W. Bode

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The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors

R. Huber, J. Deisenhofer, M. Marquart, 1983 .

Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution.

J Deisenhofer, R. Huber, J. Deisenhofer, 1974, Journal of molecular biology.

The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry.

W. Bode, E. Papamokos, D. Musil, 1987, European journal of biochemistry.

Natural protein proteinase inhibitors and their interaction with proteinases.

R. Huber, W. Bode, R. Huber, 1992, European journal of biochemistry.

Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding.

R. Huber, W. Bode, R. Engh, 1999, Structure.

Divining the serpin inhibition mechanism: a suicide substrate 'springe'?

R. Huber, W. Bode, R. Engh, 1995, Trends in biotechnology.

Structural basis of the endoproteinase-protein inhibitor interaction.

R. Huber, W. Bode, R. Huber, 2000, Biochimica et biophysica acta.

The thrombin E192Q–BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin

R. Huber, W. Bode, C. Esmon, 1997, The EMBO journal.

Coagulation factors and their inhibitors.

W. Bode, M. Stubbs, 1994, Current opinion in structural biology.

Structural basis of the activation and action of trypsin

R. Huber, W. Bode, 1978 .

Crystal structure of the apoptosis-inducing human granzyme A dimer

W. Bode, D. Jenne, E. Estébanez-Perpiñá, 2003, Nature Structural Biology.

The interaction of thrombin with fibrinogen. A structural basis for its specificity.

H Oschkinat, R. Huber, W. Bode, 1992, European journal of biochemistry.

Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors.

W. Bode, E. Meyer, J. Powers, 1989, Biochemistry.

The interaction of thrombin with fibrinogen. A structural basis for its specificity.

R. Huber, W. Bode, H. Oschkinat, 1992 .

Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme.

R. Huber, B. Castner, R. Paxton, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Electrostatic interactions in proteins: Calculations of the electrostatic term of free energy and the electrostatic potential field

W. Bode, B. Atanasov, W. Bode, 1989, European Biophysics Journal.

Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

R. Huber, K. Brew, W. Bode, 1997, Nature.

Mechanism of inhibition of papain by chicken egg white cystatin

J. Kos, W. Bode, V. Turk, 1989, FEBS letters.

Enzyme flexibility, solvent and 'weak' interactions characterize thrombin-ligand interactions: implications for drug design.

H Brandstetter, R. Huber, U. Baumann, 1996, Structure.

Geometry of binding of the benzamidine- and arginine-based inhibitors Nα-(2-naphthyl-sulphonyl-glycyl)-dl-p-amidinophenylalanyl-piperidine (NAPAP) and (2R,4R)-4-methyl-1-[Nα-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulphonyl)-l-arginyl]-2-piperidine carboxylic acid (MQPA) to human α-thrombin

D. Turk, W. Bode, J. Stürzebecher, 1990 .

Design and evaluation of novel bivalent thrombin inhibitors based on amidinophenylalanines.

W. Bode, M. Renatus, J. Stürzebecher, 1999, European journal of biochemistry.

Structural and functional analyses of benzamidine-based inhibitors in complex with trypsin: implications for the inhibition of factor Xa, tPA, and urokinase.

R. Huber, W. Bode, M. Renatus, 1998, Journal of medicinal chemistry.

Crystal structures of factor Xa specific inhibitors in complex with trypsin: structural grounds for inhibition of factor Xa and selectivity against thrombin

R. Huber, W. Bode, M. Stubbs, 1995, FEBS letters.

The X-ray crystal structure of thrombin in complex with N alpha-2-naphthylsulfonyl-L-3-amidino-phenylalanyl-4-methylpiperidide: the beneficial effect of filling out an empty cavity.

H Brandstetter, W. Bode, H. Brandstetter, 1995, Journal of enzyme inhibition.

Crystal structures of thrombin and thrombin complexes as a framework for antithrombotic drug design

W. Bode, M. Stubbs, Wolfram Bode, 1994 .

X-ray crystal structures of thrombin in complex with D-Phe-Pro-Arg and with small benzamidine- and arginine-based "non-peptidic" inhibitors.

W. Bode, 1993, Advances in experimental medicine and biology.

The refined crystal structure of bovine β-trypsin at 1·8 Å resolution

W. Bode, W. Bode, H. Fehlhammer, 1975 .

Crystal structure analysis and refinement of two variants of trigonal trypsinogen

R. Huber, W. Bode, R. Huber, 1978, FEBS letters.

The refined 2.2-A (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor.

R. Huber, J. Walter, W. Bode, 1984, European journal of biochemistry.

The structure of a complex of recombinant hirudin and human alpha-thrombin.

R. Huber, W. Bode, A. Tulinsky, 1990, Science.

On the disordered activation domain in trypsinogen: chemical labelling and low‐temperature crystallography

Robert Huber, R. Huber, J. Walter, 1982 .

Secondary amides of sulfonylated 3-amidinophenylalanine. New potent and selective inhibitors of matriptase.

