epr, which encodes glycylglycine endopeptidase resistance, is homologous to femAB and affects serine content of peptidoglycan cross bridges in Staphylococcus capitis and Staphylococcus aureus
about
Bacterial peptidoglycan degrading enzymes and their impact on host muropeptide detectionCell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges.Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope.Lysostaphin: A Staphylococcal Bacteriolysin with Potential Clinical Applications.Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotypeStaphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without'Site-specific serine incorporation by Lif and Epr into positions 3 and 5 of the Staphylococcal peptidoglycan interpeptide bridge.Self-protection against cell wall hydrolysis in Streptococcus milleri NMSCC 061 and analysis of the millericin B operonPhysiological significance of the peptidoglycan hydrolase, LytM, in Staphylococcus aureusBacteriophage endolysins as novel antimicrobials.In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus.FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and beta-lactam resistance in gram-positive cocci.Characterization of a novel family of fibronectin-binding proteins with M23 peptidase domains from Treponema denticola.The essential Staphylococcus aureus gene fmhB is involved in the first step of peptidoglycan pentaglycine interpeptide formationLysostaphin-resistant variants of Staphylococcus aureus demonstrate reduced fitness in vitro and in vivo.Chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands.Bacterial transfer RNAs.Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria.Direction of aminoacylated transfer RNAs into antibiotic synthesis and peptidoglycan-mediated antibiotic resistanceZif, the zoocin A immunity factor, is a FemABX-like immunity protein with a novel mode of action.Combinations of lysostaphin with beta-lactams are synergistic against oxacillin-resistant Staphylococcus epidermidis.Efficient Killing of Planktonic and Biofilm-Embedded Coagulase-Negative Staphylococci by Bactericidal Protein P128.Identification and molecular characterization of an N-acetylmuramyl-L-alanine amidase Sle1 involved in cell separation of Staphylococcus aureus.Potential for Bacteriophage Endolysins to Supplement or Replace Antibiotics in Food Production and Clinical Care.
P2860
Q24653921-CFCA2FE1-3B6F-4945-BAAF-6E098F54ECDFQ30160087-57FFE357-56E4-4A2D-A699-E9C03F2E04C9Q33538951-4962DFC9-F01F-46BB-B31D-D0A7DCBAFC60Q33664443-39A8A6CF-FA4A-471C-AE24-98C92CB670EEQ33714506-8522AAD2-2C54-48FA-9F99-D341B3BF27BCQ33775374-73E6BC43-7F39-425B-927F-152BA36ED11AQ33790539-682210E6-269D-48DA-AE79-2C03AAA18A73Q33990176-7A8FA323-90DC-4646-9570-F93019545689Q34152544-86F3887E-2E6F-4CAE-BF7D-364E5A6160BCQ34303439-55EC7E04-F6BE-4DA2-9176-510436DB1F72Q34330366-30CB77B4-0721-4147-BBF1-761890925038Q34735338-F51DC1C7-9C4F-40DE-8835-6456416F7543Q35012557-87FA3827-282A-4245-AC71-DB26818889E8Q35604130-BBC47F36-D850-4016-87BF-E17B24532C4CQ35635997-6CB9335F-C0C8-4573-A172-8A06C70EF1F8Q35827070-72AE890A-5481-4402-82FA-39B99AC26AC6Q35974736-816E901B-5CFD-4916-B307-D4096F8F81F0Q37081713-F5A18D66-E814-4A64-940C-4C55E8D531C7Q37207046-3F0AC8D3-20A8-4083-87BA-CBE57A5E933DQ37365310-FD77B18E-43AB-4102-BF31-939AA6E72780Q39651918-0459DEF4-FE02-4CE5-A457-D758DBB10034Q40192368-627C013C-3369-420C-9C8B-98AED7A938B8Q46785719-A4F8E8D0-EA0F-472D-87F0-30D20D1EA182Q52679093-EB0902E8-427F-4D42-B9BD-B6CDEDA0AB76
P2860
epr, which encodes glycylglycine endopeptidase resistance, is homologous to femAB and affects serine content of peptidoglycan cross bridges in Staphylococcus capitis and Staphylococcus aureus
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
epr, which encodes glycylglyci ...... itis and Staphylococcus aureus
@en
epr, which encodes glycylglyci ...... tis and Staphylococcus aureus.
@nl
type
label
epr, which encodes glycylglyci ...... itis and Staphylococcus aureus
@en
epr, which encodes glycylglyci ...... tis and Staphylococcus aureus.
@nl
prefLabel
epr, which encodes glycylglyci ...... itis and Staphylococcus aureus
@en
epr, which encodes glycylglyci ...... tis and Staphylococcus aureus.
@nl
P2093
P2860
P1476
epr, which encodes glycylglyci ...... itis and Staphylococcus aureus
@en
P2093
P2860
P304
P356
10.1128/JB.179.13.4311-4318.1997
P577
1997-07-01T00:00:00Z