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Heterologous protein secretion by bacillus species from the cradle to the grave.
scientific article published on January 2010
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1 reference
stated in
Europe PubMed Central
PubMed ID
20800757
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20800757%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 February 2020
title
Heterologous protein secretion by bacillus species from the cradle to the grave
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
20800757
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20800757%20AND%20SRC:MED&resulttype=core&format=json
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13 February 2020
author
Colin R. Harwood
series ordinal
2
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Europe PubMed Central
PubMed ID
20800757
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13 February 2020
author name string
Susanne Pohl
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1
1 reference
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Europe PubMed Central
PubMed ID
20800757
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20800757%20AND%20SRC:MED&resulttype=core&format=json
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13 February 2020
publication date
1 January 2010
1 reference
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Europe PubMed Central
PubMed ID
20800757
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retrieved
13 February 2020
published in
Advances in Applied Microbiology
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Europe PubMed Central
PubMed ID
20800757
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13 February 2020
volume
73
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Europe PubMed Central
PubMed ID
20800757
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13 February 2020
page(s)
1-25
1 reference
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Europe PubMed Central
PubMed ID
20800757
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20800757%20AND%20SRC:MED&resulttype=core&format=json
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13 February 2020
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A novel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of Bacillus subtilis
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Poly(glucosyl-N-acetylgalactosamine 1-phosphate), a wall teichoic acid of Bacillus subtilis 168: its biosynthetic pathway and mode of attachment to peptidoglycan
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Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked
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A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress
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Cell-associated degradation affects the yield of secreted engineered and heterologous proteins in the Bacillus subtilis expression system
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The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion
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Secretion of heterologous proteins in Bacillus subtilis can be improved by engineering cell components affecting post-translocational protein folding and degradation
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Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin
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based on heuristic
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Folding pathway mediated by an intramolecular chaperone: dissecting conformational changes coincident with autoprocessing and the role of Ca(2+) in subtilisin maturation
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based on heuristic
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Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity
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7 January 2021
based on heuristic
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7 January 2021
based on heuristic
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Proteomic dissection of potential signal recognition particle dependence in protein secretion by Bacillus subtilis
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7 January 2021
based on heuristic
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Sequential checkpoints govern substrate selection during cotranslational protein targeting
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based on heuristic
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7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S0065-2164(10)73001-X
1 reference
stated in
Europe PubMed Central
PubMed ID
20800757
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20800757%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 February 2020
PubMed ID
20800757
1 reference
stated in
Europe PubMed Central
PubMed ID
20800757
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20800757%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 February 2020
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