Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/73922
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Type: Journal article
Title: Structural approaches to probing metal interaction with proteins
Author: Parker, L.
Ascher, D.
Chen, G.
Miles, L.
Harris, H.
Parker, M.
Citation: Journal of Inorganic Biochemistry, 2012; 115:138-147
Publisher: Elsevier Science Inc
Issue Date: 2012
ISSN: 0162-0134
1873-3344
Statement of
Responsibility: 
Lorien J. Parker, David B. Ascher, Chen Gao, Luke A. Miles, Hugh H. Harris, Michael W. Parker
Abstract: In this mini-review we focus on metal interactions with proteins with a particular emphasis on the evident synergism between different biophysical approaches toward understanding metallobiology. We highlight three recent examples from our own laboratory. Firstly, we describe metallodrug interactions with glutathione S-transferases, an enzyme family known to attack commonly used anti-cancer drugs. We then describe a protein target for memory enhancing drugs called insulin-regulated aminopeptidase in which zinc plays a role in catalysis and regulation. Finally we describe our studies on a protein, amyloid precursor protein, that appears to play a central role in Alzheimer's disease. Copper ions have been implicated in playing both beneficial and detrimental roles in the disease by binding to different regions of this protein.
Keywords: Amyloid precursor protein; Glutathione transferase; Insulin-regulated aminopeptidase; X-ray absorption spectroscopy; X-ray crystallography
Rights: Copyright © 2012 Elsevier Inc. All rights reserved.
RMID: 0020122134
DOI: 10.1016/j.jinorgbio.2012.02.015
Appears in Collections:Chemistry publications
IPAS publications
Environment Institute publications

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