Výsledky vyhledávání - "Chak Ming Sze"

Akademický článek

Interaction of cisplatin and analogues with a Met-rich protein site.

Autor: Chak Ming Sze¹, Khairallah, George N.¹, Zhiguang Xiao¹, Donnelly, Paul S.¹, O'Hair, Richard A. J.¹, Wedd, Anthony G.¹ agw@unimelb.edu.au

Publikováno v: Journal of Biological Inorganic Chemistry (JBIC). Feb2009, Vol. 14 Issue 2, p163-165. 3p. 1 Diagram, 3 Graphs.

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Interaction of cisplatin and analogue Pt(en)Cl2 with the copper metallo-chaperone Atox1

Autor: Zhiguang Xiao, Zhenyu Shi, Paul S. Donnelly, Richard A. J. O'Hair, George N. Khairallah, Anthony G. Wedd, Chak Ming Sze, Linda Feketeová

Publikováno v: Metallomics : integrated biometal science. 5(8)

The human metallo-chaperone protein Atox1 features a high affinity Cu(I) binding site Cys(12)GlyGlyCys(15) (KD = 10(-17.4) M at pH 7.0) and delivers copper to the trans-Golgi network (TGN). Atox1 may participate in the metabolism of the drug cis-Pt(N

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a9dbe2d21371f13b366aaa128a690b1
https://pubmed.ncbi.nlm.nih.gov/23778981

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PcoE--a metal sponge expressed to the periplasm of copper resistance Escherichia coli. Implication of its function role in copper resistance

Autor: Geoffrey J. Howlett, Zhiguang Xiao, Chak Ming Sze, Saumya R. Udagedara, Anthony G. Wedd, Matthias Zimmermann, Timothy M. Ryan

Publikováno v: Journal of inorganic biochemistry. 115

Expression of the periplasmic protein PcoE of Escherichia coli is induced strongly by cupric salts under the control of the chromosomal copper tolerance system cusRS. Its isolation and study were complicated by de-amidation of Asn 54 and 103 at alkal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6d804d0cdbdbb9ebea94220460833cb
https://pubmed.ncbi.nlm.nih.gov/22658755

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Interaction of cisplatin and analogues with a Met-rich protein site

Autor: Paul S. Donnelly, Richard A. J. O'Hair, George N. Khairallah, Zhiguang Xiao, Chak Ming Sze, Anthony G. Wedd

Publikováno v: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 14(2)

The chaperone protein CopC from Pseudomonas syringae features high-affinity binding sites (K (D) ~ 10(-13) M) for both Cu(I) (Met-rich) and Cu(II) (His-rich). When presented with these sites in the apoprotein, electrospray ionisation mass spectrometr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a51026a872a3fee47915220da351fcb
https://pubmed.ncbi.nlm.nih.gov/19034536

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