Associated Papers
Study of individual domains contributing to MALT1 dimerization in BCL10-independent and dependent assembly.
Kuo BJ et al.
Biochemical and Biophysical Research Communications, 2024
Intrinsic flexibility of NLRP pyrin domains is a key factor in their conformational dynamics, fold stability, and dimerization.
Huber RG et al.
Protein Science : a Publication of the Protein Society, 2015
Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions.
Eibl C et al.
Acta Crystallographica. Section D, Biological Crystallography, 2014
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