Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
about
Bacteriophage lysins as effective antibacterialsCholine Binding Proteins from Streptococcus pneumoniae: A Dual Role as Enzybiotics and Targets for the Design of New AntimicrobialsCrystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniaeRole of Net Charge on Catalytic Domain and Influence of Cell Wall Binding Domain on Bactericidal Activity, Specificity, and Host Range of Phage LysinsC-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydratesCharacterization of Enterococcus faecalis phage IME-EF1 and its endolysinThe insertion site of the temperate phage HB-746 is located near the phage remnant in the pneumococcal host chromosomeCharacterization of Ejl, the cell-wall amidase coded by the pneumococcal bacteriophage Ej-1.Cpl-7, a lysozyme encoded by a pneumococcal bacteriophage with a novel cell wall-binding motifPeptidoglycan hydrolase fusions maintain their parental specificitiesCloning of genomic DNA of Lactococcus lactis that restores phage sensitivity to an unusual bacteriophage sk1-resistant mutantOfloxacin-like antibiotics inhibit pneumococcal cell wall-degrading virulence factors.Using phage lytic enzymes to control pathogenic bacteria.Analysis of the bacteriolytic enzymes of the autolytic lactococcus lactis subsp. cremoris strain AM2 by renaturing polyacrylamide gel electrophoresis: identification of a prophage-encoded enzymeChimeric phage-bacterial enzymes: a clue to the modular evolution of genes.Identification and characterization of a lysis module present in a large proportion of bacteriophages infecting Streptococcus thermophilus.Pneumococcal virulence factors: structure and functionBacteriophage endolysins: a novel anti-infective to control Gram-positive pathogensThe murein hydrolase of the bacteriophage phi3626 dual lysis system is active against all tested Clostridium perfringens strains.Bacteriophage endolysins as novel antimicrobials.Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.Insight into the composition of the intercellular matrix of Streptococcus pneumoniae biofilms.Sequence analysis and molecular characterization of the temperate lactococcal bacteriophage r1t.Thermal stability of Cpl-7 endolysin from the streptococcus pneumoniae bacteriophage Cp-7; cell wall-targeting of its CW_7 motifs.Recombinant bacteriophage lysins as antibacterialsGlucan-binding proteins of the oral streptococci.Changes in the carboxyl-terminal repeat region affect extracellular activity and glucan products of Streptococcus gordonii glucosyltransferaseRecent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage.Purification and characterization of an extracellular muramidase of Clostridium acetobutylicum ATCC 824 that acts on non-N-acetylated peptidoglycanMolecular characterization of lactococcal bacteriophage Tuc2009 and identification and analysis of genes encoding lysin, a putative holin, and two structural proteinsSynergistic streptococcal phage λSA2 and B30 endolysins kill streptococci in cow milk and in a mouse model of mastitis.Novel surface attachment mechanism of the Streptococcus pneumoniae protein PspAStructural properties and evolutionary relationships of PspA, a surface protein of Streptococcus pneumoniae, as revealed by sequence analysis.Mapping the pathways to staphylococcal pathogenesis by comparative secretomicsStaphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site.A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences.Improving the lethal effect of cpl-7, a pneumococcal phage lysozyme with broad bactericidal activity, by inverting the net charge of its cell wall-binding moduleIn vitro destruction of Streptococcus pneumoniae biofilms with bacterial and phage peptidoglycan hydrolases.Tracking the evolution of the bacterial choline-binding domain: molecular characterization of the Clostridium acetobutylicum NCIB 8052 cspA gene.The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain.
