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Cold shock stress-induced proteins in Bacillus subtilis
scientific journal article
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scholarly article
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stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
title
Cold shock stress-induced proteins in Bacillus subtilis
(English)
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stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
main subject
Bacillus subtilis
object named as
Bacillus subtilis
1 reference
based on heuristic
inferred from title
author
Peter L Graumann
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stated in
ORCID Public Data File 2021
author name string
P. Graumann
series ordinal
1
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stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
K. Schröder
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
R. Schmid
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
M. A. Marahiel
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
language of work or name
English
0 references
publication date
1 August 1996
1 reference
stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
published in
Journal of Bacteriology
1 reference
stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
volume
178
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stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
page(s)
4611–4619
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stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
issue
15
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stated in
PubMed
PubMed ID
8755892
retrieved
24 January 2017
cites work
Structure in solution of the major cold-shock protein from Bacillus subtilis
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Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
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Crystal structure of CspA, the major cold shock protein of Escherichia coli
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Analysis of the induction of general stress proteins of Bacillus subtilis
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Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis
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Survival of hunger and stress: the role of rpoS in early stationary phase gene regulation in E. coli
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The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- and CCAAT sequences in single stranded oligonucleotides
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PubMed Central
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Responses to nutrient starvation in Pseudomonas putida KT2442: two-dimensional electrophoretic analysis of starvation- and stress-induced proteins
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Cloning and characterization of ppiB, a Bacillus subtilis gene which encodes a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase
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The cold-shock response--a hot topic
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A gene at 333 degrees on the Bacillus subtilis chromosome encodes the newly identified sigma B-dependent general stress protein GspA.
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Extremely rapid protein folding in the absence of intermediates
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Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
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Regulation of the heat-shock response in bacteria
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29 September 2017
Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif
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Induction of proteins in response to low temperature in Escherichia coli
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29 September 2017
Sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from Bacillus subtilis
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29 September 2017
Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome
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29 September 2017
Ribosomes as sensors of heat and cold shock in Escherichia coli
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29 September 2017
Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS.
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29 September 2017
Temperature-induced protein synthesis in Bacillus stearothermophilus NUB36
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Nucleotide sequences of Bacillus subtilis flagellar biosynthetic genes fliP and fliQ and identification of a novel flagellar gene, fliZ
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29 September 2017
Function of a relaxed-like state following temperature downshifts in Escherichia coli
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29 September 2017
Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis
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Analysis of genes involved in biosynthesis of the lantibiotic subtilin
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Streptomyces contain a 7.0 kDa cold shock like protein
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Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures
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DNA gyrase, CS7.4, and the cold shock response in Escherichia coli
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Effects of low temperature on in vivo and in vitro protein synthesis in Escherichia coli and Pseudomonas fluorescens
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Occurrence and expression of cspA, a cold shock gene, in Antarctic psychrotrophic bacteria.
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Family of the major cold-shock protein, CspA (CS7.4), of Escherichia coli, whose members show a high sequence similarity with the eukaryotic Y-box binding proteins
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Interaction of the main cold shock protein CS7.4 (CspA) of Escherichia coli with the promoter region of hns.
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2 June 2018
Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis
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2 June 2018
Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin
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2 June 2018
Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjacent genes homologous to uvrC and trx of Escherichia coli
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2 June 2018
Heat and cold shock protein synthesis in arctic and temperate strains of rhizobia
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2 June 2018
spoVG sequence of Bacillus megaterium and Bacillus subtilis
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2 June 2018
Characterization and sequence of the Escherichia coli stress-induced psp operon.
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2 June 2018
Mapping of the Bacillus subtilis cspB gene and cloning of its homologs in thermophilic, mesophilic and psychrotrophic bacilli
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27 November 2018
The primary structure of Bacillus subtilis acidic ribonsomal protein B-19. Isolation and characterization of peptides and the complete amino acid sequence
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https://pubmed.ncbi.nlm.nih.gov/8755892
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12 December 2020
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Purification and characterization of 30S ribosomal proteins from Bacillus subtilis: correlation to Escherichia coli 30S proteins
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/8755892
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12 December 2020
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1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8755892
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12 December 2020
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Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8755892
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
DNA supercoiling and thermal regulation of unsaturated fatty acid synthesis in Bacillus subtilis
1 reference
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/8755892
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12 December 2020
based on heuristic
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The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8755892
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Induction of cold shock proteins in Bacillus subtilis
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8755892
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
An agarose-based gel-concentration system for microsequence and mass spectrometric characterization of proteins previously purified in polyacrylamide gels starting at low picomole levels
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8755892
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Analysis of heat and cold shock proteins in Listeria by two-dimensional electrophoresis
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8755892
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/JB.178.15.4611-4619.1996
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4865560
OpenCitations bibliographic resource ID
4865560
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4865560
PMCID
178231
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4865560
PubMed ID
8755892
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4865560
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