W. Bode, Oliver Schuster, J. Stürzebecher, 2006, Journal of medicinal chemistry.

Tachylectin‐2: crystal structure of a specific GlcNAc/GalNAc‐binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus

R. Huber, W. Bode, S. Kawabata, 1999, The EMBO journal.

Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1 and 2.5 A resolution. A common principle of phycobilin-protein interaction.

R. Huber, W. Bode, Tilman Schirmer, 1987, Journal of molecular biology.

MPSA short communications

W. E. Moddeman, J. A. Lindquist, D. N. Perkins, 1988 .

The 2.5 A X‐ray crystal structure of the acid‐stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha‐chymotrypsin.

R. Huber, W. Bode, M. Grütter, 1988, The EMBO journal.

Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibit

W. Bode, W Bode, Z Chen, 1983, Journal of molecular biology.

X-ray Structure of Human proMMP-1

W. Bode, G. Bourenkov, R. Visse, 2005, Journal of Biological Chemistry.

The X-ray structures of porcine pancreatic kallikrein and of its complex with bovine pancreatic trypsin inhibitor.

W. Bode, Z. Chen, 1983, Advances in experimental medicine and biology.

The clot thickens: clues provided by thrombin structure.

W. Bode, M. Stubbs, Wolfram Bode, 1995, Trends in biochemical sciences.

Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).

J. Fox, W. Bode, E. Meyer, 1995, Proceedings of the National Academy of Sciences of the United States of America.

The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain.

C. López-Otín, W. Bode, U. Gohlke, 1996, Journal of molecular biology.

The C‐terminal (haemopexin‐like) domain structure of human gelatinase A (MMP2): structural implications for its function

W. Bode, U. Gohlke, G. Murphy, 1996, FEBS letters.

Comparative Analysis of Haemostatic Proteinases: Structural Aspects of Thrombin, Factor Xa, Factor IXa and Protein C

W. Bode, H. Brandstetter, M. Stubbs, 1997, Thrombosis and Haemostasis.

The human mast cell tryptase tetramer: a fascinating riddle solved by structure.

W. Bode, A. Bergner, C. Sommerhoff, 2000, Biochimica et biophysica acta.

Catalytic domain structure of vampire bat plasminogen activator: a molecular paradigm for proteolysis without activation cleavage.

R. Huber, W. Bode, M. Renatus, 1997, Biochemistry.

The crystal structure of the proprotein processing proteinase furin explains its stringent specificity

R. Huber, I. Lindberg, W. Bode, 2003, Nature Structural Biology.

Tissue-type plasminogen activator: variants and crystal/solution structures demarcate structural determinants of function.

W. Bode, M. Renatus, 1997, Current opinion in structural biology.

Electrostatic Properties of Thrombin: Importance for Structural Stabilization and Ligand Binding

W. Bode, A. Karshikov, 1993, Seminars in thrombosis and hemostasis.

Specificity Profiling of Seven Human Tissue Kallikreins Reveals Individual Subsite Preferences*

C. Craik, W. Bode, V. Magdolen, 2006, Journal of Biological Chemistry.

The 2.2 .ANG. resolution x-ray crystal structure of the complex of trypsin inhibited by 4-chloro-3-ethoxy-7-guanidinoisocoumarin: a proposed model of the thrombin-inhibitor complex

W. Bode, E. Meyer, R. Radhakrishnan, 1990 .

Complex structure of human thrombin with N-methyl-arginine inhibitor

W. Bode, T. Steinmetzer, R. Friedrich, 2002 .

Structure and interaction modes of thrombin.

W. Bode, Wolfram Bode, 2006, Blood cells, molecules & diseases.

Characterization of the residues involved in the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor.

R. Huber, W. Bode, P. Fuentes-Prior, 2002, Biochemistry.

Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation

R. Huber, W. Bode, S. Kawabata, 2003, Nature.

The staphylocoagulase family of zymogen activator and adhesion proteins

W. Bode, P. Panizzi, P. Fuentes-Prior, 2004, Cellular and Molecular Life Sciences CMLS.

Fibrinogen Substrate Recognition by Staphylocoagulase·(Pro)thrombin Complexes*

W. Bode, P. Panizzi, K. Richter, 2006, Journal of Biological Chemistry.

Structural Basis for Reduced Staphylocoagulase-mediated Bovine Prothrombin Activation*

W. Bode, S. Kawabata, P. Panizzi, 2006, Journal of Biological Chemistry.

Bivalent inhibition of human beta-tryptase.

