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1H, 13C, and 15N backbone and side-chain chemical shift assignments for the 29 kDa human galectin-1 protein dimer

by: Irina Nesmelova, Mabel Pang, Linda Baum, Kevin Mayo
Biomolecular NMR Assignments, Vol. 2, No. 2. (1 December 2008), pp. 203-205, doi:10.1007/s12104-008-9121-9  Key: citeulike:3644370

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Abstract

Abstract  Galectin-1 is an important regulator of leukocyte function and tumor angiogenesis. Recently, this lectin has been identified as a molecular target for the potent angiogenesis inhibitor anginex. Here, we report 1H, 13C, and 15N chemical shift assignments for human galectin-1 as determined by using heteronuclear triple resonance NMR spectroscopy.


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