FIGURE

Fig. 1

ID

ZDB-FIG-220706-74

Publication

Bielak et al., 2022 - N'-terminal- and Ca²⁺-induced stabilization of high-order oligomers of full-length Danio rerio and Homo sapiens otolin-1

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Fig. 1

Fig. 1. Schematic representation of the domain-specific structure of otolin-1 based on UniProt data for otolin-1 with identifiers A5PN28 and A6NHN0 (A). Given segments (SP ? signal peptide; NC-N? ? noncollagenous N-terminal domain; central collagen-like domain and C-terminal globular C1q domain) are captioned with amino acid positions in the full primary sequence of the protein. Panel B shows fragments of otolin-1 trimeric structure models composed of the collagen-like domain 3 and C1q domains.

Expression Data

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Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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Reprinted from International journal of biological macromolecules, 209(Pt A), Bielak, K., Ho?ubowicz, R., Zoglowek, A., ?ak, A., K?dzierski, P., O?yhar, A., Dobryszycki, P., N'-terminal- and Ca²⁺-induced stabilization of high-order oligomers of full-length Danio rerio and Homo sapiens otolin-1, 1032-1047, Copyright (2022) with permission from Elsevier. Full text @ Int. J. Biol. Macromol.