M. Frech

发表

CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2

A. Joachimiak, M. Arnaout, J. Xiong, 2002 .

Crystal Structure of the Extracellular Segment of Integrin αVβ3 in Complex with an Arg-Gly-Asp Ligand

Thilo Stehle, Rongguang Zhang, M. Amin Arnaout, 2002, Science.

Specific Interaction of a Novel Foamy Virus Env Leader Protein with the N-Terminal Gag Domain

S. Fuller, M. Frech, M. Löchelt, 2001, Journal of Virology.

Estimation of Drug-Target Residence Times by τ-Random Acceleration Molecular Dynamics Simulations.

R. Wade, M. Frech, M. Dreyer, 2018, Journal of chemical theory and computation.

Kinetics for Drug Discovery: an industry-driven effort to target drug residence time.

Leigh A. Stoddart, R. Wade, R. Leurs, 2017, Drug discovery today.

Letter to the Editor: Sequential assignment and secondary structure of saratin, an inhibitor of von Willebrand factor-dependent platelet adhesion to collagen

M. Frech, T. Maurer, J. Bomke, 2001, Journal of biomolecular NMR.

Binding of the H-ras p21 GTPase activating protein by the activated epidermal growth factor receptor leads to inhibition of the p21 GTPase activity in vitro.

J. Serth, A. Wittinghofer, M. Frech, 1992, Biochemistry.

Production and characterization of saratin, an inhibitor of von Willebrand factor-dependent platelet adhesion to collagen.

M F Hoylaerts, M. Frech, M. Hoylaerts, 2001, Seminars in thrombosis and hemostasis.

Structure of the leech protein saratin and characterization of its binding to collagen.

W. Gronwald, H. Kalbitzer, M. Frech, 2008, Journal of molecular biology.

NMR assignment of human HSP90 N-terminal domain bound to a long residence time resorcinol ligand

J. Boisbouvier, M. Frech, Elodie Crublet, 2022, Biomolecular NMR Assignments.

Nerve growth factor promotes activation of the alpha, beta and gamma isoforms of protein kinase B in PC12 pheochromocytoma cells.

M. Andjelkovic, D. Alessi, M. Frech, 1998, European journal of biochemistry.

Crystallization and preliminary X-ray structure analysis of thermally unstable p21(H-ras) guanosine complexes.

W. Kabsch, I. Schlichting, E. Pai, 1994, Acta crystallographica. Section D, Biological crystallography.

Structural and biophysical characterization of the Syk activation switch.

Djordje Musil, Jörg Bomke, Daniel Schwarz, 2012, Journal of molecular biology.

Ubiquitin protein ligase Nedd4 binds to connexin43 by a phosphorylation-modulated process

Jörg Bomke, W. Lehmann, M. Frech, 2006, Journal of Cell Science.

The inhibition of the GTPase activating protein‐Ha‐ras interaction by acidic lipids is due to physical association of the C‐terminal domain of the GTPase activating protein with micellar structures.

J. Serth, A. Wittinghofer, M. Frech, 1991, The EMBO journal.

The Protein Kinase B Family — Structure, Regulation and Function

M. Andjelkovic, M. Frech, B. Hemmings, 1997 .

Direct interaction of PU.1 with oncogenic transcription factors reduces its serine phosphorylation and promoter binding

M. Frech, E. Puccetti, S. Beez, 2012, Leukemia.

Role of Translocation in the Activation and Function of Protein Kinase B*

P. Cohen, M. Andjelkovic, D. Alessi, 1997, The Journal of Biological Chemistry.

Rapamycin-sensitive phosphorylation of PKC on a carboxy-terminal site by an atypical PKC complex

P. Parker, M. Frech, R. Whelan, 1999, Current Biology.

Guanine nucleotide binding properties of the mammalian RalA protein produced in Escherichia coli.

I. Schlichting, A. Wittinghofer, M. Frech, 1990, The Journal of biological chemistry.

Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity

A. Wittinghofer, M. Frech, J. Scheffler, 1992, Molecular and cellular biology.

Features of the Env leader protein and the N-terminal Gag domain of feline foamy virus important for virus morphogenesis.

