Markus G. Grütter
Novartis
53 Papers
666 Citations
Markus G. Grütter is an academic researcher from Novartis. The author has contributed to research in topics: Recombinant DNA & Protein structure. The author has an hindex of 24, co-authored 53 publications.
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Papers
Refined crystal structures of subtilisin Novo in complex with wild-type and two mutant eglins: Comparison with other serine proteinase inhibitor complexes
TL;DR: The crystal structures of the complexes formed between subtilisin Novo and three inhibitors, eglin c, Arg45-eglin c and Lys53-eglins c have been determined using molecular replacement and difference Fourier techniques and refined at 2.4 A, 2.1 A, and 2.2 A resolution.
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A new structural class of serine protease inhibitors revealed by the structure of the hirustasin–kallikrein complex
Peer R. E. Mittl,Stefania Di Marco,Gabriele Fendrich,Gabriele Pohlig,Jutta Heim,Christian P. Sommerhoff,Hans Fritz,John P. Priestle,Markus G. Grütter +8 more
TL;DR: It is revealed that hirustasin differs from other serine protease inhibitors in its conformation and its disulfide bond connectivity, making it the prototype for a new class of inhibitor.
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Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP 53820, a novel pseudosymmetric inhibitor.
John P. Priestle,Alexander Fassler,Johannes Dr. Rösel,Marina Tintelnot-Blomley,P Strop,Markus G. Grütter +5 more
TL;DR: X-ray crystal structures of both HIV-1 and HIV-2 proteases each in complex with the pseudosymmetric inhibitor, CGP 53820, confirmed earlier modeling studies and revealed minor sequence changes in subsites at the active site can explain some of the observed differences in substrate and inhibitor binding.
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Three-Dimensional Models of ACE and NEP Inhibitors and Their Use in the Design of Potent Dual ACE/NEP Inhibitors
TL;DR: A composite template for angiotensin converting enzyme and a hypothetical model of the active site of neutral endopeptidase have been constructed and used to guide the design of dual ACE/NEP inhibitors.
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•Journal Article
Synovial type (group II) phospholipase A2 in cartilage.
TL;DR: The results show that syn-PLA2 is present both in articular and extraarticular cartilage and support the view that PLA2 found in SF might originate from chondrocytes, and not from synovial lining or inflammatory cells.
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