W. Bode, L. Moroder, A. Bergner, 2001, Chemistry & biology.

Bivalent inhibition of human β-tryptase

W. Bode, L. Moroder, A. Bergner, 2001 .

Low‐temperature protein crystallography. Effect on flexibility, temperature factor, mosaic spread, extinction and diffuse scattering in two examples: bovine trypsinogen and Fc fragment

R. Huber, W. Bode, T. P. Singh, 1980 .

Structure and Biology of the Globular Domain of Basement Membrane Type IV Collagen a

R. Timpl, W. Bode, J. Engel, 1985, Annals of the New York Academy of Sciences.

Horseshoe Grab Coagulogen Is an Invertebrate Protein with a Nerve Growth Factor-Like Domain

R. Delotto, W. Bode, A. Bergner, 1997, Biological chemistry.

Inflammation: the protein C pathway

W. Bode, C. Esmon, K. Fukudome, 1997 .

Structure and specificity in coagulation and its inhibition.

W. Bode, M. Stubbs, 1995, Trends in cardiovascular medicine.

Determination of the protein content of crystals formed by Mastigocladus laminosus C-phycocyanin, Chroomonas spec. phycocyanin-645 and modified human fibrinogen using an improved Ficoll density gradient method.

W. Bode, Tilman Schirmer, 1985, Biological chemistry Hoppe-Seyler.

The covalent structure of the elastase inhibitor from Anemonia sulcata--a "non-classical" Kazal-type protein.

W. Bode, H. Tschesche, H. Kolkenbrock, 1987, Biological chemistry Hoppe-Seyler.

The 1.8 A crystal structure of human cathepsin G in complex with Suc‐Val‐Pro‐PheP‐(OPh)2: a Janus‐faced proteinase with two opposite specificities.

R. Huber, W. Bode, J. Potempa, 1996, The EMBO journal.

Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.

R. Huber, W. Bode, S. Macedo-Ribeiro, 1998, Nature.

Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A.

R. Huber, W. Bode, H. Zuber, 1990, Journal of molecular biology.

Crystallization of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus and preliminary characterization of two crystal forms.

W. Bode, H. Zuber, R. Rümbeli, 1985, Journal of molecular biology.

The structure of γ‐N‐methylasparagine in C‐phycocyanin from Mastigocladus laminosus and Agmenellum quadruplicatum

R. Huber, W. Bode, M. Duerring, 1988 .

Crystallization and preliminary x-ray diffraction data of the cryptomonad biliprotein phycocyanin-645 from a Chroomonas spec.

W. Bode, W. Wehrmeyer, Tilman Schirmer, 1984, Archives of Microbiology.

Pore-forming scissors? A first structural glimpse of gamma-secretase.

W. Bode, C. Haass, M. Than, 2006, Trends in biochemical sciences.

Properties of purified gut trypsin from Helicoverpa zea, adapted to proteinase inhibitors.

W. Bode, J. Cordewener, M. Jongsma, 2002, European journal of biochemistry.

Thrombin as a multifunctional protein: induction of cell adhesion and proliferation.

M. Benezra, W. Bode, R. Bar-Shavit, 1992, American journal of respiratory cell and molecular biology.

A helping hand for collagenases: the haemopexin-like domain.

W. Bode, Wolfram Bode, 1995, Structure.

First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases.

W. Bode, F. Gomis‐Rüth, L. F. Kress, 1993, The EMBO journal.

Synthesis of a (desSer1 Ile29 Leu89) chicken cystatin gene, expression in E. coli as fusion protein and its isolation

J. Kos, W. Bode, E. Auerswald, 1989, FEBS letters.

HUMAN CATHEPSIN G

W. Bode, J. Potempa, A. Banbula, 1997 .

Increase in gelatinase-specificity of matrix metalloproteinase inhibitors correlates with antimetastatic efficacy in a T-cell lymphoma model.

A. Krüger, R. Khokha, H. Krell, 2002, Cancer research.

Changing Residue 338 in Human Factor IX from Arginine to Alanine Causes an Increase in Catalytic Activity*

W. Bode, H. Brandstetter, Jianping Jin, 1998, The Journal of Biological Chemistry.

The crystal structure of the proprotein processing proteinase furin explains its stringent specificity

Robert Huber, Angus Cameron, R. Huber, 2003, Nature Structural Biology.

The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain

D. Svergun, W. Bode, D. Franke, 2010, The Journal of Biological Chemistry.

Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain.

K. Suzuki, W. Bode, G. Bourenkov, 2000, Acta Crystallographica Section D: Biological Crystallography.

Crystallization and preliminary X‐ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H‐D‐Phe‐Phe‐Arg‐chloromethylketone

W. Bode, J. Potempa, J. Travis, 1998, Protein science : a publication of the Protein Society.

Crystals of the NC1 domain of human type IV collagen.

R. Huber, W. Bode, M. Stubbs, 1990, Journal of molecular biology.

Crystallization and preliminary X‐ray diffraction data of proteinase II from Crotalus adamanteus (Eastern Diamond Rattlesnake)

W. Bode, L. F. Kress, 1983 .

The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. I. Crystallization, data collection and application of patterson search technique.

