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The cystatins were the first amyloidogenic proteins to be shown to oligomerize through a 3D domain swapping mechanism. Here we… Expand Cystatins, an amyloid‐forming structural superfamily, form highly stable, domain‐swapped dimers at physiological protein… Expand The levels of cysteine proteinase inhibitors stefin A, stefin B, and cystatin C were determined using ELISAs in sera obtained… Expand Human cystatin C undergoes dimerization before unfolding. Dimerization leads to a complete loss of its activity as a cysteine… Expand Up-regulation of nitric oxide (NO) production by activated murine macrophages was observed during infection by Trypanosoma cruzi… Expand Two endopeptidases are present in the seeds of Vigna aconitifolia (moth bean), and their activities increase during germination… Expand Cathepsin L is known as the most unstable lysosomal cysteine proteinase at neutral or alkaline pH. The kinetics of inactivation… Expand The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures… Expand When an excess of human cystatin C or chicken cystatin was mixed with papain, an enzyme-inhibitor complex was formed immediately… Expand