(Q54677524)

English

The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptides

scientific article published on June 15, 1992

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scholarly article

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Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1318317

The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptides (English)

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1318317

12 September 2022

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based on heuristic

inferred from title

Escherichia coli proteins

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Europe PubMed Central

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12 September 2022

transmembrane transport protein

1 reference

Europe PubMed Central

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12 September 2022

recombinant protein

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1318317

12 September 2022

1 reference

10.1016/S0021-9258(19)49850-5

https://api.crossref.org/works/10.1016/S0021-9258(19)49850-5

5 December 2023

1 reference

10.1016/S0021-9258(19)49850-5

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5 December 2023

author name string

C. Hikita

1

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12 September 2022

S. Mizushima

2

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12 September 2022

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publication date

1 June 1992

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2 June 2018

http://europepmc.org/abstract/MED/1318317

15 June 1992

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National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1318317

12 September 2022

full work available at URL

http://intl.jbc.org/cgi/content/abstract/267/17/12375

online access status

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1318317

12 September 2022

https://doi.org/10.1016/s0021-9258(19)49850-5

online access status

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Europe PubMed Central

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5 December 2023

https://api.elsevier.com/content/article/PII:S0021925819498505?httpAccept=text/xml

1 reference

10.1016/S0021-9258(19)49850-5

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5 December 2023

https://api.elsevier.com/content/article/PII:S0021925819498505?httpAccept=text/plain

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10.1016/S0021-9258(19)49850-5

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5 December 2023

Journal of Biological Chemistry

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Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1318317

267

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Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1318317

12375-12379

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Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1318317

17

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1318317

Signal sequences. The limits of variation

2

1 reference

10.1016/S0021-9258(19)49850-5

https://api.crossref.org/works/10.1016/S0021-9258(19)49850-5

5 December 2023

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

3

1 reference

10.1016/S0021-9258(19)49850-5

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5 December 2023

Role of amino-terminal positive charge on signal peptide in staphylokinase export across the cytoplasmic membrane of Escherichia coli.

5

1 reference

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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

6

1 reference

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In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli.

7

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SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

8

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SecA protein is directly involved in protein secretion in Escherichia coli

9

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SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

10

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

11

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

12

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Importance of secondary structure in the signal sequence for protein secretion

13

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Biophysical studies of signal peptides: implications for signal sequence functions and the involvement of lipid in protein export

15

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5 December 2023

Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide

16

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

19

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Analysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide

21

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Efficient in vitro translocation into Escherichia coli membrane vesicles of a protein carrying an uncleavable signal peptide. Characterization of the translocation process.

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

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

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

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Proton motive force-dependent and -independent protein translocation revealed by an efficient in vitro assay system of Escherichia coli.

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SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.

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DNA sequencing with chain-terminating inhibitors

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1 Measurement of molecular weights by electrophoresis on SDS-acrylamide gel

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Role for membrane potential in the secretion of protein into the periplasm of Escherichia coli

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Involvement of membrane lipids in protein export in Escherichia coli.

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Temperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process

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Molecular cloning and nucleotide sequence of cDNA of microsomal carboxyesterase E1 of rat liver

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Identifiers

1 reference

Europe PubMed Central

2 June 2018

http://europepmc.org/abstract/MED/1318317

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