Regular ArticleInhibition of Platelet Aggregation by the Recombinant Cysteine-Rich Domain of the Hemorrhagic Snake Venom Metalloproteinase, Atrolysin A
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The Relation between α-Helical Conformation and Amyloidogenicity
2018, Biophysical JournalCysteine as a potential anti-amyloidogenic agent with protective ability against amyloid induced cytotoxicity
2017, International Journal of Biological MacromoleculesCitation Excerpt :Further, side chains of cysteine has been shown to stabilize hydrophobic interactions and also tend to associate with hydrophobic regions of proteins [31]. Cysteine and its analogue have several applications in pharmaceutical and personal-care industries and also reported for inhibition of platelet aggregation, anti-amyloidogenic and stabilization of proteins against aggregation [32–34]. In order to get further insight into cysteine mediated aggregation inhibition of stem bromelain we evaluated the effect of cysteine by using various spectroscopic and microscopic techniques.
Snake venom metalloproteinases: Structure, function and relevance to the mammalian ADAM/ADAMTS family proteins
2012, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :Alternagin-C from Bthrops alternatus has been shown to modulate α2β1 integrin-mediated cell adhesion, migration and proliferation [76]. The recombinant C domain of atrolysin A, another P-IIIa SVMP from C. atrox venom, specifically binds to collagen type-1 and the A domain of VWF, blocking collagen–VWF interactions [77,78] through binding to the VWF A-domain (VWA) [79]. The C domain of atrolysin A also binds to VWA-like domain-containing ECM proteins, such as collagen XII, collagen XIV, and matrilins 1, 3 and 4 [80].
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