W. Bode, H. Fehlhammer, 1975, Journal of molecular biology.

Heterotrimeric collagen peptides as substrates of metalloproteinases

W. Bode, L. Moroder, J. Ottl, 2002 .

Synthesis of disulfide-bridged heterotrimeric collagen peptides. Conformational properties and digestion by matrix metalloproteinases

W. Bode, L. Moroder, J. Ottl, 1999 .

Handbook of metalloproteins

R. Huber, K. Wieghardt, W. Bode, 2006 .

Novel Fluorescent Prothrombin Analogs as Probes of Staphylocoagulase-Prothrombin Interactions*

W. Bode, P. Panizzi, P. Fuentes-Prior, 2006, Journal of Biological Chemistry.

Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution.

R. Huber, W. Bode, J. Potempa, 1998, Structure.

The structure of the human betaII-tryptase tetramer: fo(u)r better or worse.

W. Bode, M. Stubbs, A. Bergner, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Interplay of human tissue kallikrein 4 (hK4) with the plasminogen activation system: hK4 regulates the structure and functions of the urokinase-type plasminogen activator receptor (uPAR)

W. Bode, M. Schmitt, V. Magdolen, 2006, Biological chemistry.

Induction of the bovine trypsinogen—trypsin transition by peptides sequentially similar to the N‐terminus of trypsin

R. Huber, W. Bode, 1976, FEBS letters.

X-ray crystallographic and biochemical characterization of single crystals formed by proteolytically modified human fibrinogen.

W. Bode, R. Gollwitzer, 1986, European journal of biochemistry.

4 Human Cysteine Proteinases and Their Inhibitors, Stefins and Cystatins

W. Bode, V. Turk, 1994 .

Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin.

R. Huber, W. Bode, J. Kellermann, 1994, Journal of molecular biology.

Structural basis of matrix metalloproteinase function.

W. Bode, 2003, Biochemical Society symposium.

Structural Studies on MMPs andTIMPs Wolfram Bode and Klaus Maskos

W. Bode, K. Maskos, 2001 .

Refined 2.3 A X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics.

H Brandstetter, D. Turk, W. Bode, 1992, Journal of molecular biology.

A Model for the Specificity of Fibrinogen Cleavage by Thrombin

W. Bode, M. Stubbs, 1993, Seminars in thrombosis and hemostasis.

The ternary microplasmin–staphylokinase–microplasmin complex is a proteinase–cofactor–substrate complex in action

R. Huber, W. Bode, A. Bergner, 1998, Nature Structural Biology.

The refined 1.9‐Å X‐ray crystal structure of d‐Phe‐Pro‐Arg chloromethylketone‐inhibited human α‐thrombin: Structure analysis, overall structure, electrostatic properties, detailed active‐site geometry, and structure‐function relationships

D. Turk, W. Bode, W Bode, 1992, Protein science : a publication of the Protein Society.

Converting blood coagulation factor IXa into factor Xa: dramatic increase in amidolytic activity identifies important active site determinants

W. Bode, R. Engh, H. Brandstetter, 1997, The EMBO journal.

Thrombin inhibitors identified by computer-assisted multiparameter design.

Andreas Schwienhorst, Michael Gebinoga, Martin Wiesenfeldt, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Dramatic enhancement of the catalytic activity of coagulation factor IXa by alcohols

W. Bode, K. Hopfner, E. Kopetzki, 1997, FEBS letters.

X-ray Structure of Active Site-inhibited Clotting Factor Xa

Robert Huber, Richard A. Engh, R. Huber, 1996, The Journal of Biological Chemistry.

X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B.

H Brandstetter, R. Huber, W. Bode, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Structure of a novel thrombin inhibitor with an uncharged D-amino acid as P1 residue.

W. Bode, D. Riester, A. Schwienhorst, 2008, European journal of medicinal chemistry.

Design of benzamidine-type inhibitors of factor Xa.

W. Bode, M. Stubbs, L. Moroder, 1998, Journal of medicinal chemistry.

Lysine 156 promotes the anomalous proenzyme activity of tPA: X‐ray crystal structure of single‐chain human tPA

R. Huber, Stefan Fischer, W. Bode, 1997, The EMBO journal.

The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution.

R. Huber, W. Bode, P. Schwager, 1978, Journal of molecular biology.

Correlation of Amino Acid Sequence with Inhibitor Activity and Specificity of Protein Inhibitors of Serine Proteinases

R. Huber, W. Ardelt, I. Kato, 1981 .

The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen.

W. Bode, W Bode, Wolfram Bode, 1979, Journal of molecular biology.

Proteinase inhibitors from the European medicinal leech Hirudo medicinalis: structural, functional and biomedical aspects.

M. Bolognesi, W. Bode, M. Coletta, 1995, Molecular aspects of medicine.

The refined 1.9 A crystal structure of human alpha‐thrombin: interaction with D‐Phe‐Pro‐Arg chloromethylketone and significance of the Tyr‐Pro‐Pro‐Trp insertion segment.

