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1  of the csp22 peptide derived from bacterial cold shock protein.
2 vergent gene cluster that encodes a putative cold shock protein.
3 ation and/or initiation of translation, is a cold-shock protein.
4 thought to be involved in RNA binding by the cold-shock proteins.
5  TF synthesis was induced, like that of many cold-shock proteins.
6 binding protein 7 (GRP7) in association with cold shock protein 1 (CSP1) emerged as a potential trans
7 Gly-rich, zinc finger-containing RBPs called cold shock proteins 1-4 (CSP1-CSP4), that possess an evo
8 n-like structure, similar to that present in cold shock protein A (CspA).
9 n of two cell-free expressed model proteins, cold shock protein A and apomyoglobin (apoMb) in cell-fr
10 , consistent with previous results for CspA (cold shock protein A) and LysN (anticodon binding domain
11                        Although well-studied cold-shock protein A (CspA) family members are induced a
12        Certain members of the CspA family of cold shock proteins act as nucleic acid chaperones: they
13 tide-binding domain found in the prokaryotic cold shock protein and the translation initiation factor
14 g factor A) protein that was identified as a cold-shock protein and an auxiliary factor acting in the
15                                          For cold-shock protein and the SH3 domain, we accurately rep
16           The RNase R of A. hydrophila was a cold-shock protein and was required for bacterial growth
17 he synthesis of cellular proteins other than cold-shock proteins and cell growth was observed.
18    This identified further interactions with cold-shock proteins and novel KH-domain proteins.
19                The present results show that cold-shock proteins and S1 domains share not only the te
20 cluding the excisionase of CP4So prophage, a cold shock protein, and a stress-related chemosensory sy
21  99.9% of bacterial genomes contain multiple cold shock proteins, and 46% carry a nonimmunogenic form
22 t CspE, a member of a family of RNA-binding "cold shock" proteins, and S1, an essential component of
23 as genes encoding methane/ammonia oxidation, cold-shock protein, and two-component systems were gener
24 is of any other protein, indicating that the cold shock proteins are able to bypass the inhibitory ef
25                                              Cold-shock proteins are synthesized to overcome the dele
26 mologous pair of thermophilic and mesophilic cold shock proteins at high temperatures.
27 lem, we studied the dynamics of the unfolded cold-shock protein at different solvent viscosities and
28 iffers from the mesophilic Bacillus subtilis cold shock protein B (Bs-CspB) in 11 of the 66 residues.
29 , we investigate the mechanical unfolding of cold shock protein B (Csp), a showcase two-state folder,
30 ctrin R16 domain, Arc repressor, apo-azurin, cold shock protein B (cspB), C-terminal domain of riboso
31       The thermophilic Bacillus caldolyticus cold shock protein (Bc-Csp) differs from the mesophilic
32                              CspA, the major cold shock protein, binds RNA with low sequence specific
33 bacterial antagonism, where a nonimmunogenic cold shock protein blocks perception of immunogenic form
34                  The data also indicate that cold-shock proteins can be translated by ribosomes under
35                         The Escherichia coli cold shock protein CsdA is a member of the DEAD box fami
36  degrees C causes transcription of the major cold shock protein (CSP) bicistronic gene cspA1/A2 to in
37 haea do not contain members of the bacterial cold shock protein (Csp) family, they all contain homolo
38                         The Escherichia coli cold shock protein CspA family consists of nine proteins
39 ter of cspA, a gene that codes for the major cold shock protein CspA of E. coli, contains an extended
40                           We report that the cold shock protein CspA of Staphylococcus aureus is requ
41 protein of high sequence similarity with the cold shock protein CspA, but cspD expression is not indu
42 helicases (DBRHs) (CsdA, SrmB, RhlB) and the cold shock protein CspA, improves fitness of two indepen
43 a protein (CspA) highly similar to the major cold shock proteins CspA and CspB of Escherichia coli an
44 by an increase in the synthesis of the major cold shock proteins CspA, CspB, and CspG.
45 ichia coli transiently synthesizes the major cold-shock protein CspA.
46                                    The major cold-shock protein (CspA) from Escherichia coli is a sin
47                                            A cold-shock protein, CspA, was associated with the ion ne
48 ctor, RpoS, but was independent of the major cold-shock protein, CspA.
