Structure-Based Mutagenesis Reveals Critical Residues in the Transferrin Receptor Participating in the Mechanism of pH-Induced Release of Iron from Human Serum Transferrin-Reference-Cited by-同舟云学术

Structure-Based Mutagenesis Reveals Critical Residues in the Transferrin Receptor Participating in the Mechanism of pH-Induced Release of Iron from Human Serum Transferrin

Published:2012-03-01 Issue:10 Volume:51 Page:2113-2121
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Steere Ashley N.¹,Chasteen N. Dennis²,Miller Brendan F.¹,Smith Valerie C.³,MacGillivray Ross T. A.³,Mason Anne B.¹

Affiliation:

1. Department of Biochemistry, University of Vermont, College of Medicine, 89 Beaumont Avenue, Burlington, Vermont 05405, United States

2. Department of Chemistry, Parsons Hall, University of New Hampshire, Durham, New Hampshire 03824, United States

3. Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, BC V6T 1Z3, Canada

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi3001038

Reference26 articles.

1. The Crystal Structure of Iron-free Human Serum Transferrin Provides Insight into Inter-lobe Communication and Receptor Binding

2. Chemistry and biology of eukaryotic iron metabolism

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