Mechanistic studies of the inactivation of TEM-1 and P99 by NXL104, a novel non-beta-lactam beta-lactamase inhibitor. - Wikidata - awgldk - TriplyDB

Mechanistic studies of the inactivation of TEM-1 and P99 by NXL104, a novel non-beta-lactam beta-lactamase inhibitor.

Mechanistic studies of the inactivation of TEM-1 and P99 by NXL104, a novel non-beta-lactam beta-lactamase inhibitor.

http://www.wikidata.org/entity/Q42046174

about

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases 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 Avibactam and Class C -Lactamases: Mechanism of Inhibition, Conservation of the Binding Pocket, and Implications for Resistance 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 Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance Biochemical characterization of CTX-M-15 from Enterobacter cloacae and designing a novel non-β-lactam-β-lactamase inhibitor Investigations on recyclisation and hydrolysis in avibactam mediated serine β-lactamase inhibition Antibiotics in the clinical pipeline at the end of 2015.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.The enzymes of β-lactam biosynthesis.Ceftazidime-avibactam: a novel cephalosporin/β-lactamase inhibitor combination.Investigational antimicrobial agents of 2013.Ceftazidime-avibactam: an evidence-based review of its pharmacology and potential use in the treatment of Gram-negative bacterial infections.Antibiotic adjuvants: diverse strategies for controlling drug-resistant pathogens.Interaction of Avibactam with Class B Metallo-β-Lactamases.Platforms for antibiotic discovery.Activity of NXL104 in combination with beta-lactams against genetically characterized Escherichia coli and Klebsiella pneumoniae isolates producing class A extended-spectrum beta-lactamases and class C beta-lactamases.In vitro activity of ceftazidime combined with NXL104 versus Pseudomonas aeruginosa isolates obtained from patients in Canadian hospitals (CANWARD 2009 study).Unexpected challenges in treating multidrug-resistant Gram-negative bacteria: resistance to ceftazidime-avibactam in archived isolates of Pseudomonas aeruginosa.Avibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitor Comparative in vitro and in vivo efficacies of human simulated doses of ceftazidime and ceftazidime-avibactam against Pseudomonas aeruginosa.Characterization of a Carbapenem-Hydrolyzing Enzyme, PoxB, in Pseudomonas aeruginosa PAO1.Kinetics of the Interaction between BAL29880 and LK157 and the Class C β-Lactamase CHE-1 Single- and multiple-dose study to determine the safety, tolerability, and pharmacokinetics of ceftaroline fosamil in combination with avibactam in healthy subjects Efficacy and Safety of Ceftazidime-Avibactam Plus Metronidazole Versus Meropenem in the Treatment of Complicated Intra-abdominal Infection: Results From a Randomized, Controlled, Double-Blind, Phase 3 Program.In Vitro Susceptibility of Global Surveillance Isolates of Pseudomonas aeruginosa to Ceftazidime-Avibactam (INFORM 2012 to 2014).Metallo-β-lactamase structure and function.New β-lactam-β-lactamase inhibitor combinations in clinical development.Current strategies for the treatment of complicated intraabdominal infections.β-Lactamase inhibitors: a review of the patent literature (2010 - 2013).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.Ceftazidime-avibactam for the treatment of complicated urinary tract infections and complicated intra-abdominal infections.Recent developments in antibiotic agents for the treatment of complicated intra-abdominal infections.Ceftazidime-avibactam: novel antimicrobial combination for the treatment of complicated urinary tract infections.Ceftazidime-avibactam (CTZ-AVI) as a treatment for hospitalized adult patients with complicated intra-abdominal infections.The road to avibactam: the first clinically useful non-β-lactam working somewhat like a β-lactam.