49                                          The cold shock protein CspB from Bacillus subtilis binds T-b
50 spB-1, which represents residues 1-22 of the cold shock protein CspB from Bacillus subtilis, has been
51 -TB that has the same core as the mesophilic cold shock protein CspB-Bs from Bacillus subtilis, but o
52 r verification, we have shown that the major cold shock protein (CspB) from Bacillus subtilis binds w
53  chaperone-like proteins, HdeA and HdeB; the cold shock protein, CspC; the YbgS (or homeobox protein)
54 s by repressing cspE at the LexA palindrome; cold-shock protein CspE enhances translation of rpoS mRN
55      During this acclimation phase, specific cold shock proteins (CSPs) are highly induced.
56                                              Cold shock proteins (CSPs) enhance acclimatization of ba
57                                    Bacterial cold shock proteins (CSPs) function as RNA chaperones.
58                                              Cold-shock proteins (Csps) are a family of small nucleic
59 dmCl concentration [C] for the protein L and cold shock protein CspTm compare well with experiments.
60 /beta protein L and the 66-residue, all-beta cold-shock protein CspTm.
61                                We found that cold shock protein E (cspE or STM14_0732) is up-regulate
62 3 and the mechanisms by which mRNAs encoding cold shock proteins escape cooling-induced translational
63                               RbfA is also a cold-shock protein essential for Escherichia coli cells
64 single-molecule FRET measurements of a small cold-shock protein expose equilibrium collapse of the un
65 lt is correlated with thermostability in the cold shock protein family.
66                    Members of bacterial Csp (cold-shock protein) family promote cellular adaptation t
67 ion in the denatured state of CspTm, a small cold-shock protein from Thermotoga maritima, engineered
68  amino acid sequence identity with the major cold shock protein in E. coli, CspA, which has been show
69                   The mRNA for CspA, a major cold shock protein in Escherichia coli, contains an unus
70                                  PNPase is a cold shock protein in S. coelicolor and the activity of
71       CspA was originally found as the major cold-shock protein in Escherichia coli, consisting of 70
72 ling and hibernation also induce a number of cold-shock proteins in the brain, including the RNA bind
73 and is characterized by induction of several cold shock proteins, including CsdA, during the acclimat
74 and is characterized by induction of several cold shock proteins, including polynucleotide phosphoryl
75 nse is characterized by induction of several cold shock proteins, including the DEAD-box helicase Csd
76               Escherichia coli CspA, a major cold shock protein, is dramatically induced upon tempera
77                                      CspA, a cold shock protein, is known to control sigma(B) activit
78 parison with 25 experimentally characterized cold shock protein mutants reveals an average correlatio
79 of four pairs of residues in CspA, the major cold shock protein of E. coli.
80         The relaxation kinetics of the major cold shock protein of Escherichia coli (CspA) in respons
81 -containing proteins such as CspA (the major cold shock protein of Escherichia coli) and its homologu
82 ism of cold shock induction of CspA, a major cold shock protein of Escherichia coli, deletion analysi
83                              CspA, the major cold shock protein of Escherichia coli, is dramatically
84            When the gene for CspA, the major cold shock protein of Escherichia coli, was disrupted by
85              CspA, CspB, and CspG, the major cold shock proteins of Escherichia coli, are dramaticall
86                 The gene for CspA, the major cold-shock protein of Escherichia coli is known to be dr
87                              CspA, the major cold-shock protein of Escherichia coli, has recently bee
88                              CspA, the major cold-shock protein of Escherichia coli, is an RNA chaper
89                              CspA, the major cold-shock protein of Escherichia coli, is dramatically
90                                              Cold-shock proteins of the CspA family help bacterial ce
91                                              Cold-shock proteins of the CspA family of Escherichia co
92 functional homologue of the Escherichia coli cold-shock protein pY.
93 otective, mediated, at least in part, by the cold shock protein, RBM3.
94                   Enhanced expression of the cold-shock protein RNA binding motif 3 (RBM3) is highly
95 slatome, including the upregulation of a new cold shock protein, RTN3, a reticulon protein implicated
96 Mutational analyses confirmed that the small cold shock proteins, So1648 and So2787, are involved in
97 he synthesis of not only CspA but also other cold-shock proteins such as CspB and CsdA to be no longe
98 translatable ribosomes by the association of cold-shock proteins such as RbfA.
99 rature downshift, a group of proteins called cold shock proteins, such as CspA, CspB, and CsdA, are t
100 s reduced to new basal levels, while the non-cold shock protein synthesis is resumed, resulting in ce
101                              Three wild-type cold shock proteins taken from mesophilic, thermophilic,
102 structural similarity to the RbfA protein, a cold shock protein that also specifically associates wit
103  ns of the compact unfolded state of a small cold shock protein under native conditions, but decrease
104    Finally, it is demonstrated that designed cold shock protein variants exhibit electrostatic proper
105     Surprisingly, the synthesis of all these cold shock proteins was induced at a significantly high
106 utational and sequence analysis of bacterial cold shock proteins, we designed a protein (CspB-TB) tha

 
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