A novel variant in caspase recruitment domain family member 11 highlights the variability of clinical manifestations and management in a three generation family.
Study present a structure of the N-terminal region of CARD9 which exhibits an extensive autoinhibitory interface required to prevent constitutive activation in both CARD9 and CARD11 and define the distinct structural mechanisms of activation in CARD9 and CARD11 and demonstrate that upon activation both proteins form helical templates that directly nucleate Bcl10 polymerization.
Studies indicate that caspase recruitment domain family member 11 protein (CARD11) functions as a key signaling scaffold that controls antigen-induced lymphocyte activation during the adaptive immune response (review).
Data indicate the importance of "tuning" caspase recruitment domain family member 11 (CARD11 or CARMA1)-B cell CLL/lymphoma 10 (BCL10)-MALT1 paracaspase (MALT1) complex (CBM) signaling to preserve immune homeostasis (review)
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