Members of a family of cold-shock proteins (CSPs) are found throughout the eubacterial
domain and appear to function as RNA-chaperones. They have been implicated in various …

Members of a family of small cold-shock proteins (CSPs) are induced during bacterial cell
response to a temperature decrease. Here we review available data about the structure …

The molecular mechanisms of cold acclimation are still largely unknown; however, it has
been established that overwintering plants such as winter wheat increases freeze tolerance …

CspA, the major cold-shock protein of Escherichia coli, is dramatically induced during the
cold-shock response. The amino acid sequence of CspA shows 43% identity to the" cold …

Ensuring the correct folding of RNA molecules in the cell is of major importance for a large
variety of biological functions. Therefore, chaperone proteins that assist RNA in adopting …

Bacterial cold shock proteins (CSPs) regulate the cellular response to temperature
downshift. Their general principle of function involves RNA chaperoning and transcriptional …

Cold shock proteins (Csps) comprise a family of small proteins that are structurally highly
conserved and bind to single-stranded nucleic acids via their nucleic acid binding motifs …

Cold‐shock proteins (Csps) are a subgroup of the cold‐induced proteins preferentially
expressed in bacteria and other organisms on reduction of the growth temperature below …

One of the many important consequences that temperature down-shift has on cells is
stabilization of secondary structures of RNAs. This stabilization has wide-spread effects …

In Escherichia coli, a family of cold shock proteins (CSPs) function as transcription
antiterminators or translational enhancers at low temperature by destabilizing RNA …