Protein Folding and Metal Ions: Mechanisms, Biology and Disease

Stewart Loh, PhD
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Journal of Biological Chemistry 24 , — Chorell , E. Bacterial chaperones CsgE and CsgC differentially modulate human alpha-synuclein amyloid formation via transient contacts. Christiansen , A.

Protein folding and metal ions : mechanisms, biology and disease in SearchWorks catalog

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Stewart Loh, PhD

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Differences in the binding of copper I to alpha- and beta-synuclein. Inorganic Chemistry 54 1 , — Chembiochem 16 16 , — Dean , K. Visualizing metal ions in cells: an overview of analytical techniques, approaches, and probes. Biochimica et Biophysica Acta 9 , — Demaurex , N. Mechanism of acidification of the trans-Golgi network TGN. In situ measurements of pH using retrieval of TGN38 and furin from the cell surface. Journal of Biological Chemistry 4 , — Denoyer , D. Metallomics 7 11 , — Dhar , A.

Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells. Biophysical Journal 2 , — Dominant mutants of ceruloplasmin impair the copper loading machinery in aceruloplasminemia. Journal of Biological Chemistry 7 , — Durao , P. Perturbations of the T1 copper site in the CotA laccase from Bacillus subtilis : structural, biochemical, enzymatic and stability studies.

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Oct 5, Summary. The role of metal ions in protein folding and structure is a critical topic to a range of scientists in numerous fields, particularly those. Jan 24, Protein Folding and Metal Ions: Mechanisms, Biology and Disease. Edited by Cláudio M. Gomes and Pernilla Wittung‐Stafshede. Jia‐Cherng.

Copper: an essential metal in biology. Current Biology 21 21 , R — R Fink , A. The aggregation and fibrillation of alpha-synuclein. Accounts of Chemical Research 39 9 , — Finney , L. X-ray fluorescence microscopy reveals large-scale relocalization and extracellular translocation of cellular copper during angiogenesis.

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Similar Items Related Subjects: 6 Metalloproteins. Previous Figure Next Figure. A second weak class of binding sites did not permit the accurate determination of binding stoichiometry, affinity or enthalpy change of the reaction. Interestingly, zinc fingers and carbon anhydrase represent the extremes of metalloprotein design in terms of protein-folding thermodynamics due to the fact that the former are unfolded while the latter are folded in the absence of zinc. The column was charged with 1 column volume CV of 0. Given that glyoxylase is inactivated by Zn II but activated by Ni II and Co II , it is unclear whether it is a true Ni-enzyme especially since 1 zinc binds more tightly than nickel, 2 nickel proteins are virtually unknown is higher eukaryotes and 3 no known nickel homeostasis factors in humans have yet been found To further eliminate apparent nonspecific binding of proteins to IMAC, fractionation of the proteins into weakly and strongly interacting sets by electrostatic or competitive displacement with NH 4 Cl and imidazole, respectively, was conducted.

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protein folding in the ER

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Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis. Hanahan , D. Hallmarks of cancer: the next generation. Cell 5 , — Harris , E. Basic and clinical aspects of copper. Critical Reviews in Clinical Laboratory Sciences 40 5 , — Hartl , F.

Unfolding the chaperone story. Molecular Biology of the Cell 28 22 , — Hasan , N. Journal of Biological Chemistry 43 , — Hatori , Y. Hellman , N. Ceruloplasmin metabolism and function. Annual Review of Nutrition 22 , — Homouz , D. Crowded, cell-like environment induces shape changes in aspherical protein.

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Journal of the American Chemical Society 7 , — Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson's disease.