C. Spitzfaden

发表

Inhibition of fibril formation in beta-amyloid peptide by a novel series of benzofurans.

J. Swatton, K. H. Jennings, D. Howlett, 1999, The Biochemical journal.

Building proteins with fibronectin type III modules.

I. Campbell, C. Spitzfaden, Claus Spitzfaden, 1994, Structure.

Structurally Diverse Mitochondrial Branched Chain Aminotransferase (BCATm) Leads with Varying Binding Modes Identified by Fragment Screening.

S. Pickett, C. Chung, C. Jamieson, 2016, Journal of medicinal chemistry.

Conformational polymorphism of cyclosporin A.

K Wüthrich, D Altschuh, K. Wüthrich, 1994, Structure.

The Discovery of in Vivo Active Mitochondrial Branched-Chain Aminotransferase (BCATm) Inhibitors by Hybridizing Fragment and HTS Hits.

S. Pickett, C. Chung, E. Nicodème, 2015, Journal of medicinal chemistry.

Structural Requirements for Biological Activity of the Ninth and Tenth FIII Domains of Human Fibronectin*

I. Campbell, H. Mardon, C. Spitzfaden, 1997, The Journal of Biological Chemistry.

Novel hydroxyl tricyclics (e.g., GSK966587) as potent inhibitors of bacterial type IIA topoisomerases.

S. Dabbs, D. Davies, E. Minthorn, 2013, Bioorganic & medicinal chemistry letters.

Crystallization and initial crystallographic analysis of covalent DNA-cleavage complexes of Staphyloccocus aureus DNA gyrase with QPT-1, moxifloxacin and etoposide.

A. Fosberry, O. Singh, M. Gwynn, 2015, Acta crystallographica. Section F, Structural biology communications.

Type IIA topoisomerase inhibition by a new class of antibacterial agents

Kristin K. Brown, M. Hann, A. Fosberry, 2010, Nature.

Mycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a dissociative mechanism that explains how ATP hydrolysis is coupled to domain motion.

M. Hann, M. Roué, C. Mayer, 2013, The Biochemical journal.

Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy

G. Wider, K. Wüthrich, M. Walkinshaw, 1991, Nature.

Protein secondary structure determination by NMR Application with recombinant human cyclophilin

G. Wider, K. Wüthrich, K. Memmert, 1991, FEBS letters.

Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity.

I D Campbell, I. Campbell, H. Mardon, 1997, Journal of molecular biology.

Discovery of functionally distinct anti-C7 monoclonal antibodies and stratification of anti-nicotinic AChR positive Myasthenia Gravis patients

Isabelle H. Osuch, Sébastien Petit-Frère, B. Morgan, 2022, Frontiers in Immunology.

Cyclosporin A—cyclophilin complex formation A model based on X‐ray and NMR data

G. Wider, K. Wüthrich, W. Braun, 1992, FEBS letters.

Structural basis of DNA gyrase inhibition by antibacterial QPT-1, anticancer drug etoposide and moxifloxacin

M. Hann, R. Tanner, A. Fosberry, 2015, Nature Communications.

A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules.

I D Campbell, C. Dobson, I. Campbell, 1997, Journal of molecular biology.

Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex

G. Wider, K. Wüthrich, W. Braun, 1994, Journal of biomolecular NMR.

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL

K. Wüthrich, A. Plückthun, R. Zahn, 1994, Nature.

The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA.

C. Prescott, R. Lehr, C. Spitzfaden, 2000, Journal of molecular biology.

Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module.

I. Campbell, K. Plaxco, C. M. Dobson, 1996, Proceedings of the National Academy of Sciences of the United States of America.