R. Huber, U. Baumann, J. Hofsteenge, 1989, The EMBO journal.

X-ray Structure of Human proMMP-1 NEW INSIGHTS INTO PROCOLLAGENASE ACTIVATION AND COLLAGEN BINDING*

W. Bode, G. Bourenkov, R. Visse, 2005 .

Multiple Conformations of Cystatin, Mung Bean Inhibitor, and Serpins

R. Huber, W. Bode, R. Engh, 1994 .

The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin.

R. Huber, G. Lin, W. Bode, 1993, European journal of biochemistry.

The refined 2.3 Å crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor

W. Bode, I. Mayr, Wei An-zhi, 1988, FEBS letters.

Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases

R. Huber, W. Bode, F. Gomis-Rüth, 1992, Nature.

The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

P. Reinemer, U. Baumann, W. Bode, 1995, Protein science : a publication of the Protein Society.

Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’

W. Bode, W Bode, F X Gomis-Rüth, 1993, FEBS letters.

A player of many parts: the spotlight falls on thrombin's structure.

W. Bode, M. Stubbs, 1993, Thrombosis research.

Inflammation, sepsis, and coagulation.

W. Bode, C. Esmon, K. Fukudome, 1999, Haematologica.

The 2.8 A crystal structure of Gla‐domainless activated protein C.

S Foundling, R. Huber, S. Foundling, 1996, The EMBO journal.

Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin.

R. Huber, W. Bode, W Bode, 1977, Journal of molecular biology.

Expression of the glyceraldehyde‐3‐phosphate dehydrogenase gene from the extremely thermophilic archaebacterium Methanothermus fervidus in E. coli

W. Bode, R. Hensel, S. Fabry, 1988, FEBS letters.

The refined 2.0 Å X‐ray crystal structure of the complex formed between bovine β‐trypsin and CMTI‐I, a trypsin inhibitor from squash seeds (Cucurbita maxima) Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes

J Otlewski, R. Huber, J. Otlewski, 1989, FEBS letters.

X‐ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor.

R. Huber, W. Bode, S. Neumann, 1986, The EMBO journal.

Structural basis of the zinc inhibition of human tissue kallikrein 5.

R. Huber, W. Bode, V. Magdolen, 2007, Journal of molecular biology.

Structure of astacin with a transition-state analogue inhibitor

W. Bode, V. Dive, I. Yiallouros, 1996, Nature Structural Biology.

The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis Structural analysis, subtilisin structure and interface geometry

Djordje Musil, W. Bode, E. Papamokos, 1987 .

Refined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin.

W. Bode, K. Bartels, W Bode, 1983, Journal of molecular biology.

Macrocyclic Statine‐Based Inhibitors of BACE‐1

P. Reinemer, C. Renner, W. Bode, 2007, Chembiochem : a European journal of chemical biology.

Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors.

À. Bayés, W. Bode, F. Avilés, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Primary structure of human neutrophil elastase.

W. Bode, J. Travis, S. Sinha, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor.

W. Bode, P. Huxley, H. Tschesche, 1995, Biochemistry.

cystatins: protein inhibitors of cysteine proteinases

W. Bode, V. Turk, Wolfram Bode, 2001 .

Structural Mapping of the Active Site Specificity Determinants of Human Tissue-type Plasminogen Activator

R. Huber, Stefan Fischer, W. Bode, 1997, The Journal of Biological Chemistry.

Specific inhibition of insect α-amylases: yellow meal worm α-amylase in complex with the Amaranth α-amylase inhibitor at 2.0 Å resolution

R. Huber, S. Pongor, W. Bode, 1999 .

Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor.

R. Huber, D. Typke, W. Bode, 1996, The EMBO journal.

X-ray crystallographic structure of the light-harvesting biliprotein C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus and its resemblance to globin structures.

R. Huber, W. Bode, H. Zuber, 1985, Journal of molecular biology.

Structure of malonic acid‐based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data

R. Huber, W. Bode, R. Engh, 1998, Protein science : a publication of the Protein Society.

An active zymogen: unravelling the mystery of tissue-type plasminogen activator.

W. Bode, M. Renatus, M. Stubbs, 1998, Biological chemistry.

Structural properties of matrix metalloproteinases

W. Bode, K. Maskos, H. Tschesche, 1999, Cellular and Molecular Life Sciences CMLS.

The primary structure of bdellin B-3 from the leech Hirudo medicinalis. Bdellin B-3 is a compact proteinase inhibitor of a "non-classical" Kazal type. It is present in the leech in a high molecular mass form.

W. Bode, M. Eulitz, W. Machleidt, 1986, Biological chemistry Hoppe-Seyler.

LASER DIFFRACTION OF ORIENTED FIBRINOGEN MOLECULES *

D. Typke, W. Bode, R. Guckenberger, 1983, Annals of the New York Academy of Sciences.

On the aggregation of fibrinogen molecules.

W. Bode, R. Gollwitzer, H. Karges, 1983, Thrombosis research.

The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium.

R. Huber, K. Suzuki, W. Bode, 2000, Proceedings of the National Academy of Sciences of the United States of America.

The X-ray crystal structure analysis of the refined complex formed by bovine trypsin and p-amidinophenylpyruvate at 1.4 A resolution.