P2860

Q24617763-878AEC7F-9348-43BE-8A9A-3B41CA3853DA Q27676626-AEA95069-227E-4823-80E8-992876E07829 Q27679097-8CC41E22-CD85-43EA-8A99-B7465D56B91B Q27684678-BE0FE81E-D7B6-4C44-9446-8E6807D293D7 Q27704563-199A011D-4E36-429D-B792-64BFA5CC7396 Q28084628-6B0A9B74-8EEA-4F2B-9EF7-4B023BAB82A3 Q28486539-0C6466EC-DD68-4AB7-8BF9-9E8F3CD1160C Q28834096-B3D60800-27AF-485A-B159-035F5739AF9F Q30249262-D4F85F2B-2295-48D7-8DEA-E86AB80D49F5 Q33622976-BF639D45-C15A-48BC-AAE9-30B0229ED146 Q34058217-B4042E22-BF35-4804-B062-E7A5A80CB39D Q34310470-B3A2BF08-5573-4C70-A305-3EE3C5A9F333 Q34325573-91D3626D-DC6E-4E8C-91E3-6B2B2ED66EE5 Q34375204-D71E4A2D-7F4E-4758-861D-42BDD18FE9F7 Q34402134-FC23B15E-21BB-43BD-A6CB-6570633581B4 Q34447679-9D36FAFD-1C5F-4B63-83AD-F24CC9169C90 Q34533834-C30D51A2-4040-4145-97D7-AA9D28B8829F Q34694926-B57FD032-9958-4B96-9341-86489B0C42FD Q34932937-6295CC89-99A4-4B91-8D2C-DE50FA7282DB Q35004966-2686F47B-844A-4BEB-BA73-B2DCE0CDA479 Q35105960-E905B370-6157-48E1-972F-779AB5E5936C Q36122731-B801F8E6-9B26-4DB9-B0CE-3938C9EE4FAF Q36396244-E9958CC2-29A0-45AF-A41F-016E384941ED Q36571851-CFC82050-A970-4DCD-9FE8-37DF16174E20 Q36644853-070B3396-1952-4A44-8065-195849DD9008 Q36667104-3F703EB9-FCAE-4D52-8EA1-D755A7FD1011 Q36915096-2A3C85A3-A483-4545-BEEB-A3F64B253CF5 Q37120019-1C54F20B-348A-46D7-915D-3A06DEF6F53A Q38060809-0E82EAE1-7CE0-4182-B7B3-E853A50DE888 Q38076455-DFC185A5-0EA9-45E3-A5EB-B0FD4413D427 Q38123247-B957862A-B390-4F94-9FC3-BC46013FECD2 Q38130715-1280459B-6212-44EE-9EA2-D66C9DE157E2 Q38264182-9641F268-8A8E-4A1D-8EA3-699873AD9B0A Q38367722-C34E038A-A6FC-446B-AA97-E1EE85E6A2AB Q38407413-D2F362B9-472B-41F1-B11E-9A92FE4512FF Q38595451-59C8264A-57F2-40BC-8BD1-979FC4C8022D Q38648594-E6E6117F-76BD-4993-82B6-181EFE299D5E Q38740494-88C50DBF-B47D-4175-B15D-FEDF84D301C0 Q38797485-295ECF22-EE60-4C59-AC04-A5CDF5BDAA10 Q38850240-E6181D91-F3EE-4BC7-8236-7A4CF06255C4

P2860

Mechanistic studies of the inactivation of TEM-1 and P99 by NXL104, a novel non-beta-lactam beta-lactamase inhibitor.

http://www.wikidata.org/entity/Q42046174

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

2010年學術文章

@zh

2010年學術文章

@zh-hant

name

Mechanistic studies of the ina ...... ctam beta-lactamase inhibitor.

@en

Mechanistic studies of the ina ...... ctam beta-lactamase inhibitor.

@nl

type

label

Mechanistic studies of the ina ...... ctam beta-lactamase inhibitor.

@en

Mechanistic studies of the ina ...... ctam beta-lactamase inhibitor.

@nl

prefLabel

Mechanistic studies of the ina ...... ctam beta-lactamase inhibitor.

@en

Mechanistic studies of the ina ...... ctam beta-lactamase inhibitor.

