Signal peptides: exquisitely designed transport promoters.
about
Leucine-rich repeat, immunoglobulin-like and transmembrane domain 3 (LRIT3) is a modulator of FGFR1Overlapping functions of components of a bacterial Sec-independent protein export pathwayA new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocaseIsolation, sequence, and expression of the gene encoding halocin H4, a bacteriocin from the halophilic archaeon Haloferax mediterranei R4Class IIa bacteriocins: diversity and new developmentsCrystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitorCloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatisThe conformation of a signal peptide bound by Escherichia coli preprotein translocase SecAATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophagesThe major phase-variable outer membrane protein of Escherichia coli structurally resembles the immunoglobulin A1 protease class of exported protein and is regulated by a novel mechanism involving Dam and oxyRPet, an autotransporter enterotoxin from enteroaggregative Escherichia coli.Characterization of an arylesterase from Lactobacillus helveticus CNRZ32.Enterocins L50A and L50B, two novel bacteriocins from Enterococcus faecium L50, are related to staphylococcal hemolysins.Domain organization of long signal peptides of single-pass integral membrane proteins reveals multiple functional capacity.Protein targeting to the bacterial cytoplasmic membrane.Glucansucrases: mechanism of action and structure-function relationships.The Tat protein export pathway.Comprehensive mutational analysis of the Moloney murine leukemia virus envelope protein.Archaeal protein translocation crossing membranes in the third domain of life.Purification and genetic characterization of enterocin I from Enterococcus faecium 6T1a, a novel antilisterial plasmid-encoded bacteriocin which does not belong to the pediocin family of bacteriocins.Green fluorescent protein functions as a reporter for protein localization in Escherichia coli.Conservation of the 17-kilodalton antigen gene within the genus Bartonella.Characterization of pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli.Protein transport via amino-terminal targeting sequences: common themes in diverse systems.Protein targeting by the twin-arginine translocation pathway.Molecular characterization of cold adaptation of membrane proteins in the Vibrionaceae core-genome.Effect of signal peptide on stability and folding of Escherichia coli thioredoxin.Construction and application of the vectors to identify genes encoding exported proteins of Escherichia coli.Combined effects of the signal sequence and the major chaperone proteins on the export of human cytokines in Escherichia coliNondisruptive detection of activity of catabolic promoters of Pseudomonas putida with an antigenic surface reporter system.Expression of the antimicrobial peptide carnobacteriocin B2 by a signal peptide-dependent general secretory pathway.Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum.Evidence for a methyl-accepting chemotaxis protein gene (mcp1) that encodes a putative sensory transducer in virulent Treponema pallidum.Aggregative adherence fimbria II, a second fimbrial antigen mediating aggregative adherence in enteroaggregative Escherichia coli.Cloning, sequencing, and expression of the mig gene of Mycobacterium avium, which codes for a secreted macrophage-induced protein.A signal peptide secretion-dependent bacteriocin from Carnobacterium divergensGenetic analysis of the modABCD (molybdate transport) operon of Escherichia coli.Escherichia coli SecB stimulates export without maintaining export competence of ribose-binding protein signal sequence mutants.Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway.The Tla protein of Porphyromonas gingivalis W50: a homolog of the RI protease precursor (PrpRI) is an outer membrane receptor required for growth on low levels of hemin.
P2860
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P2860
Signal peptides: exquisitely designed transport promoters.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Signal peptides: exquisitely designed transport promoters.
@en
type
label
Signal peptides: exquisitely designed transport promoters.
@en
prefLabel
Signal peptides: exquisitely designed transport promoters.
@en
P2860
P1476
Signal peptides: exquisitely designed transport promoters.
@en
P2093
P2860
P304
P356
10.1111/J.1365-2958.1994.TB00469.X
P407
P577
1994-09-01T00:00:00Z