J. Walter, W. Bode, 1983, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

Structural aspects of serpin inhibition

W. Bode, R. Engh, A. Schulze, 1994, FEBS letters.

The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3).

R. Huber, W. Ardelt, M. Laskowski, 1985, European journal of biochemistry.

Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases.

R. Huber, I. Kato, M. Laskowski, 1982, Journal of molecular biology.

Crystallization, crystal structure analysis and molecular model of the third domain of Japanese quail ovomucoid, a Kazal type inhibitor.

R. Huber, I. Kato, M. Laskowski, 1981, Journal of molecular biology.

Crystal structure analysis and refinement at 2.5 A of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum. The molecular model and its implications for light-harvesting.

R. Huber, W. Bode, M. Miller, 1986, Journal of molecular biology.

X-Ray Crystal Structures of Human α-Thrombin and of the Human Thrombin-Hirudin Complex

R. Huber, W. Bode, A. Tulinsky, 1992 .

The cysteine proteinase inhibitor chicken cystatin is a phosphoprotein

J. Kos, W. Bode, V. Turk, 1989, FEBS letters.

Crystals of urokinase type plasminogen activator complexes reveal the binding mode of peptidomimetic inhibitors.

W. Bode, U. Jacob, E. Żesławska, 2003, Journal of molecular biology.

Inhibition of Furin by Polyarginine-containing Peptides

I. Lindberg, R. Houghten, W. Bode, 2004, Journal of Biological Chemistry.

(4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase.

R. Huber, W. Bode, V. Magdolen, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Refined structure of the hirudin-thrombin complex.

R. Huber, W. Bode, A. Tulinsky, 1991, Journal of molecular biology.

Structural basis for the anticoagulant activity of the thrombin–thrombomodulin complex

Robert Huber, R. Huber, W. Bode, 2000, Nature.

Physiological fIXa Activation Involves a Cooperative Conformational Rearrangement of the 99-Loop*

R. Huber, W. Bode, H. Brandstetter, 2003, The Journal of Biological Chemistry.

Crystal structures of uninhibited factor VIIa link its cofactor and substrate-assisted activation to specific interactions.

R. Huber, D. Banner, A. D'arcy, 2002, Journal of molecular biology.

Structure of human des(1-45) factor Xa at 2.2 A resolution.

R. Huber, W. Kisiel, W. Bode, 1993, Journal of molecular biology.

Calorimetric studies on thein vitro polymerization ofPr. mirabilis flagellin

W. Bode, R. Jaenicke, A. Blume, 1974, Biophysics of structure and mechanism.

The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism

Robert Huber, Hans-Ulrich Demuth, Ulrich Heiser, 2003, Proceedings of the National Academy of Sciences of the United States of America.

ACTIVATION, ACTION AND INHIBITION OF TRYPSIN AS DEDUCED FROM THE THREEDIMENSIONAL STRUCTURES OF TRYPSINOGEN, TRYPSIN AND THEIR COMPLEXES WITH THE BASIC PANCREATIC TRYPSIN INHIBITOR

R. Huber, W. Bode, 1978 .

STRUCTURAL STUDIES ON THE PANCREATIC TRYPSIN INHIBITOR – TRYPSIN COMPLEX AND ITS FREE COMPONENTS: STRUCTURE AND FUNCTION RELATIONSHIP IN SERINE PROTEASE INHIBITION AND CATALYSIS

R. Huber, W. Bode, P. Schwager, 1976 .

The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0.

W. Bode, P. Schwager, W Bode, 1975, Journal of molecular biology.

Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family

W. Bode, A. Romero, J. Garcia, 1998, The EMBO journal.

The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases.

R. Huber, W. Bode, U. Jacob, 1998, Structure.

Identification of functionally important amino acid residues within the C2-domain of human factor V using alanine-scanning mutagenesis.

W. Bode, S. Macedo-Ribeiro, W. Kane, 2000, Biochemistry.

Activation of snake venom metalloproteinases by a cysteine switch‐like mechanism

R. Huber, W. Bode, L. Moroder, 1993, FEBS letters.

Nuclear magnetic resonance solution and X-ray structures of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop.

R. Huber, T. Holak, J. Otlewski, 1989, Journal of molecular biology.

Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.

W. Bode, E. Papamokos, D. Musil, 1986, The EMBO journal.

Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases

W. Bode, K. Maskos, Wolfram Bode, 2003, Molecular biotechnology.

Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI.

R. Huber, P. Colman, W. Bode, 1974, European journal of biochemistry.

The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase.

R. Huber, B. Dunn, W. Bode, 2002, Structure.

Proteinase-protein inhibitor interaction.

R. Huber, W. Bode, 1991, Biomedica biochimica acta.

The refined 2.4 A X‐ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.

R. Huber, W. Bode, B. Lenarčič, 1990, The EMBO journal.

Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site.