@nl

P1433

Q42046174-8C77C1CE-086B-42B1-B0AB-5F54CD4CE9A1

P1476

Q42046174-08315351-8BE5-4201-9B96-C31D7501BDCB

P2093

Q42046174-0305E8D7-E5CE-4C43-9435-A1424CC16C14

Q42046174-2C8F66F5-EA70-4DB5-8AFB-CAA6595558B6

Q42046174-79DD2D87-30B8-49B2-880A-BAB7272C2809

Q42046174-8DCA859D-C321-4AC1-B49D-BC8DA41B4CE2

Q42046174-B536CAE7-47BD-4EDC-901C-9B8C46ECFEF2

Q42046174-D457239E-B15C-4B75-AEFF-E22118B06220

Q42046174-E9D1E87A-BE42-4C34-B8FF-55F1A3AC33C9

Q42046174-F500CB2A-47C0-4605-8ADA-F3D0A664B91F

P2860

Q42046174-00FCBC1C-D15A-4D2E-B3CD-02A710AE1743

Q42046174-0168D4A6-4F6A-4429-8553-BE6DDB2B9FA8

Q42046174-03972CEF-ABF2-4FBC-A122-CF469C5FA9F0

Q42046174-097F9E00-5D08-4AAD-B71A-7707A6EF8D3C

Q42046174-0A8ADE5F-541D-45A0-98F5-960B4C0E0551

Q42046174-0D0599C5-77CD-4F38-8D9F-4A6A241A1959

Q42046174-0EE9D7B1-0A07-42FE-9FD6-EDC4EA6C9131

Q42046174-109401EB-D583-4ADB-B932-9A258E4A642C

Q42046174-18D53C11-B0E0-474F-B21E-511D4263BC83

Q42046174-1C62F813-5640-47ED-8A12-E47A67C95027

P304

Q42046174-F2C387AF-2056-45B6-BD9A-0FD7D304812E

P31

Q42046174-9D920C09-8301-4BBD-B7BE-6CEE3FC7FA82

P356

Q42046174-503FF253-B290-4466-AF4B-388B329D2CB6

P407

Q42046174-40869CD6-A916-4971-B006-7B0FB52E0907

P433

Q42046174-8915993D-8435-476B-8A87-75746EEBE456

P478

Q42046174-41F7175A-9FA6-4F87-8A56-E220A4729A21

P577

Q42046174-EA812309-D3ED-4316-939A-6CBA87611F75

P5875

Q42046174-E223E4E5-413A-41C3-9235-445FA1B66176

P698

Q42046174-9545B7F8-033D-47FC-8E6D-9123C439B6F4

P932

Q42046174-48055B7A-5348-4B81-84FF-0FD6A8520A59

P356

P1433

Antimicrobial Agents and Chemotherapy

P1476

Mechanistic studies of the ina ...... ctam beta-lactamase inhibitor.

@en

P2093

Christine Miossec

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

Jean-Marie Frère

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

Jean-Michel Bruneau

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

Kenneth Coleman

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

Marie-Claude Péchereau

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

Michael T Black

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

Monique Claudon

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

Thérèse Stachyra

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

P2860

Clavulanic acid: a beta-lactamase-inhiting beta-lactam from Streptomyces clavuligerus

Three decades of beta-lactamase inhibitors

Sulbactam forms only minimal amounts of irreversible acrylate-enzyme with SHV-1 beta-lactamase

Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution

Inhibition of class A and class C beta-lactamases by penems: crystallographic structures of a novel 1,4-thiazepine intermediate

Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog

Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution

Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration

Why the extended-spectrum beta-lactamases SHV-2 and SHV-5 are "hypersusceptible" to mechanism-based inhibitors

Overexpression and biosynthetic deuterium enrichment of TEM-1 beta-lactamase for structural characterization by magnetic resonance methods.

P304

5132-5138

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

P31

scholarly article

P356

10.1128/AAC.00568-10

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

P407

P433

12

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

P478

54

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

P577

2010-10-04T00:00:00Z

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

P5875

47336517

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

P698

20921316

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

P932

2981269

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