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Petr Halada

Researcher at Academy of Sciences of the Czech Republic

Publications -  185
Citations -  4536

Petr Halada is an academic researcher from Academy of Sciences of the Czech Republic. The author has contributed to research in topics: Proteome & Pyranose. The author has an hindex of 34, co-authored 179 publications receiving 3987 citations. Previous affiliations of Petr Halada include Charles University in Prague & University of Agricultural Sciences, Dharwad.

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Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens

TL;DR: It is to be hoped that the availability of the mycobacterial proteome will facilitate the design of novel measures for prevention and therapy of one of the great health threats, tuberculosis.
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C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances

TL;DR: The data identify C-terminal phosphorylation of Hsp70 and Hsp90 as a switch for regulating co-chaperone binding and indicate that cancer cells possess an elevated protein folding environment by the concerted action of co-Chaperone expression and chaperone modifications.
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Hepcidin, the hormone of iron metabolism, is bound specifically to α-2-macroglobulin in blood

TL;DR: The demonstration that alpha2-M is the hePCidin transporter could lead to better understanding of hepcidin physiology, methods for its sensitive measurement and the development of novel drugs for the treatment of iron-related diseases.
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Characteristics of Gloeophyllum trabeum Alcohol Oxidase, an Extracellular Source of H2O2 in Brown Rot Decay of Wood

TL;DR: The extracellular distribution and the enzyme's abundance and preference for methanol, potentially available from the demethylation of lignin, all point to a possible role for AOX as a major source of H2O2, a component of Fenton's reagent implicated in the generally accepted mechanisms for brown rot through the production of highly destructive hydroxyl radicals.