R. Huber, W. Bode, V. Magdolen, 2006, Journal of molecular biology.

Structural determinants of the ADAM inhibition by TIMP-3: crystal structure of the TACE-N-TIMP-3 complex.

R. Black, W. Bode, P. Goettig, 2008, Journal of molecular biology.

Crystal structure of the TACE-N-TIMP-3 complex

R. Black, W. Bode, P. Goettig, 2008 .

Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution.

R. Huber, U. Baumann, W. Bode, 1992, Journal of molecular biology.

Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins.

R. Huber, U. Baumann, W. Bode, 1991, Journal of molecular biology.

Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors.

R. Huber, D. Turk, W. Bode, 1995, Biochemistry.

The 2.0 A X‐ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.

W. Bode, R. Huber, J. Kos, 1988, The EMBO journal.

The single calcium‐binding site of crystalline bovine β‐trypsin

W. Bode, P. Schwager, 1975 .

Human β-tryptase is a ring-like tetramer with active sites facing a central pore

R. Huber, W. Bode, S. Macedo-Ribeiro, 1998, Nature.

Endoproteinase‐protein inhibitor interactions

W. Bode, K. Maskos, H. Nagase, 1999, APMIS : acta pathologica, microbiologica, et immunologica Scandinavica.

The influence of residue 190 in the S1 site of trypsin‐like serine proteases on substrate selectivity is universally conserved

R. Huber, W. Bode, H. Brandstetter, 2002, FEBS letters.

The Three-dimensional Structure of Recombinant Leech-derived Tryptase Inhibitor in Complex with Trypsin

R. Huber, W. Bode, E. Auerswald, 1997, The Journal of Biological Chemistry.

Fine Mapping of Inhibitory Anti-factor V Antibodies Using Factor V C2 Domain Mutants

T. Ortel, W. Bode, S. Macedo-Ribeiro, 2001, Thrombosis and Haemostasis.

Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin.

W. Bode, R. Huber, W. Bode, 1995, The EMBO journal.

The NC1 dimer of human placental basement membrane collagen IV: does a covalent crosslink exist?

W. Bode, G. Bourenkov, M. Than, 2005, Biological chemistry.

(R)-3-Amidinophenylalanine-Derived Inhibitors of Factor Xa with a Novel Active-Site Binding Mode

Luis Moroder, W. Bode, S. Sperl, 2002, Biological chemistry.

Flexibility Analysis and Structure Comparison of Two Crystal Forms of Calcium-Free Human m-Calpain

W. Bode, D. Reverter, H. Sorimachi, 2002, Biological chemistry.

Crystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera.

R. Huber, À. Bayés, W. Bode, 2001, Journal of molecular biology.

Urethanyl-3-Amidinophenylalanine Derivatives as Inhibitors of Factor Xa. X-Ray Crystal Structure of a Trypsin/Inhibitor Complex and Modeling Studies

W. Bode, V. Magdolen, A. Bergner, 2000, Biological chemistry.

The structure of thrombin: a janus-headed proteinase.

W. Bode, 2006, Seminars in thrombosis and hemostasis.

Crystal structure of gingipain R: an Arg‐specific bacterial cysteine proteinase with a caspase‐like fold

R. Huber, W. Bode, U. Jacob, 1999, The EMBO journal.

Electrostatic interactions in the association of proteins: An analysis of the thrombin–hirudin complex

W. Bode, A. Tulinsky, S. Stone, 1992, Protein science : a publication of the Protein Society.

Rigidity and flexibility of dipeptidyl peptidase IV: crystal structures of and docking experiments with DPIV.

R. Huber, T. Hoffmann, W. Bode, 2006, Journal of molecular biology.

Crystal structures of MMP-9 complexes with five inhibitors: contribution of the flexible Arg424 side-chain to selectivity.

Robert Huber, R. Huber, W. Bode, 2007, Journal of molecular biology.

Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides.

R. Huber, W. Bode, V. Dive, 2002, Structure.

New enzyme lineages by subdomain shuffling.

R. Huber, W. Bode, R. Engh, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Catalytic Domain Structures of MT-SP1/Matriptase, a Matrix-degrading Transmembrane Serine Proteinase*

Robert Huber, R. Huber, W. Bode, 2002, The Journal of Biological Chemistry.

Recognition and catabolism of synthetic heterotrimeric collagen peptides by matrix metalloproteinases.

Y. Tominaga, W. Bode, M. Kröger, 2000, Chemistry & biology.

Structural Basis for Possible Calcium-Induced Activation Mechanisms of Calpains

K. Suzuki, W. Bode, D. Reverter, 2001, Biological chemistry.

The 2.2-Å Crystal Structure of Human Pro-granzyme K Reveals a Rigid Zymogen with Unusual Features*

W. Bode, D. Jenne, P. Fuentes-Prior, 2002, The Journal of Biological Chemistry.

Crystal Structure of the Caspase Activator Human Granzyme B, a Proteinase Highly Specific for an Asp-P1 Residue

R. Huber, W. Bode, R. Kiefersauer, 2000, Biological chemistry.

The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa.

