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Adriano O. Henriques

Researcher at Universidade Nova de Lisboa

Publications -  103
Citations -  6765

Adriano O. Henriques is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: Bacillus subtilis & Gene. The author has an hindex of 38, co-authored 99 publications receiving 6161 citations. Previous affiliations of Adriano O. Henriques include Emory University.

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Structure, assembly, and function of the spore surface layers

TL;DR: New insights into the molecular details of spore surface morphogenesis provide avenues for exploitation of the sporesurface layers in applications for biotechnology and medicine.
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Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat.

TL;DR: This model of CotA contains all the structural features of a laccase, including the reactive surface-exposed copper center (T1) and two buried copper centers (T2 and T3), and shows a half-life of inactivation at 80 °C of about 4 and 2 h, indicating that CotA is intrinsically highly thermostable.
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Characterization of Bacillus Probiotics Available for Human Use

TL;DR: The results that provided evidence of colonization, immunostimulation, and antimicrobial activity support the hypothesis that the organisms carried in five commercial probiotic products have a potential probiotic effect.
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Screening for Bacillus Isolates in the Broiler Gastrointestinal Tract

TL;DR: Together, the results suggest that some of the sporeformers isolated in this study have the potential to persist in or transiently associate with the complex gut ecosystem.
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Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties.

TL;DR: Comparisons with the structure of other monomeric multicopper oxidases containing four copper atoms suggest that CotA may accept the largest substrates of any known laccase, and unlike other laccases, CotA appears to have a flexible lidlike region close to the substrate-binding site that may mediate substrate accessibility.