Recent Advances in Molecular and Cellular Functions of S100A10-Reference-Cited by-同舟云学术

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Recent Advances in Molecular and Cellular Functions of S100A10

Published:2023-09-26 Issue:10 Volume:13 Page:1450
ISSN:2218-273X
Container-title:Biomolecules
language:en
Short-container-title:Biomolecules

Author:

Okura Gillian C.¹^ORCID,Bharadwaj Alamelu G.¹²,Waisman David M.¹²^ORCID

Affiliation:

1. Department of Pathology, Dalhousie University, Halifax, NS B3H 1X5, Canada

2. Departments of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS B3H 1X5, Canada

Abstract

S100A10 (p11, annexin II light chain, calpactin light chain) is a multifunctional protein with a wide range of physiological activity. S100A10 is unique among the S100 family members of proteins since it does not bind to Ca2+, despite its sequence and structural similarity. This review focuses on studies highlighting the structure, regulation, and binding partners of S100A10. The binding partners of S100A10 were collated and summarized.

Funder

CIHR

Publisher

MDPI AG

Subject

Molecular Biology,Biochemistry

Link

https://www.mdpi.com/2218-273X/13/10/1450/pdf

Reference245 articles.

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4. Relaxation in Extracted Muscle Fibers;Bozler;J. Gen. Physiol.,1954

5. The Role of “Relaxing Factor” in Contraction-Relaxation Cycle of Muscle;Ebashi;Prog. Theor. Phys. Suppl.,1961

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