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GenomicsExpression data from mice kidneys with urinary tract infection treated with NlpD or LytM
Expression data from mice kidneys with urinary tract infection treated with NlpD or LytM
PRJNA1463761 | ENA
TranscriptomicsExpression data from mice kidneys with urinary tract infection treated with NlpD or LytM
Finding new ways of treating bacterial infections is essential. The NlpD protein, which inhibits RNA Polymerase II (Pol II), has shown therapeutic efficacy against urinary tract infection. This study investigated the mechanism of Pol II inhibition and protection by NlpD and its LytM peptide. Recombi...
ORGANISM(S): Mus musculus 
2026-05-15 | GSE330388 | GEO
ProteomicsS. aureus peptidoglycan hydrolysis by mutanolysin and LytM catalytic domain
(Manuscript abstract) "Peptidoglycan, a gigadalton polymer, functions as the scaffold for bacterial cell walls and provides cell integrity. Peptidoglycan is remodelled by a large and diverse group of peptidoglycan hydrolases, which control bacterial cell growth and division. Over the years, many stu...
ORGANISM(S): Staphylococcus aureus 
2023-11-06 | PXD045859 | Pride
Peptidoglycan Lytm Staphylococcus aureus Mutanolysin 
UnknownAnti-staphylococcal activities of lysostaphin and LytM catalytic domain.
Not available
S-EPMC3413552 | biostudies-literature
UnknownVarious checkpoints prevent the synthesis of Staphylococcus aureus peptidoglycan hydrolase LytM in the stationary growth phase.
Not available
S-EPMC4841606 | biostudies-literature
UnknownStructure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site.
Not available
S-EPMC3923381 | biostudies-literature
UnknownFusion with a cell wall binding domain renders autolysin LytM a potent anti-Staphylococcus aureus agent.
Not available
S-EPMC4445658 | biostudies-literature
UnknownDiversification of LytM Protein Functions in Polar Elongation and Cell Division of Agrobacterium tumefaciens.
Not available
S-EPMC8416486 | biostudies-literature
UnknownReassessing the substrate specificities of the major Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM.
Not available
S-EPMC11534333 | biostudies-literature
UnknownLytM proteins play a crucial role in cell separation, outer membrane composition, and pathogenesis in nontypeable Haemophilus influenzae.
Not available
S-EPMC4358004 | biostudies-literature
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