Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
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Bacteriophage lysins as effective antibacterialsCholine Binding Proteins from Streptococcus pneumoniae: A Dual Role as Enzybiotics and Targets for the Design of New AntimicrobialsA chimeolysin with extended-spectrum streptococcal host range found by an induced lysis-based rapid screening methodStructural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entryRole of Net Charge on Catalytic Domain and Influence of Cell Wall Binding Domain on Bactericidal Activity, Specificity, and Host Range of Phage LysinsMultiple enzymatic activities of the murein hydrolase from staphylococcal phage phi11. Identification of a D-alanyl-glycine endopeptidase activityCharacterization of Enterococcus faecalis phage IME-EF1 and its endolysinGMEnzy: a genetically modified enzybiotic databaseUsing phage lytic enzymes to control pathogenic bacteria.Staphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without'Lytic activity of the virion-associated peptidoglycan hydrolase HydH5 of Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88.Molecular peculiarities of the lytA gene isolated from clinical pneumococcal strains that are bile insolublePneumococcal virulence factors: structure and functionBacteriophage endolysins: a novel anti-infective to control Gram-positive pathogensBacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity.Bacteriophage endolysins as novel antimicrobials.Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.Engineered bacteriophage lysins as novel anti-infectivesThermal stability of Cpl-7 endolysin from the streptococcus pneumoniae bacteriophage Cp-7; cell wall-targeting of its CW_7 motifs.Recombinant bacteriophage lysins as antibacterialsGenomic sequence of C1, the first streptococcal phageChimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands.Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site.Bacteriophage and their lysins for elimination of infectious bacteria.Domain exchange: characterization of a chimeric lipase of hepatic lipase and lipoprotein lipase.Tracking the evolution of the bacterial choline-binding domain: molecular characterization of the Clostridium acetobutylicum NCIB 8052 cspA gene.Bacteriophage therapy against Enterobacteriaceae.The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain.PEGylating a bacteriophage endolysin inhibits its bactericidal activity.The autolysin-encoding gene (lytA) of Streptococcus pneumoniae displays restricted allelic variation despite localized recombination events with genes of pneumococcal bacteriophage encoding cell wall lytic enzymes.Molecular aspects and comparative genomics of bacteriophage endolysins.Role of the major pneumococcal autolysin in the atypical response of a clinical isolate of Streptococcus pneumoniae.EJ-1, a temperate bacteriophage of Streptococcus pneumoniae with a Myoviridae morphotype.LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions.A novel chimeric phage lysin with high in vitro and in vivo bactericidal activity against Streptococcus pneumoniae.A two-component, multimeric endolysin encoded by a single gene.Exploiting what phage have evolved to control gram-positive pathogensAccumulation of partly folded states in the equilibrium unfolding of the pneumococcal choline-binding module C-LytA.Domain shuffling and module engineering of Listeria phage endolysins for enhanced lytic activity and binding affinity.Chimeric Ply187 endolysin kills Staphylococcus aureus more effectively than the parental enzyme.
P2860
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P2860
Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
description
1990 nî lūn-bûn
@nan
1990 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
@ast
Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
@en
type
label
Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
@ast
Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
@en
prefLabel
Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
@ast
Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
@en
P2093
P2860
P356
P1476
Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.
@en
P2093
P2860
P304
P356
10.1073/PNAS.87.20.8125
P407
P577
1990-10-01T00:00:00Z