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Items: 5

1.

Unique structural features in an Nramp metal transporter impart substrate-specific proton cotransport and a kinetic bias to favor import.

Bozzi AT, Bane LB, Zimanyi CM, Gaudet R.

J Gen Physiol. 2019 Oct 16. pii: jgp.201912428. doi: 10.1085/jgp.201912428. [Epub ahead of print]

PMID:
31619456
2.

Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter.

Bozzi AT, Zimanyi CM, Nicoludis JM, Lee BK, Zhang CH, Gaudet R.

Elife. 2019 Feb 4;8. pii: e41124. doi: 10.7554/eLife.41124.

3.

Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.

Bozzi AT, Bane LB, Weihofen WA, Singharoy A, Guillen ER, Ploegh HL, Schulten K, Gaudet R.

Structure. 2016 Dec 6;24(12):2102-2114. doi: 10.1016/j.str.2016.09.017. Epub 2016 Nov 10.

4.

Conserved methionine dictates substrate preference in Nramp-family divalent metal transporters.

Bozzi AT, Bane LB, Weihofen WA, McCabe AL, Singharoy A, Chipot CJ, Schulten K, Gaudet R.

Proc Natl Acad Sci U S A. 2016 Sep 13;113(37):10310-5. doi: 10.1073/pnas.1607734113. Epub 2016 Aug 29.

5.

IRF3 contributes to sepsis pathogenesis in the mouse cecal ligation and puncture model.

Walker WE, Bozzi AT, Goldstein DR.

J Leukoc Biol. 2012 Dec;92(6):1261-8. doi: 10.1189/jlb.0312138. Epub 2012 Oct 9.

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