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Crystal Structure of the Ca2+ - form and Ca2+ binding kinetics of metastasis-associated protein, S100A4

By A.R. Gingras, J. Basran, A. Prescott, M. Kriajevska, Clive R. Bagshaw and Igor L. Barsukov

Abstract

This is the author's final draft of the version published as FEBS Letters, 2008, 582, (2008), pp.1651-1656. The online version can also be accessed via http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T36-4SBHBHT-C&_user=123215&_coverDate=05%2F28%2F2008&_rdoc=4&_fmt=high&_orig=browse&_srch=doc-info(%23toc%234938%232008%23994179987%23690098%23FLA%23display%23Volume)&_cdi=4938&_sort=d&_docanchor=&_ct=26&_acct=C000010181&_version=1&_urlVersion=0&_userid=123215&md5=3371b907fc79bdf84ebf59e7604416f

Publisher: Elsevier
Year: 2008
OAI identifier: oai:lra.le.ac.uk:2381/3874

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Citations

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  2. (2002). Calcium coordination studies of the metastatic Mts1 protein. doi
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  6. (2006). Molecular mechanisms of Ca(2+) signaling in neurons induced by the S100A4 protein. doi
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  8. (2006). Recognition of the tumor suppressor protein p53 and other protein targets by the calcium-binding protein S100B. doi
  9. (2005). Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation. doi
  10. (2006). S100A4, a mediator of metastasis. doi
  11. (2002). Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy. doi
  12. (1997). Spectral studies on the calcium-binding properties of Mts1 protein and its interaction with target protein. doi
  13. (2005). The metastasis associated protein S100A4: role in tumour progression and metastasis. doi

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