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Here we review recent structural studies of carbohydrate binding modules that mediate recognition events important for cell invasion and cytoadhesion.
Results of these simulations show that pathways evolve readily distinct sub-pathways or modules that mediate specific signal-response relations.
Mitogen-activated protein kinase (MAPK) cascades are highly conserved signaling modules that mediate the transduction of extracellular stimuli via receptors/sensors into intracellular responses and play key roles in plant immunity against pathogen attack.
A central role is assigned to modules that mediate between the users' workstations and data resources.
SH3 domains are protein modules that mediate protein-protein interactions in many eukaryotic signal transduction pathways.
It is believed that SH3 domains serve as modules that mediate protein-protein associations and, along with Src homology 2 (SH2) domains, regulate cytoplasmic signaling.
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The results demonstrate that GA releases DELLA-mediated inhibition of BZR1, and that the DELLA-BZR1-PIF4 interaction defines a core transcription module that mediates coordinated growth regulation by GA, BR and light signals.
The data presented here show that GEF-H1 and ZONAB form a signalling module that mediates Rho-stimulated transcription.
The caspase-recruitment domain (CARD) is a protein-binding module that mediates the assembly of CARD-containing proteins.
Our data thus indicate that GEF-H1 and ZONAB form a signalling module that mediates Rho-regulated cyclin D1 promoter activation and expression.
The caspase recruitment domain (CARD) is a protein-binding module that mediates the assembly of CARD-containing proteins into apoptosis and NFκB signaling complexes [ 28].
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