(Q38329012)

2 September 2017

title

The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo (English)

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2 September 2017

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5

Schmid FX

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2 September 2017

Schindler T

1

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2 September 2017

Graumann PL

2

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2 September 2017

Perl D

3

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2 September 2017

Ma S

4

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2 September 2017

Marahiel MA

6

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2 September 2017

language of work or name

English

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publication date

1 February 1999

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

274

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2 September 2017

issue

6

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2 September 2017

page(s)

3407-3413

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A superfamily of proteins that contain the cold-shock domain

2 September 2017

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Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins

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Sequence-specific RNA recognition by the Xenopus Y-box proteins. An essential role for the cold shock domain.

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Translational repression dependent on the interaction of the Xenopus Y-box protein FRGY2 with mRNA. Role of the cold shock domain, tail domain, and selective RNA sequence recognition.

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CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone.

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A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures

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Identification and purification of a family of dimeric major cold shock protein homologs from the psychrotrophic Bacillus cereus WSBC 10201.

21 January 2018

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Structure in solution of the major cold-shock protein from Bacillus subtilis

21 January 2018

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Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein

21 January 2018

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Crystal structure of CspA, the major cold shock protein of Escherichia coli

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Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.

21 January 2018

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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

21 January 2018

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Induction of proteins in response to low temperature in Escherichia coli

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DNA gyrase, CS7.4, and the cold shock response in Escherichia coli

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The CspA family in Escherichia coli: multiple gene duplication for stress adaptation

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Chloramphenicol induces the transcription of the major cold shock gene of Escherichia coli, cspA

21 January 2018

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RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose absence triggers the cold-shock response.

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

21 January 2018

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Thermodynamic properties of an extremely rapid protein folding reaction

21 January 2018

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Cold shock stress-induced proteins in Bacillus subtilis

21 January 2018

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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

21 January 2018

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Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.

21 January 2018

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Major cold shock protein of Escherichia coli

21 January 2018

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Post-transcriptional regulation of CspA expression in Escherichia coli

21 January 2018

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Differential mRNA stability of the cspA gene in the cold-shock response of Escherichia coli

21 January 2018

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Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichlorophenolindophenol and potassium ferricyanide by L-ascorbic acid

21 January 2018

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Effects of heterologous expression of CspB, the major cold shock protein of Bacillus subtillis, on protein synthesis in Escherichia coli

21 January 2018

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First steps from a two-dimensional protein index towards a response-regulation map forBacillus subtilis

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.6.3407

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2 September 2017

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