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- W4241029419 abstract "Page 13901: In the course of studies that involved resequencing of equistatin molecule, an error in the published sequence was discovered. Consequently, Figs. 3 and 4should be replaced by the following figures. These lead to the conclusion that equistatin is not a two-domain protein as previously described, but a three-domain protein with molecular weight of 21,755. The inhibition properties and other characteristics are unchanged.Figure 4Alignment of thyroglobulin type-1 repeats. A, schematic diagram of thyroglobulin type-1 repeats as found in thyroglobulin (Tg, 10 repeats), ascidian nidogen (Nido asc, 3 repeats) (49), nidogen (Nido), saxiphilin (Sax, 2 repeats), pancreatic carcinoma marker protein (GA733), p41 invariant chain (p41), insulin-like growth factor binding proteins (IGFBP), chum salmon egg cysteine protease inhibitor (ECI), and equistatin (3 repeats). B, alignment of the equistatin-related proteins relative to the 48 amino acids of each of the three domains of equistatin (equista,equistb, and equistc). The compared sequences are human thyroglobulin domain 1.1 (Tg) (32), human invariant chain (p41) (50), chum salmon egg cysteine proteinase inhibitor (ECI) (34), mouse nidogen (nido) (36), two domains of bullfrog saxifilin (saxa and saxb) (39), human pancreatic carcinoma marker protein (GA733-2) (40), and human insulin-like growth factor binding protein (IGFBP-5) (37). Residues in boldface type are present in at least 6 of 11 sequences. The conserved cysteine residues are indicated with an arrowhead.View Large Image Figure ViewerDownload Hi-res image Download (PPT)" @default.
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- W4241029419 date "1998-05-01" @default.
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- W4241029419 title "Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain." @default.
- W4241029419 doi "https://doi.org/10.1016/s0021-9258(19)84313-2" @default.
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