Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor.
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Crystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reactionSynthesis and Characterization of the Arylomycin Lipoglycopeptide Antibiotics and the Crystallographic Analysis of Their Complex with Signal PeptidaseOrigin of phagotrophic eukaryotes as social cheaters in microbial biofilmsSolution NMR of signal peptidase, a membrane protein.Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallizationImaging mass spectrometry and genome mining via short sequence tagging identified the anti-infective agent arylomycin in Streptomyces roseosporusAltered -3 substrate specificity of Escherichia coli signal peptidase 1 mutants as revealed by screening a combinatorial peptide library.Modeling Escherichia coli signal peptidase complex with bound substrate: determinants in the mature peptide influencing signal peptide cleavageBroad-spectrum antibiotic activity of the arylomycin natural products is masked by natural target mutationsIn vitro activities of arylomycin natural-product antibiotics against Staphylococcus epidermidis and other coagulase-negative staphylococciSecretion of the chlamydial virulence factor CPAF requires the Sec-dependent pathwaySynthesis and biological characterization of arylomycin B antibioticsInitial efforts toward the optimization of arylomycins for antibiotic activity.Origins of Yersinia pestis sensitivity to the arylomycin antibiotics and the inhibition of type I signal peptidaseMembrane proteases in the bacterial protein secretion and quality control pathway.Broadening the spectrum of β-lactam antibiotics through inhibition of signal peptidase type I.The inhibition of type I bacterial signal peptidase: Biological consequences and therapeutic potential.Mechanism of action of the arylomycin antibiotics and effects of signal peptidase I inhibitionExpression, purification and crystallization of a birnavirus-encoded protease, VP4, from blotched snakehead virus (BSNV).Purification, crystallization and preliminary X-ray analysis of truncated and mutant forms of VP4 protease from infectious pancreatic necrosis virusInteractions that drive Sec-dependent bacterial protein transport.MS/MS-based networking and peptidogenomics guided genome mining revealed the stenothricin gene cluster in Streptomyces roseosporus.Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.Efforts toward broadening the spectrum of arylomycin antibiotic activity.Screening strategies for discovery of antibacterial natural products.Signal peptidase I: cleaving the way to mature proteins.Bacterial type I signal peptidases as antibiotic targets.Strained cyclophane natural products: macrocyclization at its limits.Proteases in Mycobacterium tuberculosis pathogenesis: potential as drug targets.Polishing the tarnished silver bullet: the quest for new antibiotics.Expression, purification and crystallization of a membrane-associated, catalytically active type I signal peptidase from Staphylococcus aureus.Inhibition of the sole type I signal peptidase of Mycobacterium tuberculosis is bactericidal under replicating and nonreplicating conditions.Export of a hyperexpressed mammalian globular cytochrome b5 precursor in Escherichia coli is dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bondThe identification of residues that control signal peptidase cleavage fidelity and substrate specificity.Plastidic type I signal peptidase 1 is a redox-dependent thylakoidal processing peptidase.The Sec System: Protein Export in Escherichia coli.Molecular insights into the m-AAA protease-mediated dislocation of transmembrane helices in the mitochondrial inner membrane.Biosynthesis of new lipopentapeptides by an engineered strain of Streptomyces sp.Scalable Access to Arylomycins via C-H Functionalization Logic.Biphenomycin B and derivatives: total synthesis and translation inhibition.
P2860
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P2860
Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor.
description
2004 nî lūn-bûn
@nan
2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
@zh-my
2004年学术文章
@zh-sg
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name
Crystallographic and biophysic ...... a lipopeptide-based inhibitor.
@en
Crystallographic and biophysic ...... a lipopeptide-based inhibitor.
@nl
type
label
Crystallographic and biophysic ...... a lipopeptide-based inhibitor.
@en
Crystallographic and biophysic ...... a lipopeptide-based inhibitor.
@nl
prefLabel
Crystallographic and biophysic ...... a lipopeptide-based inhibitor.
@en
Crystallographic and biophysic ...... a lipopeptide-based inhibitor.
@nl
P2093
P2860
P356
P1476
Crystallographic and biophysic ...... a lipopeptide-based inhibitor.
@en
P2093
Jonathon J Goodall
Malcolm G P Page
Malgosia Kania
Mark Paetzel
Ross E Dalbey
P2860
P304
30781-30790
P356
10.1074/JBC.M401686200
P407
P577
2004-05-10T00:00:00Z