Interactions of ceftobiprole with beta-lactamases from molecular classes A to D. - Wikidata - wikimedia - TriplyDB

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

http://www.wikidata.org/entity/Q42584480

about

New treatment options against gram-negative organisms Three decades of beta-lactamase inhibitors Antimicrobials: a global alliance for optimizing their rational use in intra-abdominal infections (AGORA).Ceftobiprole for the treatment of pneumonia: a European perspective Structural Insights into the Anti-methicillin-resistant Staphylococcus aureus (MRSA) Activity of Ceftobiprole Newer antibacterial drugs for a new century.Safety profiles of old and new antimicrobials for the treatment of MRSA infections.In vivo activity of ceftobiprole in murine skin infections due to Staphylococcus aureus and Pseudomonas aeruginosa.Resistance and the management of complicated skin and skin structure infections: the role of ceftobiprole.Ceftobiprole medocaril: a review of its use in patients with hospital- or community-acquired pneumonia.Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms.Current and novel antibiotics against resistant Gram-positive bacteria Emerging agents to combat complicated and resistant infections: focus on ceftobiprole Efficacy of ceftobiprole Medocaril against Enterococcus faecalis in a murine urinary tract infection model Cefepime: a reappraisal in an era of increasing antimicrobial resistance.Ceftobiprole: an extended-spectrum anti-methicillin-resistant Staphylococcus aureus cephalosporin.Molecular basis and phenotype of methicillin resistance in Staphylococcus aureus and insights into new beta-lactams that meet the challenge.Ceftobiprole: first cephalosporin with activity against methicillin-resistant Staphylococcus aureus.Beta-lactams and beta-lactamase-inhibitors in current- or potential-clinical practice: a comprehensive update.Update on the treatment of Pseudomonas aeruginosa pneumonia.Ceftobiprole: a new broad spectrum cephalosporin.Ceftobiprole: a new cephalosporin for the treatment of skin and skin structure infections.Resistant pathogen-associated skin and skin-structure infections: antibiotic options.Pharmacokinetic and pharmacodynamics evaluation of ceftobiprole medocaril for the treatment of hospital-acquired pneumonia.New antibiotics for bad bugs: where are we?β-lactams against emerging 'superbugs': progress and pitfalls.Development of novel antibacterial drugs to combat multiple resistant organisms.One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams Determination of an inoculum effect with various cephalosporins among clinical isolates of methicillin-susceptible Staphylococcus aureus.In vitro properties of BAL30072, a novel siderophore sulfactam with activity against multiresistant gram-negative bacilli.VIM-15 and VIM-16, two new VIM-2-like metallo-beta-lactamases in Pseudomonas aeruginosa isolates from Bulgaria and Germany.New variant of CTX-M-type extended-spectrum beta-lactamases, CTX-M-71, with a Gly238Cys substitution in a Klebsiella pneumoniae isolate from Bulgaria Effect of MexXY overexpression on ceftobiprole susceptibility in Pseudomonas aeruginosa.Differential selection of single-step AmpC or efflux mutants of Pseudomonas aeruginosa by using cefepime, ceftazidime, or ceftobiprole Hydrolysis and inhibition profiles of beta-lactamases from molecular classes A to D with doripenem, imipenem, and meropenem.In vitro susceptibility of characterized β-lactamase-producing strains tested with avibactam combinations.Overproduction of K1 enzyme in Klebsiella oxytoca clinical isolates against ceftazidime, cefepime and ceftobiprole.

P2860

Q21194906-FF75B39D-F46E-4597-B4D4-D82F9BF923B5 Q24646623-EADA22C9-790B-413F-B37B-6B613B4F5E33 Q26739860-E99D4320-7F4D-4D4A-B057-EC0B21BB3E13 Q26796463-BFD29185-42D4-4C05-924B-FC9959A1C699 Q27670836-396F7960-DCE5-4812-8871-F849E16555A6 Q30433333-4D0007F9-B984-4DED-8291-92F6D342BBAD Q33429168-E58AB23F-FAE7-4D41-996C-508590E2EB89 Q33559139-D11018F4-E430-48CB-9CF7-4D2AEC44C78A Q34187667-FED04D64-7834-422B-A1EE-B144E8178032 Q34433342-DC988D76-A77D-46B6-897E-4ABC68CF8AD2 Q34571608-32708E89-E15F-4C20-BD1A-4F7C87E3171A Q35007624-26F60347-2064-42C7-9095-E5F8E16C525B Q35026521-C79290A6-4353-4FF4-9F35-6C5BCE049C12 Q35026567-D52B0B16-EB77-406F-AA19-3D95A85277F3 Q36018587-1B9ECA6C-E13C-454E-89AF-7ECB77C6E99B Q37079350-AB23C54E-291F-48A3-8BCF-55AF99847F6D Q37162872-EB3FC35D-EE21-4FEE-A4DA-674ABEF6CE5A Q37392891-9249B849-9390-4CEB-815B-B31F5C9C76F1 Q37461413-54E6100A-8E5E-4B16-A808-5C0A52411C6B Q37514259-2C33453B-12B8-4942-842A-8D31FB211C64 Q37516904-C160248C-5C5C-4AE9-A1AC-38C891DB4977 Q37519733-8D6949B1-65AA-40F2-901F-B4D335216A45 Q37593094-BB493CA0-61D0-4518-963C-7D1661DA60E0 Q37785546-696893AF-0BB8-484F-85B9-8071E6678236 Q38099393-342174FA-8CB4-4EE0-987B-86A3554DECCD Q38132217-F71EDABA-971D-4189-9695-CFCA9673659A Q38177344-00D19302-A019-4B2C-898C-C6FF84B0C3E5 Q38350301-34083DC7-5195-40B9-90DB-E575FAB3B760 Q38712471-B732196F-52FB-4198-A82A-AD6F4FAE9E49 Q40336487-2E626717-FEFD-44F8-89DB-DCD6948E036B Q40751280-DD7EEEAA-058D-47EE-BF6D-E966D6C04B06 Q41337222-7E54D718-4C93-404B-BFAE-B5DE5C95542A Q41774142-CB25F64F-AD8C-47F7-BB8B-9EDC101658C5 Q41901627-57D652E9-9E59-40E7-858A-1D851736F9F1 Q42089045-75E20342-4D8E-4244-B652-F1DFB89B79BE Q42099309-096E8BA2-01E0-4761-8E6B-A3870413DBC4 Q43144149-2B7B1FC3-1DA4-4054-AE5B-A4B6A3A5BC8A Q45945760-CE4730E9-5B62-4247-8002-818613308358

