Analysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide.
about
Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coliExpression and efficient secretion of a functional chitinase from Chromobacterium violaceum in Escherichia coliThe complete general secretory pathway in gram-negative bacteriaExport of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutations.Protein targeting to the bacterial cytoplasmic membrane.Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB proteinEffect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence.Comprehensive characterization of methicillin-resistant Staphylococcus aureus subsp. aureus COL secretome by two-dimensional liquid chromatography and mass spectrometry.Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulation.The code for directing proteins for translocation across ER membrane: SRP cotranslationally recognizes specific features of a signal sequence.PrlA and PrlG suppressors reduce the requirement for signal sequence recognitionEffect of alteration of charged residues at the N termini of signal peptides on protein export in Bacillus subtilis.Thirty-three amino acids of the mature moiety of an unprocessed maltose-binding protein are sufficient for export in Escherichia coli.Effect of signal sequence alterations on export of levansucrase in Bacillus subtilis.Alterations in the hydrophilic segment of the maltose-binding protein (MBP) signal peptide that affect either export or translation of MBP.Interactions that drive Sec-dependent bacterial protein transport.Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process.Protein secretion in Bacillus species.Coupling between codon usage, translation and protein export in Escherichia coli.Evaluation of a novel subtilisin inhibitor gene and mutant derivatives for the expression and secretion of mouse tumor necrosis factor alpha by Streptomyces lividans.Escherichia coli signal peptides direct inefficient secretion of an outer membrane protein (OmpA) and periplasmic proteins (maltose-binding protein, ribose-binding protein, and alkaline phosphatase) in Bacillus subtilis.Effect of OmpA signal peptide mutations on OmpA secretion, synthesis, and assembly.A negatively charged N terminus in the alpha polypeptide inhibits formation of light-harvesting complex I in Rhodobacter capsulatus.Targeting of cytochrome b2 into the mitochondrial intermembrane space: specific recognition of the sorting signal.Roles of the signal peptide and mature domains in the secretion and maturation of the neutral metalloprotease from Streptomyces cacaoi.Selection for efficient translation initiation biases codon usage at second amino acid position in secretory proteins.Domain organization of long autotransporter signal sequences.
P2860
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P2860
Analysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Analysis of mutational alterat ...... inding protein signal peptide.
@ast
Analysis of mutational alterat ...... inding protein signal peptide.
@en
type
label
Analysis of mutational alterat ...... inding protein signal peptide.
@ast
Analysis of mutational alterat ...... inding protein signal peptide.
@en
prefLabel
Analysis of mutational alterat ...... inding protein signal peptide.
@ast
Analysis of mutational alterat ...... inding protein signal peptide.
@en
P2093
P2860
P1476
Analysis of mutational alterat ...... inding protein signal peptide.
@en
P2093
J W Puziss
P J Bassford
P2860
P304
P356
10.1128/JB.171.5.2303-2311.1989
P407
P577
1989-05-01T00:00:00Z