J. Orts

发表

Proteome‐wide analysis of phospho‐regulated PDZ domain interactions

P. Güntert, Roland Arnold, Celestine N. Chi, 2018, Molecular systems biology.

Protein-ligand interactions revealed by liquide state NMR

J. Orts, 2010 .

Specific methyl group protonation for the measurement of pharmacophore-specific interligand NOE interactions.

C. Griesinger, T. Carlomagno, S. Bartoschek, 2008, Chemistry.

Proteome-wide analysis of phospho-regulated PDZ domain interactions through phosphomimetic proteomic peptide phage display

Roland Arnold, Celestine N. Chi, Y. Ivarsson, 2017, bioRxiv.

Stereospecific assignments in proteins using exact NOEs

R. Riek, P. Güntert, Beat Vögeli, 2013, Journal of Biomolecular NMR.

Methyl probes in proteins for determining ligand binding mode in weak protein–ligand complexes

M. Scanlon, M. Mobli, B. Doak, 2022, Scientific Reports.

eNORA2 Exact NOE Analysis Program.

Roland Riek, Beat Vögeli, Dean Strotz, 2017, Journal of chemical theory and computation.

Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.

Roland Riek, Julien Orts, R. Riek, 2017, Angewandte Chemie.

Crystallography-independent determination of ligand binding modes.

Peter Monecke, Christian Griesinger, Teresa Carlomagno, 2008, Angewandte Chemie.

Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds

R. Riek, Dhiman Ghosh, S. Saupe, 2019, Chembiochem : a European journal of chemical biology.

Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph

R. Riek, J. Orts, M. Wälti, 2017, PloS one.

The description of protein internal motions aids selection of ligand binding poses by the INPHARMA method

T. Carlomagno, B. Stauch, J. Orts, 2012, Journal of biomolecular NMR.

Comprehensive Fragment Screening of the SARS‐CoV‐2 Proteome Explores Novel Chemical Space for Drug Development

D. Laurents, J. Hoch, K. Saxena, 2022, Angewandte Chemie.

Solution NMR Studies of Recombinant Aβ(1–42): From the Presence of a Micellar Entity to Residual β‐Sheet Structure in the Soluble Species

R. Riek, Beat Vögeli, S. Campioni, 2015, Chembiochem : a European journal of chemical biology.

Towards a true protein movie: a perspective on the potential impact of the ensemble-based structure determination using exact NOEs.

R. Riek, P. Güntert, Beat Vögeli, 2014, Journal of magnetic resonance.

The description of protein internal motions aids selection of ligand binding poses by the INPHARMA method

Teresa Carlomagno, Julien Orts, T. Carlomagno, 2012, Journal of Biomolecular NMR.

The INPHARMA technique for pharmacophore mapping: A theoretical guide to the method.

Christian Griesinger, Teresa Carlomagno, Julien Orts, 2009, Journal of magnetic resonance.

NMR Molecular Replacement Provides New Insights into Binding Modes to Bromodomains of BRD4 and TRIM24

R. Walser, G. Walker, M. Packer, 2022, Journal of medicinal chemistry.

Protein—ligand structure determination with the NMR molecular replacement tool, NMR2

R. Riek, J. Orts, 2020, Journal of Biomolecular NMR.

Structure determination of protein-ligand complexes by NMR in solution.

J. Orts, A. Gossert, 2018, Methods.

The Exact Nuclear Overhauser Enhancement: Recent Advances

Peter Güntert, Simon Olsson, Morkos A. Henen, 2017, Molecules.

A Structural Ensemble for the Enzyme Cyclophilin Reveals an Orchestrated Mode of Action at Atomic Resolution.

Peter Güntert, Roland Riek, Beat Vögeli, 2015, Angewandte Chemie.

Elucidation of a nutlin-derivative—HDM2 complex structure at the interaction site by NMR Molecular Replacement: a straightforward derivation

N. Coudevylle, J. Orts, M. Marsh, 2022, Journal of Magnetic Resonance Open.

NMR-Based Determination of the 3D Structure of the Ligand-Protein Interaction Site without Protein Resonance Assignment.

R. Riek, P. Güntert, M. Marsh, 2016, Journal of the American Chemical Society.

The tubulin-bound structure of the antimitotic drug tubulysin.

K. Kubícek, T. Carlomagno, F. Sasse, 2010, Angewandte Chemie.

The experimental accuracy of the uni-directional exact NOE.

Beat Vögeli, J. Orts, D. Strotz, 2015, Journal of magnetic resonance.

Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications

Rachel W. Martin, D. Laurents, J. Hoch, 2021, Frontiers in Molecular Biosciences.

Protein–fragment complex structures derived by NMR molecular replacement† †Electronic supplementary information (ESI) available: ESI Fig. S1–S8, and Table S1 and S2. See DOI:10.1039/d0md00068j

B. Davis, Celestine N. Chi, Dhiman Ghosh, 2020, RSC medicinal chemistry.

Nuclear magnetic resonance structure-based drug design.

J. Orts, Felix Torres, 2018, Future medicinal chemistry.

Intermolecular detergent-membrane protein noes for the characterization of the dynamics of membrane protein-detergent complexes.

R. Riek, Beat Vögeli, J. Lorieau, 2014, The journal of physical chemistry. B.

The NMR2 Method to Determine Rapidly the Structure of the Binding Pocket of a Protein–Ligand Complex with High Accuracy

J. Orts, M. Wälti, 2018 .

Relaxation Matrix Analysis of Spin Diffusion for the NMR Structure Calculation with eNOEs.

R. Riek, Beat Vögeli, J. Orts, 2012, Journal of chemical theory and computation.

An NMR-based scoring function improves the accuracy of binding pose predictions by docking by two orders of magnitude

C. Griesinger, T. Carlomagno, S. Bartoschek, 2011, Journal of biomolecular NMR.

Serum adenosine deaminase assay in sarcoidosis has little clinical usefulness.

J. Orts, J. Mañá, F. Badrinas, 1986, Clinical chemistry.