Contribution of penicillin-binding protein homologs to antibiotic resistance, cell morphology, and virulence of Listeria monocytogenes EGDe. - Wikidata - awgldk - TriplyDB

Contribution of penicillin-binding protein homologs to antibiotic resistance, cell morphology, and virulence of Listeria monocytogenes EGDe.

Contribution of penicillin-binding protein homologs to antibiotic resistance, cell morphology, and virulence of Listeria monocytogenes EGDe.

http://www.wikidata.org/entity/Q34973702

about

Crystal Structures of Bifunctional Penicillin-Binding Protein 4 from Listeria monocytogenes Lantibiotic resistance.Comparative analysis of extracellular and intracellular proteomes of Listeria monocytogenes strains reveals a correlation between protein expression and serovar How Listeria monocytogenes organizes its surface for virulence Penicillin-binding proteins (PBP) and Lmo0441 (a PBP-like protein) play a role in Beta-lactam sensitivity of Listeria monocytogenes.Identification of the full set of Listeria monocytogenes penicillin-binding proteins and characterization of PBPD2 (Lmo2812).Deciphering the intracellular metabolism of Listeria monocytogenes by mutant screening and modelling.Re-evaluation of the significance of penicillin binding protein 3 in the susceptibility of Listeria monocytogenes to β-lactam antibiotics Listeria monocytogenes PrsA2 is required for virulence factor secretion and bacterial viability within the host cell cytosol.A systematic proteomic analysis of Listeria monocytogenes house-keeping protein secretion systems.Identification of a ferritin-like protein of Listeria monocytogenes as a mediator of β-lactam tolerance and innate resistance to cephalosporins Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence.Discrete and overlapping functions of peptidoglycan synthases in growth, cell division and virulence of Listeria monocytogenes.Listeria monocytogenes surface proteins: from genome predictions to function.Microarray-based characterization of the Listeria monocytogenes cold regulon in log- and stationary-phase cells.Identification of novel Listeria monocytogenes secreted virulence factors following mutational activation of the central virulence regulator, PrfA.(D)-Amino acid chemical reporters reveal peptidoglycan dynamics of an intracellular pathogen.Bacterial peptidoglycan (murein) hydrolases.Imaging bacterial peptidoglycan with near-infrared fluorogenic azide probes The intrinsic cephalosporin resistome of Listeria monocytogenes in the context of stress response, gene regulation, pathogenesis and therapeutics.Do Shoot the Messenger: PASTA Kinases as Virulence Determinants and Antibiotic Targets.The two-component system CesRK controls the transcriptional induction of cell envelope-related genes in Listeria monocytogenes in response to cell wall-acting antibiotics.Cooperation between prokaryotic (Lde) and eukaryotic (MRP) efflux transporters in J774 macrophages infected with Listeria monocytogenes: studies with ciprofloxacin and moxifloxacin.Genomic characterization of Salmonella bacteriophages isolated from India.Purification, crystallization and preliminary X-ray crystallographic analysis of Lmo0540 from Listeria monocytogenes.Role of PBPD1 in stimulation of Listeria monocytogenes biofilm formation by subminimal inhibitory β-lactam concentrations The ABC transporter AnrAB contributes to the innate resistance of Listeria monocytogenes to nisin, bacitracin, and various beta-lactam antibiotics.Assessing the contributions of the LiaS histidine kinase to the innate resistance of Listeria monocytogenes to nisin, cephalosporins, and disinfectants.Penicillin-binding protein encoded by pbp4 is involved in mediating copper stress in Listeria monocytogenes.Stimulation of PgdA-dependent peptidoglycan N-deacetylation by GpsB-PBP A1 in Listeria monocytogenes.Genome scale identification, structural analysis, and classification of periplasmic binding proteins from Mycobacterium tuberculosis.

P2860

Q27678120-98DC6CB3-E74A-450C-97A5-334E9F97CFCB Q27692563-B87B00B9-180B-42BE-9F43-B421CC09B4B8 Q33373968-BA5A8CF5-E5CD-45A9-9A1E-2DBA3780F65A Q33569229-EF726FB0-F5C6-4B32-9236-CC76C8149DE9 Q33571444-592D7068-EBEF-40AE-B0E9-C2FA20CDD76C Q33693304-858FFABF-525E-4217-AA7A-1EFFB3D9C6E5 Q33721327-7A67D77F-E5D6-4439-93CF-3207C44CF745 Q34237626-12E5A6C1-8D2A-473D-B4C4-13390EE4459D Q34290715-145B2602-1933-4E96-8649-84476E24F1CC Q34468365-5A9661AC-C444-477D-B752-047C587542F1 Q34486837-BB7A7E29-588C-4D38-A367-7991A3E898D1 Q35046397-2BD9AF65-BB5B-4BCC-B4F0-E126E53F45FE Q35061107-22284175-0FD9-44D4-A553-163F1BCEF89F Q35856683-869C5FCB-89E3-4666-9F3E-E96BBF152F50 Q36137182-26CD14E3-CB57-4BAB-83B9-E6F8394D15F1 Q36313978-1A494C25-7A35-4385-8FB8-BF934E730B37 Q36696350-D3B0FCEB-198F-41AF-A64B-D83FCA6FF2D1 Q37081704-FE8EAAAF-C85B-4223-918B-0AEC8BF6DE96 Q37711895-987DA9B3-F04C-441B-88B4-C322F23D5E58 Q38618228-DE0EEC23-C119-45DE-88CA-651520A5E578 Q39451994-0A1E685A-544B-4580-9E47-DAFE421BD9BC Q39759777-EC0AD6F4-756F-42E2-92B5-BC2E25C0619A Q39968960-5B82B940-2159-4862-ACF5-13556383553D Q40983100-2AEE9E98-2509-4DD3-B37E-CAA7F73176C1 Q42000363-FCEF2C21-7386-44AE-8D2C-DD603457FF60 Q42201298-25D896B3-DAF8-4305-9664-5A1DBDB53F91 Q42421199-99193356-4311-4E0B-8EB7-4148850B57F0 Q42558328-CE3E39F0-CC37-4B54-A99E-AFAD7BC5810D Q44876167-B28D7EAD-A036-42F9-838F-E193A5DC6957 Q47320441-3666D3D0-603F-45B2-B9C4-71C45BA6EE97 Q48218876-A229B8A0-C604-4D53-9B6F-EAAD0A8B4CD3

