M. Schade

发表

NMR fragment screening: Advantages and applications.

Markus Schade, M. Schade, 2006, IDrugs : the investigational drugs journal.

Antigen 85C Inhibition Restricts Mycobacterium tuberculosis Growth through Disruption of Cord Factor Biosynthesis

S. Kaufmann, B. Schlegel, A. Diehl, 2012, Antimicrobial Agents and Chemotherapy.

Discovery of Novel MDR-Mycobacterium tuberculosis Inhibitor by New FRIGATE Computational Screen

C. Scheich, B. Vértessy, Zoltan Szabadka, 2011, PloS one.

A 6 bp Z‐DNA hairpin binds two Zα domains from the human RNA editing enzyme ADAR1

A. Rich, K. Lowenhaupt, H. Oschkinat, 1999 .

Novel small molecule inhibitors of MDR Mycobacterium tuberculosis by NMR fragment screening of antigen 85C.

C. Scheich, M. Schade, V. Puetter, 2010, Journal of medicinal chemistry.

Discovery of low-molecular-weight ligands for the AF6 PDZ domain.

P. Schmieder, A. Diehl, K. Moelling, 2006, Angewandte Chemie.

Design and structure of stapled peptides binding to estrogen receptors.

Robert B. Moore, Nichola L. Davies, A. Pannifer, 2011, Journal of the American Chemical Society.

Does the primary deposit affect the biogeochemical transformation of placer gold and associated biofilms?

A. Bissett, F. Reith, M. Rea, 2019, Gondwana Research.

The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA.

H Oschkinat, P. Schmieder, A. Rich, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Small‐Molecule Inhibitors of AF6 PDZ‐Mediated Protein–Protein Interactions

P. Schmieder, D. Doyle, A. Diehl, 2014, ChemMedChem.

Structure–function analysis of the Z‐DNA‐binding domain Zα of dsRNA adenosine deaminase type I reveals similarity to the (α + β) family of helix–turn–helix proteins

A. Rich, K. Lowenhaupt, M. Schade, 1999, The EMBO journal.

Fragment-Based Discovery of Novel Potent Sepiapterin Reductase Inhibitors.

M. Wagener, F. Christian, G. Bahrenberg, 2019, Journal of medicinal chemistry.

Highly selective sub-nanomolar cathepsin S inhibitors by merging fragment binders with covalent nitrile inhibitors.

M. Wagener, Katrien Pletinckx, M. Schade, 2020, Journal of medicinal chemistry.

The Zalpha domain from human ADAR1 binds to the Z-DNA conformer of many different sequences.

A. Rich, Y. Lyubchenko, K. Lowenhaupt, 1998, Nucleic acids research.

NMR fragment screening: tackling protein-protein interaction targets.

Markus Schade, Hartmut Oschkinat, H. Oschkinat, 2005, Current opinion in drug discovery & development.

The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro.

P. Schmieder, A. Rich, K. Lowenhaupt, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Novel Disease Targets Are the Life-blood of the Biotech and Pharmaceutical Industries. However, of Equal Fragment Screening: Biochemical Assays versus Nmr

T. Hesterkamp, M. Schade, 2007 .