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Tuomo Laitinen

Researcher at University of Eastern Finland

Publications -  87
Citations -  1697

Tuomo Laitinen is an academic researcher from University of Eastern Finland. The author has contributed to research in topics: Monoacylglycerol lipase & Chemistry. The author has an hindex of 22, co-authored 79 publications receiving 1340 citations. Previous affiliations of Tuomo Laitinen include Martin Luther University of Halle-Wittenberg.

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Molecular dynamics studies on the thermostability of family 11 xylanases.

TL;DR: The MD analysis suggests regions in the protein structure which are more unstable and thus potential targets for mutation experiments to improve thermostability, in agreement with experimental mutant studies.
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Integrative and personalized QSAR analysis in cancer by kernelized Bayesian matrix factorization.

TL;DR: A novel kernelized Bayesian matrix factorization method is applied to solve the modeling task of predicting the responses to new drugs for new cancer cell lines, and a complete global map of drug response is explored to assess treatment potential and treatment range of therapeutically interesting anticancer drugs.
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Piperazine and Piperidine Triazole Ureas as Ultrapotent and Highly Selective Inhibitors of Monoacylglycerol Lipase

TL;DR: Piperazine and piperidine triazole ureas are characterized that combine the high potency attributable to the Triazole leaving group together with the bulky aromatic benzodioxolyl moiety required for selectivity, culminating in compound JJKK-048 that potently inhibited human and rodent MAGL.
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Covalent Binding of Three Epoxyalkyl Xylosides to the Active Site of endo-1,4-Xylanase II from Trichoderma reesei†,‡

TL;DR: In all three complexes, clear conformational changes were found in XYNII compared to the native structure, and these changes were largest in the X-O-C3 complex structure.
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Chiral 1,3,4-oxadiazol-2-ones as highly selective FAAH inhibitors.

TL;DR: The separated enantiomers showed clear differences in the potency and selectivity toward both FAAH and MAGL, and the selected S-enantiomers 51, 53, and 55 were shown to be tight binding, slowly reversible inhibitors of the hrFAAH.