084-7557107D-9A93-4943-B2A8-4E55A68484E1 Q37735996-B6A7F7FD-12EF-46E0-AE86-DC84FA0EAD7E Q38741819-9B975028-D4E2-4657-B9F8-6DAE83DC7283 Q38811605-2371D966-0610-4B26-B17F-9D6F51B1EE26 Q38901844-E8F9CB7A-CD8D-42EE-88D3-2998C15A9ADF Q38962641-8F52B9AF-D233-4202-9A09-5CEFEDE4B198 Q40093529-BBC02F73-7A8A-4946-95E3-771AAB51D5E3 Q40368667-9D898FE1-B4FC-42E7-B733-F867062305EE Q40772367-AE0ADE04-EEED-4840-B476-47CFF546046C Q41619575-D57FFD47-E34F-4A1E-9EF5-2C27AA97F970 Q41990551-1BE6177F-9656-4AB9-B45E-D24BEB53680A Q42319612-F0BC46FF-11CB-4D2F-ADFB-BCABD50EACC7 Q47762869-E12AB472-9B44-4DF0-AB3E-22930856242B Q50044324-D6DB36C3-0591-4E7D-A96E-F0927ABCF104 Q51225225-84F2F08F-A730-4AC2-BAD7-F76C53C689FE Q52314897-360DB880-D722-4B36-AE1E-7D842BA1013E Q52596288-76B8FBE6-3BCF-4AD4-8E62-8B5E48A9BC8B Q52768051-5A516320-C366-4F6F-BE32-75AF36A86883 Q55323579-D993BD3B-8CE3-4ABC-97BF-10DCA50BA7EB Q55381713-5C06B27C-8069-483C-AA57-82A68735004A Q57492057-CC43C66D-BD59-4AF8-88B8-FD2391AABBD4 Q58746601-3133DB6E-72E5-4650-99A7-FE1BAE502C3C

P2860

β-Lactamase inhibition by avibactam in Mycobacterium abscessus.

http://www.wikidata.org/entity/Q38927000

description

2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

2014年论文

@zh

2014年论文

@zh-cn

name

β-Lactamase inhibition by avibactam in Mycobacterium abscessus.

@en

type

label

β-Lactamase inhibition by avibactam in Mycobacterium abscessus.

@en

prefLabel

β-Lactamase inhibition by avibactam in Mycobacterium abscessus.

@en

P1433

Q38927000-310E1BED-142A-48E2-B9FD-058BCE8272BD

P1476

Q38927000-9A1A9DDB-78AA-4D5E-BED9-2DCAFC06C621

P2093

Q38927000-0BBD7614-15C0-4005-98C9-26C72FB88227

Q38927000-1CB72C62-54BE-4CB5-86DC-18279B11C5B3

Q38927000-303EA768-4174-42E4-AF84-F46F974A5546

Q38927000-3B9CA1FB-70F1-4CBE-967A-B16D6056C376

Q38927000-6881AFD4-49CA-4F34-BF0F-97933C68C25C

Q38927000-90D353ED-CA27-47A3-8D98-8220514ED72D

Q38927000-AF696922-AA26-42AF-85E1-C45F3A826ED2

Q38927000-BA775056-2CF6-4E66-AE8C-34FB290ED087

P2860

Q38927000-17472D08-9796-44FD-96D5-652271D8358A

Q38927000-1760F805-9E2A-4756-B6A6-409649D956EB

Q38927000-24A7295C-A72A-4A36-8D51-B2BA456224AC

Q38927000-26509610-7C01-403E-953C-FE8C5EBE4387

Q38927000-2DE4873E-0D7B-4697-9E7D-A6638DB8DAA2

Q38927000-341A3F0D-3E7A-4E7C-832D-18DD712B174B

Q38927000-39CC16E1-CF52-4E22-98D6-7D718A754CD5

Q38927000-3F6F6402-C24A-40CB-9E84-0B0F94A2488C

Q38927000-400DEC01-704D-42C1-BE44-A2229C6B92EC

Q38927000-456B55EB-1EFE-4644-A903-75FBC07F5B2A

P304

Q38927000-E91AE378-9A48-45E7-8521-CAA45C419478

P31

Q38927000-608ADE29-6062-4EBE-960B-C1CB13268438

P356

Q38927000-FC709D2B-EF47-4801-9405-A732ABF3BF0D

P407

Q38927000-B351478B-85FC-4B1B-9DA2-6EE9BF1FCA3E

P433

Q38927000-2952A6F0-3047-4E2D-A753-86ABE187834B

P478

Q38927000-78527FAA-2AAC-4F90-AF85-8286150B4A74

P50

Q38927000-010D43CF-23B8-4586-91C1-DB96D674BEF4

Q38927000-5A5FE67F-6A06-4977-8538-ECDE229E352F

Q38927000-64E71BD8-1794-4222-9FC3-F0515653DB43

Q38927000-6BE00689-1918-4068-82E1-ACBBA4FC987E

Q38927000-9DD54867-B118-4142-97D4-F4E8D2112A01

P577

Q38927000-154E9B21-8C13-4A70-9DCE-240295F16C1F

P5875

Q38927000-94130D80-6082-4B61-A538-AD6E4BD84A2F

P698

Q38927000-E4431FD2-3238-46C9-B379-0146D5D0C768

P356

P1433

Journal of Antimicrobial Chemotherapy

P1476

β-Lactamase inhibition by avibactam in Mycobacterium abscessus.

@en

P2093

Anne-Laure Lefebvre

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

Delphine Dorchene

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

Jean-Louis Gaillard

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

Jean-Luc Mainardi

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

Laurent Gutmann

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

Mélanie Cortes

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

Tiffany Lesne

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

Vincent Dubée

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

P2860

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

Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis

NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis

Proposal of Mycobacterium peregrinum sp. nov., nom. rev., and elevation of Mycobacterium chelonae subsp. abscessus (Kubica et al.) to species status: Mycobacterium abscessus comb. nov

The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation

Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics

Kinetic features of L,D-transpeptidase inactivation critical for β-lactam antibacterial activity

Non mycobacterial virulence genes in the genome of the emerging pathogen Mycobacterium abscessus

In vivo assessment of drug efficacy against Mycobacterium abscessus using the embryonic zebrafish test system.

Meropenem/clavulanate and linezolid treatment for extensively drug-resistant tuberculosis.

P304

1051-1058

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

P31

scholarly article

P356

10.1093/JAC/DKU510

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

P407

P433

4

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

P478

70

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

P50

Jean-Louis Herrmann

Jean-Emmanuel Hugonnet

P577

2014-12-18T00:00:00Z

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

P5875

269768139

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

P698

25525201

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