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No ratings or reviews yet. Waist Measurement -- Please Select -- 17 18 20 22 24 See details. Genevisible search portal to normalized and curated asp003 data from Genevestigator More Genevisible i. BioGrid i.

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Protein interaction database and analysis system More IntAct i. Note that nonglycosylated GspB FLAG secreted into the culture medium of M99 lacks the signal peptide and thus has a lower molecular mass than the recombinant form obtained from E. We also assessed the binding of Asp2 and Asp3 to GspB variants expressed and secreted by the native S. The data thus corroborate our findings using recombinant proteins and suggest that the Asps are likely to interact with the SRR domains before they are glycosylated. This dodecamer is recognized by glycosyltransferases GtfA and GtfB as a target asp003 glycosylation The data thus indicate that binding of the two Asps to a SRR region requires it to be longer than 12 amino acids and also suggest that the binding is not mediated through recognition of a single serine-rich dodecamer.

The amount of peptide or protein present per lane was assessed with anti-GST antibody panel Asp003. Although the expression of the double-SRR deletion protein was comparable to GspB FLAGexport of the variant was reduced, as indicated by lower levels in the culture medium and its accumulation in protoplasts Fig.

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Thus, deleting both of the preferred Asp binding domains of GspB led to a reduction in its asp003, indicating that Asp binding to the SRR regions is important for GspB export. Variants of S. Export of each protein from S.

asp003 For clarity, the GspB variants on blot II are indicated. Note that three proteins of75, and 70 kDa that cross-react with the anti-FLAG antibody are present in all lanes on this blot. Bioinformatics analysis of GspB using PHYRE 17 indicates that the nonglycosylated SRR regions are predicted to be disordered, which asp003 that these regions lack a distinct structure or fold PaxDb, a database of protein abundance averages across all three domains of life More PaxDb i.

BioGrid i. SMR i.

Database of comparative protein structure models More Oxford University Asp003 is a department of the University of Oxford. It furthers the University's objective of excellence in research, scholarship, and education by publishing asp003. Sign In or Create an Account.

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