Johan Aqvist

发表

Combining docking, molecular dynamics and the linear interaction energy method to predict binding modes and affinities for non-nucleoside inhibitors to HIV-1 reverse transcriptase.

Jens Carlsson, Lars Boukharta, J. Åqvist, 2008, Journal of medicinal chemistry.

Computational analysis of plasmepsin IV bound to an allophenylnorstatine inhibitor

Hugo Gutiérrez-de-Terán, J. Åqvist, H. Gutiérrez‐de‐Terán, 2006, FEBS letters.

Computational prediction of structure, substrate binding mode, mechanism, and rate for a malaria protease with a novel type of active site.

J. Åqvist, S. Bjelic, Johan Aqvist, 2004, Biochemistry.

Catalysis and linear free energy relationships in aspartic proteases.

J. Åqvist, S. Bjelic, Johan Aqvist, 2006, Biochemistry.

Computational study of the binding affinity and selectivity of the bacterial ammonium transporter AmtB.

Martin Almlöf, J. Åqvist, V. Luzhkov, 2006, Biochemistry.

Ligand binding to the voltage-gated Kv1.5 potassium channel in the open state--docking and computer simulations of a homology model.

J. Åqvist, V. Luzhkov, M. Andér, 2008, Biophysical journal.

Free energy calculations show that acidic P1 variants undergo large pKa shifts upon binding to trypsin

J. Åqvist, Johan Aqvist, Arne O Smalås, 2006, Proteins.

Inhibitor binding to the plasmepsin IV aspartic protease from Plasmodium falciparum.

Peng Liu, Hugo Gutiérrez-de-Terán, Anders Hallberg, 2006, Biochemistry.

Calculations of solute and solvent entropies from molecular dynamics simulations.

Jens Carlsson, J. Åqvist, Jens Carlsson, 2006, Physical chemistry chemical physics : PCCP.

Free energy calculations and ligand binding.

Martin Almlöf, J. Åqvist, V. Luzhkov, 2003, Advances in protein chemistry.

Energetics of codon-anticodon recognition on the small ribosomal subunit.

Martin Almlöf, J. Åqvist, M. Almlöf, 2007, Biochemistry.

Probing the effect of point mutations at protein-protein interfaces with free energy calculations.

Martin Almlöf, J. Åqvist, B. Brandsdal, 2006, Biophysical journal.

Electrostatic contributions to binding of transition state analogues can be very different from the corresponding contributions to catalysis: phenolates binding to the oxyanion hole of ketosteroid isomerase.

Arieh Warshel, Johan Aqvist, Pankaz K Sharma, 2007, Biochemistry.

Potent inhibitors of the Plasmodium falciparum enzymes plasmepsin I and II devoid of cathepsin D inhibitory activity.

Anders Hallberg, J. Åqvist, Elizabeth Hamelink, 2004, Journal of medicinal chemistry.

Cold adaptation of enzyme reaction rates.

J. Åqvist, B. Brandsdal, S. Bjelic, 2008, Biochemistry.