Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Amino-acid sequence of sarcoplasmic calcium-binding protein from scallop (Patinopecten yessoensis) adductor striated muscle
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Cited by (19)
Seafood allergy: A comprehensive review of fish and shellfish allergens
2018, Molecular ImmunologyCitation Excerpt :The sequence identity varies greatly between species and multiple isoforms have been characterised. Crustacean SCBPs have two peptides (Wnuk and Jauregui-Adell, 1983; Takagi et al., 1984), subunits α and β, which can combine as either a homodimer or heterodimer isotype (α2, αβ, β2; SCBP-I, -II, and -III, respectively). Furthermore, multiple variants have also been reported (White et al., 2011).
Effects of triclosan in the freshwater mussel Dreissena polymorpha: A proteomic investigation
2012, Aquatic ToxicologyCitation Excerpt :Interestingly, we have found that TCS provokes a definite overexpression of two proteins involved in the mechanism of Ca2+-binding that is sarcoplasmic calcium-binding protein (spot no. 12, 1.9 fold variation) and annexin B9 (1.6 fold variation). Sarcoplasmic calcium-binding proteins (SCPs) are high-affinity EF-hand Ca2+ buffers identified exclusively in invertebrates, including molluscs (Takagi et al., 1984). Their role is in coordinating Ca2+ ion fluxes from the cytoplasm that in turn regulate cellular functions, such as cell proliferation, apoptosis, contraction and metabolism (Nagata et al., 1998; Cho et al., 2000).
Sarcoplasmic calcium-binding protein
1995, Comparative Biochemistry and Physiology -- Part B: Biochemistry andStructure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2·0 Å resolution
1992, Journal of Molecular Biology