P2860

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

http://www.wikidata.org/entity/Q42584480

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

@en

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

@nl

type

label

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

@en

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

@nl

prefLabel

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

@en

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

@nl

P1433

Q42584480-0A5FE560-C0CC-4349-83B3-01BB3C705689

P1476

Q42584480-1B93CB37-1227-4645-B684-C6C550D820E8

P2093

Q42584480-029FE3BE-BC6A-4D6C-B91C-EE73CFB9D204

Q42584480-79BD63AD-3D9F-41B8-9ABC-BF366EA17612

Q42584480-9AA091CC-8DFF-4AB4-A3FC-76FBDC39E1E7

Q42584480-A2B1B880-16DD-4E26-A7CA-E88E36E4BBB1

Q42584480-C7E41FC3-9CAE-4C41-98C0-3B7F586AF689

P2860

Q42584480-0B14A8F3-0EF7-4B13-BAFC-B6221D3F38F5

Q42584480-26A49F21-3302-45D1-9A91-DF7FFCF859F6

Q42584480-319CECA2-F71B-4AB1-B170-12E876DA180E

Q42584480-325196A6-13D3-4D33-A79C-CDF0D7B6E3D4

Q42584480-34EC2863-9FA6-4AE5-8E8F-481DD1A4AA52

Q42584480-38650082-57D3-48FD-9AF9-3CD14CE5D0E1

Q42584480-3DC70D97-30F0-44FD-B9F6-BD3AD5F2CF9D

Q42584480-3F5054CE-4782-4693-8181-33C9F1456A0B

Q42584480-4637C8F7-892E-4BEA-BF2B-1508F63C18D9

Q42584480-49E41CFC-7401-49B8-8376-9573BF295AC4

P304

Q42584480-EE132D23-63F4-43C1-9A3E-92DFF359CE61

P31

Q42584480-0F054165-7EE9-4402-801B-90FEF1940E66

P356

Q42584480-8A13BD17-D4BA-4540-B97D-ED52CD545F40

P407

Q42584480-86738CEF-4725-4414-9657-B223D5E3D568

P433

Q42584480-712B0A56-E897-47DB-81E9-BD80E52C048F

P478

Q42584480-E50FEEB9-1CD0-42A8-BEC9-2D30BB8496AA

P577

Q42584480-0F772EAA-C48B-4A5B-B5E0-83C594FE0D3C

P698

Q42584480-B71EC180-7D2B-424D-8072-08E9A342C4D5

P932

Q42584480-91B7E7BE-269F-42A5-A1D9-0901AB841DB7

P356

P1433

Antimicrobial Agents and Chemotherapy

P1476

Interactions of ceftobiprole with beta-lactamases from molecular classes A to D.

@en

P2093

Anne Marie Queenan

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

Karen Bush

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

Malcolm G P Page

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

Malgosia Kania

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

Wenchi Shang

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

P2860

Extended-spectrum beta-lactamases: a clinical update

In vitro and in vivo properties of Ro 63-9141, a novel broad-spectrum cephalosporin with activity against methicillin-resistant staphylococci

Extended-spectrum beta-lactamases in the 21st century: characterization, epidemiology, and detection of this important resistance threat

Antimicrobial resistance: the example of Staphylococcus aureus

A functional classification scheme for beta-lactamases and its correlation with molecular structure

Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction

The amino acid sequence of Staphylococcus aureus penicillinase

Metallo-beta-lactamases: the quiet before the storm?

Regulation of inducible AmpC beta-lactamase expression among Enterobacteriaceae.

First nosocomial outbreak of Pseudomonas aeruginosa producing an integron-borne metallo-beta-lactamase (VIM-2) in the United States

P304

3089-3095

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

P31

scholarly article

P356

10.1128/AAC.00218-07

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

P407

P433

9

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

P478

51

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

P577

2007-06-25T00:00:00Z

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

P698

17591851

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

P932

2043179

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