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Metal binding to the N-terminal cytoplasmic domain of the PIB ATPase HMA4 is required for metal transport in Arabidopsis.
Plant Mol Biol. 2016 Mar;90(4-5):453-66. doi: 10.1007/s11103-016-0429-z. Epub 2016 Jan 21.
Plant Mol Biol. 2016.
PMID: 26797794
Free article.
di-Cysteine motifs in the C-terminus of plant HMA4 proteins confer nanomolar affinity for zinc and are essential for HMA4 function in vivo.
Lekeux G, Laurent C, Joris M, Jadoul A, Jiang D, Bosman B, Carnol M, Motte P, Xiao Z, Galleni M, Hanikenne M.
Lekeux G, et al.
J Exp Bot. 2018 Nov 26;69(22):5547-5560. doi: 10.1093/jxb/ery311.
J Exp Bot. 2018.
PMID: 30137564
Free PMC article.
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Homology modeling and in vivo functional characterization of the zinc permeation pathway in a heavy metal P-type ATPase.
Lekeux G, Crowet JM, Nouet C, Joris M, Jadoul A, Bosman B, Carnol M, Motte P, Lins L, Galleni M, Hanikenne M.
Lekeux G, et al.
J Exp Bot. 2019 Jan 1;70(1):329-341. doi: 10.1093/jxb/ery353.
J Exp Bot. 2019.
PMID: 30418580
Free PMC article.
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di-Cysteine Residues of the Arabidopsis thaliana HMA4 C-Terminus Are Only Partially Required for Cadmium Transport.
Ceasar SA, Lekeux G, Motte P, Xiao Z, Galleni M, Hanikenne M.
Ceasar SA, et al. Among authors: lekeux g.
Front Plant Sci. 2020 May 26;11:560. doi: 10.3389/fpls.2020.00560. eCollection 2020.
Front Plant Sci. 2020.
PMID: 32528485
Free PMC article.
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