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Armin Lahm
Researcher at Merck & Co.
Publications - 83
Citations - 4910
Armin Lahm is an academic researcher from Merck & Co.. The author has contributed to research in topics: Binding site & Virus. The author has an hindex of 33, co-authored 80 publications receiving 4623 citations. Previous affiliations of Armin Lahm include Schering-Plough & Centre national de la recherche scientifique.
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Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases.
Armin Lahm,Chantal Paolini,Michele Pallaoro,Maria Chiara Nardi,Philip Jones,Petra Neddermann,Sonia Sambucini,Matthew J. Bottomley,P. Lo Surdo,Andrea Carfi,Uwe Koch,R. De Francesco,Christian Steinkühler,Paola Gallinari +13 more
TL;DR: Evidence is presented supporting the view that vertebrate class IIa HDACs may have evolved to maintain low basal activities on acetyl-lysines and to efficiently process restricted sets of specific, still undiscovered natural substrates.
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A T-cell HCV vaccine eliciting effective immunity against heterologous virus challenge in chimpanzees.
Antonella Folgori,Stefania Capone,Lionello Ruggeri,Annalisa Meola,Elisabetta Sporeno,Bruno Bruni Ercole,Monica Pezzanera,Rosalba Tafi,Mirko Arcuri,Elena Fattori,Armin Lahm,Alessandra Luzzago,Alessandra Vitelli,Stefano Colloca,Riccardo Cortese,Alfredo Nicosia +15 more
TL;DR: The findings show that it is possible to elicit effective immunity against heterologous HCV strains by stimulating only the cellular arm of the immune system, and suggest a path for new immunotherapy against highly variable human pathogens like HCV, HIV or malaria, which can evade humoral responses.
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Structure refined to 2A of a nicked DNA octanucleotide complex with DNase I.
TL;DR: In this article, the authors co-crystallized a complex of DNase I with a self-complementary octanucleotide and refined the crystal structure at 2 A resolution.
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X-ray structure of the DNase I-d(GGTATACC)2 complex at 2.3 A resolution.
TL;DR: Results further support the hypothesis that the minor-groove width and depth and the intrinsic flexibility of DNA are the most important parameters affecting the interaction, and reveal some differences that may explain the relative resistance of the d(GGTATACC)2 duplex to cleavage by DNase I.
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Crystal structure of Penicillium citrinum P1 nuclease at 2.8 A resolution.
TL;DR: P1 nuclease from Penicillium citrinum is a zinc dependent glyco‐enzyme which cleaves single‐stranded RNA and DNA into 5′‐mononucleotides and a cleavage mechanism is proposed involving nucleophilic attack by a Zn activated water molecule.