M. Frech, M. Löchelt, V. Geiselhart, 2003, Virology.

Direct interaction of PU.1 with oncogenic transcription factors reduces its serine phosphorylation and promoter binding

M. Frech, E. Puccetti, S. Beez, 2012, Leukemia.

High Affinity Binding of Inositol Phosphates and Phosphoinositides to the Pleckstrin Homology Domain of RAC/Protein Kinase B and Their Influence on Kinase Activity*

M. Andjelkovic, M. Frech, B. Hemmings, 1997, The Journal of Biological Chemistry.

Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules

W. Kabsch, I. Schlichting, E. Pai, 1990, Cell.

Inhibition of GTPase activating protein stimulation of Ras-p21 GTPase by the Krev-1 gene product.

A. Wittinghofer, F. McCormick, M. Frech, 1990, Science.

Role of glutamine-61 in the hydrolysis of GTP by p21H-ras: an experimental and theoretical study.

T. Darden, L. Pedersen, P. Charifson, 1994, Biochemistry.

[13] Purification of baculovirus-expressed human Sos 1 protein

D. Bar-Sagi, D. Cussac, M. Frech, 1995 .

Protein conformational flexibility modulates kinetics and thermodynamics of drug binding

R. Wade, M. Frech, J. Bomke, 2017, Nature Communications.

Structure-kinetic relationship reveals the mechanism of selectivity of FAK inhibitors over PYK2.

R. Wade, S. Knapp, J. Elkins, 2021, Cell chemical biology.

The Three-Dimensional Structure of P21 in the Catalytically Active Conformation and Analysis of Oncogenic Mutants

W. Kabsch, I. Schlichting, E. Pai, 1991 .

Proton NMR studies of transforming and nontransforming H-ras p21 mutants.

I. Schlichting, A. Wittinghofer, M. Frech, 1990, Biochemistry.

Biochemical properties of Ha-ras encoded p21 mutants and mechanism of the autophosphorylation reaction.

R. Goody, A. Wittinghofer, M. Frech, 1988, The Journal of biological chemistry.

Scale-Up of Antibody Purification

M. Frech, L. Jacob, 2004 .

Affinity of guanine nucleotide binding proteins for their ligands: facts and artefacts.

R. Goody, A. Wittinghofer, M. Frech, 1991, Trends in biochemical sciences.

Protein conformational flexibility modulates kinetics and thermodynamics of drug binding

R. Wade, M. Frech, P. Matias, 2017, Nature Communications.

Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline‐rich motifs.

D. Cussac, M. Frech, P. Chardin, 1994, The EMBO journal.

Accurate absolute free energies for ligand–protein binding based on non-equilibrium approaches

Klaus Gerwert, Jürgen Schlitter, Djordje Musil, 2019, Communications Chemistry.

p21 with a phenylalanine 28----leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties.

I. Schlichting, J. Reinstein, R. Goody, 1991, The Journal of biological chemistry.

Visualizing the transiently populated closed-state of human HSP90 ATP binding domain

P. Gans, J. Boisbouvier, M. Frech, 2022, bioRxiv.

Optimized precursor to simplify assignment transfer between backbone resonances and stereospecifically labelled valine and leucine methyl groups: application to human Hsp90 N-terminal domain

P. Gans, J. Boisbouvier, M. Frech, 2021, Journal of Biomolecular NMR.

Ligand Desolvation Steers On-Rate and Impacts Drug Residence Time of Heat Shock Protein 90 (Hsp90) Inhibitors.

G. Ecker, M. Frech, D. Musil, 2018, Journal of Medicinal Chemistry.

PH domain of serine-threonine protein kinase B (RAC-PKB). Expression and binding assay for phosphoinositides and inositol phosphates.

M. Frech, B. Hemmings, 1998, Methods in molecular biology.

Ligand‐Induced Conformational Changes in HSP90 Monitored Time Resolved and Label Free—Towards a Conformational Activity Screening for Drug Discovery

K. Gerwert, M. Frech, D. Musil, 2018, Angewandte Chemie.

Structure-Kinetic-Relationship Reveals the Mechanism of Selectivity of FAK Inhibitors Over PYK2

R. Wade, S. Knapp, J. Elkins, 2020 .