P2860

Contribution of penicillin-binding protein homologs to antibiotic resistance, cell morphology, and virulence of Listeria monocytogenes EGDe.

http://www.wikidata.org/entity/Q34973702

description

2006 nî lūn-bûn

@nan

2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

name

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@ast

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@en

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@nl

type

label

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@ast

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@en

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@nl

prefLabel

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@ast

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@en

Contribution of penicillin-bin ...... f Listeria monocytogenes EGDe.

@nl

P1433

Q34973702-EDD40D18-6484-472F-A8C5-4955A4D4111F

P1476

Q34973702-78A550E1-3A44-47F2-85B2-16A3806624AC

P2093

Q34973702-05198DE7-099A-437B-A624-F2BA7E065AD8

Q34973702-0CAC2D0E-105E-4F41-9EB0-589B9D555F3D

Q34973702-EBA7B06F-5AB2-48B5-B3A1-CD69C9069A68

Q34973702-F354BF25-4585-454A-B50A-7144E202666E

P2860

Q34973702-11F5B0F8-EEE0-4F12-B6B7-2EF7396B9A6C

Q34973702-165C0580-17F2-4258-BBAA-E8A0DA4E7F45

Q34973702-1DF3A23D-FDE1-408E-8409-86C468E76631

Q34973702-2029A951-AD7D-483A-AD94-CDC3A2C3C7BC

Q34973702-25EB727C-5A57-431E-9B50-E4833F6A7973

Q34973702-38D2281B-032C-420E-9A0E-3B52A2E31077

Q34973702-41FF188C-77F0-4197-9832-230DCFB7ACAD

Q34973702-4550E4CA-7C86-4181-96B0-88D8E32837D5

Q34973702-4C6734CF-ABAE-4B93-8360-8DDC4AD2BA1F

Q34973702-5DCF9AF9-53AE-4E01-8FC7-A6E4A1B31B0C

P304

Q34973702-EDFB031F-12E7-480B-86FC-F6351408DE53

P31

Q34973702-6C589152-2006-4036-9AA5-3C3B576A4C3A

P356

Q34973702-14DC918E-7341-4660-811F-854B22F5A10B

P407

Q34973702-A1F8B2A3-3C09-43C5-A927-6BD02F422A4C

P433

Q34973702-F17A21E4-EE55-45E3-AE14-F576FC83E8B6

P478

Q34973702-EB38AD69-8199-4D4A-AA5E-C5158C800744

P50

Q34973702-09E9BAE4-C4ED-48F7-AA66-59BC75BA979E

Q34973702-2C721290-18CC-4557-A1F1-A719E4E73176

Q34973702-E33BDEC9-7B58-467F-A46E-99B1788FE08E

Q34973702-EE469341-5F72-4014-A956-2343D9E138A7

P577

Q34973702-710F0BC1-D6BA-4BC6-9F63-CD70F09B694E

P698

Q34973702-578963D6-FEF2-477C-859B-5DA1D0D5970B

P921

Q34973702-6ED21443-8ECC-404C-B9CD-CE1095E0FA31

Q34973702-F4E88AF6-6E2C-4306-93E6-B02B71C1C87E

P932

Q34973702-C8CB0F03-AEAD-4F2F-B643-A77D138C814F

P356

P1433

Antimicrobial Agents and Chemotherapy

P1476

Contribution of penicillin-bin ...... of Listeria monocytogenes EGDe

@en

P2093

Caitriona M Guinane

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

Colin Hill

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

Paul D Cotter

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

R Paul Ross

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

P2860

Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs

Reduced heat resistance of mutant spores after cloning and mutagenesis of the Bacillus subtilis gene encoding penicillin-binding protein 5

Food-related illness and death in the United States

Penicillin-binding protein 1 of Staphylococcus aureus is essential for growth.

Altered PBP 2A and its role in the development of penicillin, cefotaxime, and ceftriaxone resistance in a clinical isolate of Streptococcus pneumoniae.

Mechanisms of resistance to imipenem and ampicillin in Enterococcus faecalis

Treatment of listeriosis.

Identification of new genes involved in the virulence of Listeria monocytogenes by signature-tagged transposon mutagenesis.

Complete sequences of six penicillin-binding protein genes from 40 Streptococcus pneumoniae clinical isolates collected in Japan.

Listeria monocytogenes PerR mutants display a small-colony phenotype, increased sensitivity to hydrogen peroxide, and significantly reduced murine virulence

P304

2824-2828

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

P31

scholarly article

P356

10.1128/AAC.00167-06

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

P407

P433

8

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

P478

50

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

P50

Reynolds Paul Ross

Caitriona M Guinane

P577

2006-08-01T00:00:00Z

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

P698

16870778

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

P921

Listeria monocytogenes

antibiotic resistance

P932

1538649

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