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Martin Zacharias

Researcher at Technische Universität München

Publications -  344
Citations -  11986

Martin Zacharias is an academic researcher from Technische Universität München. The author has contributed to research in topics: Molecular dynamics & Medicine. The author has an hindex of 56, co-authored 304 publications receiving 10109 citations. Previous affiliations of Martin Zacharias include Jacobs University Bremen & International University, Cambodia.

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Separation‐shifted scaling, a new scaling method for Lennard‐Jones interactions in thermodynamic integration

TL;DR: In this paper, a new method of simultaneously scaling and shifting the LJ potential in molecular dynamics and thermodynamic integration (TI) simulations is presented, which allows the smooth creation or annihilation of atoms or molecules in an ensemble of solvent molecules during a molecular simulation.
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NWChem: Past, present, and future

Edoardo Aprà, +113 more
TL;DR: The NWChem computational chemistry suite is reviewed, including its history, design principles, parallel tools, current capabilities, outreach, and outlook.
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Protein–protein docking with a reduced protein model accounting for side-chain flexibility

TL;DR: The multicopy approach significantly improves the docking performance, using unbound (apo) binding partners without a significant increase in computer time and could be extended to include protein loop flexibility, and might also be useful for docking of modeled protein structures.
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NWChem: Past, Present, and Future

Edoardo Aprà, +113 more
TL;DR: The NWChem computational chemistry suite as discussed by the authors provides tools to support and guide experimental efforts and for the prediction of atomistic and electronic properties by using first-principledriven methodologies to model complex chemical and materials processes.
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A family of macrodomain proteins reverses cellular mono-ADP-ribosylation

TL;DR: These discoveries establish the complete reversibility of PARP-catalyzed cellular ADP-ribosylation as a regulatory modification and identify a family of macrodomain enzymes present in viruses, yeast and animals that reverse cellular ADp-ribsylation by acting on mono-ADP- ribosylated substrates.