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Janda, Jan-Oliver und Busch, Markus und Kuck, Fabian und Porfenenko, Mikhail und Merkl, Rainer (2012) CLIPS-1D: Analysis of multiple sequence alignments to deduce for residue-positions a role in catalysis, ligand-binding, or protein structure. BMC Bioinformatics (OA-ID: 89)
Janda, Jan-Oliver und Popal, Ajmal und Baucer, Jochen und Busch, Markus und Klocke, Michael und Spitzer, Wolfgang und Keller, Jörg und Merkl, Rainer (2014) H2rs: Deducing evolutionary and functionally important residue positions by means of an entropy and similarity based analysis of multiple sequence alignments. BMC Bioinformatics (OA-ID: 389)
Kandlinger, Florian und Plach, Maximilian G. und Merkl, Rainer (2017) AGeNNT: annotation of enzyme families by means of refined neighborhood networks. BMC Bioinformatics (OA-ID: 947)
Merkl, Rainer und Löffler, Patrick und Schmitz, Samuel und Hupfeld, Enrico und Stern, Reinhard (2017) Rosetta:MSF: a modular framework for multi-state computational protein design. PLoS Computational Biology (OA-ID: 865)
Merkl, Rainer und Plach, Maximilian G. und Reisinger, Bernd und Sterner, Reinhard (2016) Long-Term Persistence of Bi-functionality Contributes to the Robustness of Microbial Life through Exaptation. PLoS Genetics (OA-ID: 614)
Merkl, Rainer und Verprinsky, Valery und Heizinger, Leonhard und Plach, Maximilian G. (2017) Assessing in silico the recruitment and functional spectrum of bacterial enzymes from secondary metabolism. BMC Evolutionary Biology (OA-ID: 797)
Merkl, Rainer und Žváček, Clemens und Friedrichs, Gerald und Heizinger, Leonhard (2015) An assessment of catalytic residue 3D ensembles for the prediction of enzyme function. BMC Bioinformatics (OA-ID: 586)
von Mandach, Conrad und Merkl, Rainer (2010) Genes optimized by evolution for accurate and fast translation encode in Archaea and Bacteria a broad and characteristic spectrum of protein functions. BMC Genomics (OA-ID: 3)