Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
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The molecular mechanism of bacterial lipoprotein modification--how, when and why?Dynamic localization of Tat protein transport machinery components in Streptomyces coelicolor.Tat-dependent translocation of an F420-binding protein of Mycobacterium tuberculosis.Mislocalization of Rieske protein PetA predominantly accounts for the aerobic growth defect of Tat mutants in Shewanella oneidensis.Lipoproteins of slow-growing Mycobacteria carry three fatty acids and are N-acylated by apolipoprotein N-acyltransferase BCG_2070cOverexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase.Adherence and invasive properties of Corynebacterium diphtheriae strains correlates with the predicted membrane-associated and secreted proteomeMembrane proteases in the bacterial protein secretion and quality control pathway.Cosmid based mutagenesis causes genetic instability in Streptomyces coelicolor, as shown by targeting of the lipoprotein signal peptidase gene.Functional analyses of mycobacterial lipoprotein diacylglyceryl transferase and comparative secretome analysis of a mycobacterial lgt mutant.Streptomyces as symbionts: an emerging and widespread theme?A phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteria.The twin-arginine translocation (Tat) protein export pathway.The iron-regulated staphylococcal lipoproteins.Lipoproteins in bacteria: structures and biosynthetic pathways.Twin-Arginine Protein Translocation.Mycobacterium tuberculosis lipoproteins in virulence and immunity - fighting with a double-edged sword.Organophosphate Hydrolase Is a Lipoprotein and Interacts with Pi-specific Transport System to Facilitate Growth of Brevundimonas diminuta Using OP Insecticide as Source of Phosphate.Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase.Residues located on membrane-embedded flexible loops are essential for the second step of the apolipoprotein N-acyltransferase reaction.Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane.Identification of the Lyso-Form N-Acyl Intramolecular Transferase in Low-GC Firmicutes.The Cellular Mechanisms that Ensure an Efficient Secretion in Streptomyces.Equations of bark thickness and volume profiles at different heights with easy-measurement variables
P2860
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P2860
Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
description
2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
@zh-hans
2011年学术文章
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2011年学术文章
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2011年學術文章
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name
Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
@en
Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
@nl
type
label
Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
@en
Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
@nl
prefLabel
Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
@en
Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
@nl
P2093
P2860
P50
P1476
Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.
@en
P2093
Andreas Tschumi
David A Widdick
Juliane K Brülle
Matthew G Hicks
P2860
P304
P356
10.1111/J.1365-2958.2011.07656.X
P407
P577
2011-05-02T00:00:00Z