Results 141 to 147 of about 3,141 (147)
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Novel interaction between CCR4 and CAF1 in rice CCR4–NOT deadenylase complex
Plant Molecular Biology, 2016Rice is an important crop in the world. However, little is known about rice mRNA deadenylation, which is an important regulation step of gene expression at the post-transcriptional level. The CCR4-NOT1 complex contains two key components, CCR4 and CAF1, which are the main cytoplasmic deadenylases in eukaryotic cells.
Wei-Lun, Chou +3 more
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The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states
Vaccine, 2010Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism. Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa). The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins ...
Soliakov A +3 more
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Biochemistry, 2001
A comparative study of the structural and functional properties of recombinant Yersinia pestis Caf1 and human IL-1beta was performed. According to Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) data, IL-1beta and Caf1 are typical beta-structural proteins.
Abramov, Vyacheslav +12 more
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A comparative study of the structural and functional properties of recombinant Yersinia pestis Caf1 and human IL-1beta was performed. According to Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) data, IL-1beta and Caf1 are typical beta-structural proteins.
Abramov, Vyacheslav +12 more
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Mouse CAF1, a mouse homologue of the yeast POP2 gene, complements the yeast pop2 null mutation
Yeast, 1999The yeast POP2 protein (Pop2p) is a component of a global transcription regulatory complex and is required for gene expression of many genes in Saccharomyces cerevisiae. We constructed POP2 deletion plasmids encoding various Pop2p regions under the native POP2 promoter and found that the minimum functional region was located in two-thirds of the ...
Y, Shimizu-Yoshida +5 more
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[Stabilization energy of the compact Caf1(13-149) subunit from Yersinia pestis].
Biofizika, 2011It has been shown by a variety of methods (circular dichroism, viscosimetry, intrinsic fluorescence, and fluorescence of labels) that, as in the case of small globular proteins the folding-unfolding transition in the Caf1(13-149) subunit under the action of two denaturants (urea and 1,3-dimethylurea) occurs between two major states (unfolded and ...
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The cooperative structure of the interleukin-like capsular protein CAF1 of Yersinia pestis
Immunology Letters, 1997A.M. Vasiliev +6 more
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