The hydrophobic region of signal peptides is involved in the interaction with membrane-bound SecA. (Q54565669)

1 June 2018

title

The hydrophobic region of signal peptides is involved in the interaction with membrane-bound SecA. (English)

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1 June 2018

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H Mori

1

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1 June 2018

M Araki

2

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1 June 2018

C Hikita

3

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1 June 2018

M Tagaya

4

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1 June 2018

S Mizushima

5

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1 June 2018

publication date

1 May 1997

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1 June 2018

Biochimica et Biophysica Acta

published in

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1 June 2018

volume

1326

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1 June 2018

issue

1

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1 June 2018

page(s)

23-36

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1 June 2018

Signal sequences. The limits of variation

cites work

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https://api.crossref.org/works/10.1016%2FS0005-2736%2897%2900004-7

Role of positive charge on the amino-terminal region of the signal peptide in protein secretion across the membrane

7 January 2021

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The role of the positively charged N-terminus of the signal sequence of E. coli outer membrane protein PhoE in export

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Sequence analysis of mutations that prevent export of lambda receptor, an Escherichia coli outer membrane protein.

7 January 2021

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Importance of secondary structure in the signal sequence for protein secretion

7 January 2021

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Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0005-2736%2897%2900004-7

Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide

7 January 2021

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Engineering of the hydrophobic segment of the signal sequence for efficient secretion of human lysozyme by Saccharomyces cerevisiae

7 January 2021

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E. coli mutant pleiotropically defective in the export of secreted proteins

7 January 2021

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Roles of the Pribnow box in positive regulation of the ompC and ompF genes in Escherichia coli

7 January 2021

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Efficientin vitrosynthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter

7 January 2021

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SecA protein is directly involved in protein secretion in Escherichia coli

7 January 2021

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DNA sequencing with chain-terminating inhibitors

7 January 2021

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The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins

7 January 2021

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Penetration of the signal sequence of Escherichia coli PhoE protein into phospholipid model membranes leads to lipid-specific changes in signal peptide structure and alterations of lipid organization

7 January 2021

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Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments

7 January 2021

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SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study

7 January 2021

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In vivo studies of the role of SecA during protein export in Escherichia coli

7 January 2021

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Anionic phospholipids and protein translocation

7 January 2021

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10.1016/S0005-2736(97)00004-7

7 January 2021

Identifiers

DOI

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1 June 2018

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1 June 2018