P2860
Q24648457-489B950A-87B8-4182-A775-9185C0572426Q26744448-B4BCBE22-D25E-4398-9C58-63B4DB4747D8Q27653500-0CE8CFD9-4056-4B59-B62E-17EA9F706B18Q27671535-28A5FB89-FB02-40C5-8855-9362D2698EFBQ28215660-141F7824-7FAA-457C-9D30-2A7C8D9F399EQ28535077-805EF9B6-E6ED-4C6D-9461-A4A6AEDADDB1Q28776742-E57FE8F7-3A68-40F8-9460-BDD5FB83E86FQ30330465-075BA9B0-0C9F-43E3-989F-670068CB1930Q30392766-7642B25E-F81B-4F86-9EF4-DABDD4D0BD4DQ30446323-922DFD61-EF82-428F-B456-73EE2E3BD6FDQ30649492-03C72E81-9681-49D6-A23F-72CC3BEF794EQ33212929-268BA236-78EF-4ABF-B531-8BCF2FA2AFB9Q33255357-288FC2C7-1D8B-4766-9197-D4A5CD9DC39BQ33718604-164FD45D-FE03-49A3-9172-0565E0787511Q33851733-00F9FF03-7D3F-47C4-B729-B0394FE5B7C5Q33984236-F2D897C7-306B-45D4-AD51-1ABC43826DC5Q34010335-A6AFC0C5-5F9E-4E26-81C5-DC320F3E1B3AQ34114172-19B6BD6C-36CF-48F2-B6D4-3891245088A1Q34166006-D0777F71-41D5-4D12-B533-BB0FC5C26862Q34303439-9D51C4A3-664A-4FAD-B9D2-473705A0821DQ34318134-A07F5348-1812-4037-AC0D-8AF4075D3EC1Q34390055-87DC8CD3-B002-4756-BDD5-451B2AF71152Q34390501-1E8A15CC-4527-4CE1-80A2-9F2F98600B7FQ34441804-6451609A-AABC-42D8-ADFC-B35FFA5C6CB7Q34558237-B1FCD4E5-4B3C-42F5-912C-FCAA0F275B83Q35134880-641A561F-EF02-407E-B8D0-ABAEEDACF0DDQ35531728-B66E87C9-77E2-47FC-B5CC-FBF642E71A4EQ35946160-1ADB5D2F-1421-4060-8EA3-DB4350854668Q35956196-4F1F54D9-E53F-4BDD-95F9-ECDB81E34CD3Q36056003-057DBE29-3E35-415C-8EBA-F74AB29F815CQ36070204-1150B219-691F-4975-AC08-138846C30D62Q36107664-81702BA0-BBC5-4A2B-A766-008E422BD782Q36109895-7EE6D21E-F192-48CA-BEF8-A3A31BF2C3E8Q36588782-FE6AE3DB-545F-4EF2-A069-24A001A57975Q37062915-1E36F5EF-E5C9-4E80-BFAE-AC6B98EEB2CDQ37096019-98B603F3-8655-453D-BAA9-6A23925048C7Q37263537-A4E77956-996D-4E6A-862D-09AFDBD413A4Q38282910-EB89024A-037A-469E-B917-AA80DB6459A1Q38299048-672FF46B-7969-4B74-9551-147E5D6FB9E0Q38361188-CDD5DD85-F8FC-4D22-B413-A500CA5CAAE3
P2860
Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
description
1990 nî lūn-bûn
@nan
1990 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հունվարին 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
Modular organization of the ly ...... umoniae and its bacteriophages
@ast
Modular organization of the ly ...... umoniae and its bacteriophages
@en
Modular organization of the ly ...... umoniae and its bacteriophages
@nl
type
label
Modular organization of the ly ...... umoniae and its bacteriophages
@ast
Modular organization of the ly ...... umoniae and its bacteriophages
@en
Modular organization of the ly ...... umoniae and its bacteriophages
@nl
prefLabel
Modular organization of the ly ...... umoniae and its bacteriophages
@ast
Modular organization of the ly ...... umoniae and its bacteriophages
@en
Modular organization of the ly ...... umoniae and its bacteriophages
@nl
P2093
P3181
P1433
P1476
Modular organization of the ly ...... umoniae and its bacteriophages
@en
P2093
J L García
J M Sánchez-Puelles
P3181
P356
10.1016/0378-1119(90)90116-9
P407
P50
P577
1990-01-31T00:00:00Z