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1 vergent gene cluster that encodes a putative cold shock protein.
2 of the csp22 peptide derived from bacterial 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 Gly-rich, zinc finger-containing RBPs called cold shock proteins 1-4 (CSP1-CSP4), that possess an evo
8 n of two cell-free expressed model proteins, cold shock protein A and apomyoglobin (apoMb) in cell-fr
9 , consistent with previous results for CspA (cold shock protein A) and LysN (anticodon binding domain
12 tide-binding domain found in the prokaryotic cold shock protein and the translation initiation factor
13 g factor A) protein that was identified as a cold-shock protein and an auxiliary factor acting in the
18 t CspE, a member of a family of RNA-binding "cold shock" proteins, and S1, an essential component of
19 is of any other protein, indicating that the cold shock proteins are able to bypass the inhibitory ef
22 lem, we studied the dynamics of the unfolded cold-shock protein at different solvent viscosities and
23 iffers from the mesophilic Bacillus subtilis cold shock protein B (Bs-CspB) in 11 of the 66 residues.
24 , we investigate the mechanical unfolding of cold shock protein B (Csp), a showcase two-state folder,
25 ctrin R16 domain, Arc repressor, apo-azurin, cold shock protein B (cspB), C-terminal domain of riboso
30 degrees C causes transcription of the major cold shock protein (CSP) bicistronic gene cspA1/A2 to in
31 haea do not contain members of the bacterial cold shock protein (Csp) family, they all contain homolo
33 ter of cspA, a gene that codes for the major cold shock protein CspA of E. coli, contains an extended
35 protein of high sequence similarity with the cold shock protein CspA, but cspD expression is not indu
36 helicases (DBRHs) (CsdA, SrmB, RhlB) and the cold shock protein CspA, improves fitness of two indepen
37 a protein (CspA) highly similar to the major cold shock proteins CspA and CspB of Escherichia coli an
44 spB-1, which represents residues 1-22 of the cold shock protein CspB from Bacillus subtilis, has been
45 -TB that has the same core as the mesophilic cold shock protein CspB-Bs from Bacillus subtilis, but o
46 r verification, we have shown that the major cold shock protein (CspB) from Bacillus subtilis binds w
47 chaperone-like proteins, HdeA and HdeB; the cold shock protein, CspC; the YbgS (or homeobox protein)
48 s by repressing cspE at the LexA palindrome; cold-shock protein CspE enhances translation of rpoS mRN
52 dmCl concentration [C] for the protein L and cold shock protein CspTm compare well with experiments.
54 3 and the mechanisms by which mRNAs encoding cold shock proteins escape cooling-induced translational
56 single-molecule FRET measurements of a small cold-shock protein expose equilibrium collapse of the un
59 ion in the denatured state of CspTm, a small cold-shock protein from Thermotoga maritima, engineered
60 amino acid sequence identity with the major cold shock protein in E. coli, CspA, which has been show
64 ling and hibernation also induce a number of cold-shock proteins in the brain, including the RNA bind
65 and is characterized by induction of several cold shock proteins, including CsdA, during the acclimat
66 and is characterized by induction of several cold shock proteins, including polynucleotide phosphoryl
67 nse is characterized by induction of several cold shock proteins, including the DEAD-box helicase Csd
69 parison with 25 experimentally characterized cold shock protein mutants reveals an average correlatio
72 -containing proteins such as CspA (the major cold shock protein of Escherichia coli) and its homologu
73 ism of cold shock induction of CspA, a major cold shock protein of Escherichia coli, deletion analysi
85 slatome, including the upregulation of a new cold shock protein, RTN3, a reticulon protein implicated
86 Mutational analyses confirmed that the small cold shock proteins, So1648 and So2787, are involved in
87 he synthesis of not only CspA but also other cold-shock proteins such as CspB and CsdA to be no longe
89 rature downshift, a group of proteins called cold shock proteins, such as CspA, CspB, and CsdA, are t
90 s reduced to new basal levels, while the non-cold shock protein synthesis is resumed, resulting in ce
92 structural similarity to the RbfA protein, a cold shock protein that also specifically associates wit
93 ns of the compact unfolded state of a small cold shock protein under native conditions, but decrease
94 Finally, it is demonstrated that designed cold shock protein variants exhibit electrostatic proper
96 utational and sequence analysis of bacterial cold shock proteins, we designed a protein (CspB-TB) tha
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