R. Huber, P. Grootenhuis, W. Bode, 1997, Journal of molecular biology.

Identification of a β-Secretase Activity, Which Truncates Amyloid β-Peptide after Its Presenilin-dependent Generation*

G. Westmeyer, G. Multhaup, W. Bode, 2003, The Journal of Biological Chemistry.

1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile.

W. Bode, F. Gomis-Rüth, P. Huxley, 1997, European journal of biochemistry.

Structural basis for the activation of human procaspase-7

G. Salvesen, W. Bode, M. Renatus, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Crystal structure of the thrombin‐hirudin complex: a novel mode of serine protease inhibition.

W. Bode, J. Hofsteenge, W. Bode, 1990, The EMBO journal.

The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity.

R. Huber, W. Bode, S. Strobl, 1999, Journal of molecular biology.

Structural features of a superfamily of zinc-endopeptidases: the metzincins.

W. Bode, W. Stöcker, 1995, Current opinion in structural biology.

The crystal structure of adamalysin II, a zinc-endopeptidase from the snake venom of the eastern diamondback rattlesnake Crotalus adamanteus.

W. Bode, E. Meyer, F. Gomis-Rüth, 1994, Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas.

Crystal structure of the complex formed by the membrane type 1‐matrix metalloproteinase with the tissue inhibitor of metalloproteinases‐2, the soluble progelatinase A receptor

J. Calvete, D. Turk, W. Bode, 1998, The EMBO journal.

Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug.

R. Huber, W. Bode, W. Schleuning, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The metzincin-superfamily of zinc-peptidases.

P. Reinemer, U. Baumann, W. Bode, 1996, Advances in experimental medicine and biology.

Structural Basis of the Matrix Metalloproteinases and Their Physiological Inhibitors, the Tissue Inhibitors of Metalloproteinases

W. Bode, K. Maskos, K. Maskos, 2003, Biological chemistry.

Crystallographic Evidence That the F2 Kringle Catalytic Domain Linker of Prothrombin Does Not Cover the Fibrinogen Recognition Exosite (*)

W. Bode, M. Stubbs, M. Bauer, 1996, The Journal of Biological Chemistry.

Human b-tryptase isa ring-like tetramerwithactive sites facingacentral pore

R. Huber, W. Bode, S. Macedo-Ribeiro, 2022 .

Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2

Francesc X. Avilés, Robert Huber, Josep Vendrell, 2000, Nature Structural Biology.

Refined X-ray crystal structures of the reactive site modified ovomucoid inhibitor third domains from silver pheasant (OMSVP3*) and from Japanese quail (OMJPQ3*).

R. Huber, W. Ardelt, T. Lin, 1991, Journal of molecular biology.

The 1.9-Å crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link

Robert Huber, Hans D. Bartunik, R. Huber, 2002, Proceedings of the National Academy of Sciences of the United States of America.

The 2.0-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems

R. Huber, W. Bode, S. Kawabata, 2001, Proceedings of the National Academy of Sciences of the United States of America.

The structure of thrombin, a chameleon‐like proteinase

W. Bode, 2005, Journal of thrombosis and haemostasis : JTH.

1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase.

Robert Huber, Kohei Oda, Hiroshi Oyama, 2004, Structure.

Crystal structure of the human α‐thrombin–haemadin complex: an exosite II‐binding inhibitor

R. Huber, W. Bode, P. Fuentes-Prior, 2000, The EMBO journal.

L-Isoaspartate 115 of porcine beta-trypsin promotes crystallization of its complex with bdellastasin.

R. Huber, W. Bode, M. Moser, 2000, Acta crystallographica. Section D, Biological crystallography.

Structure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of the bdellastasin-microplasmin system.

R. Huber, W. Bode, E. Auerswald, 1999, Journal of molecular biology.

The ornithodorin‐thrombin crystal structure, a key to the TAP enigma?

R. Huber, W. Bode, M. Stubbs, 1996, The EMBO journal.

Proteinase — Protein inhibitor interactions

R. Huber, W. Bode, 1994 .

Ligand binding: proteinase-protein inhibitor interactions

Robert Huber, R. Huber, W. Bode, 1991 .

Crystal structure of bovine trypsinogen at 1-8 A resolution. I. Data collection, application of patterson search techniques and preliminary structural interpretation.

R. Huber, W. Bode, H. Fehlhammer, 1976, Journal of molecular biology.

Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane

W. Bode, F. Gomis-Rüth, J. Arolas, 2012, Proceedings of the National Academy of Sciences.

Interaction of human alpha 1-proteinase inhibitor with chymotrypsinogen A and crystallization of a proteolytically modified alpha 1-proteinase inhibitor.

R. Huber, W. Bode, F. Lottspeich, 1982, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

The Specific Interaction of Human Leukocyte Elastase with Various Protein Inhibitors

W. Bode, 1988 .

Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution.

R. Huber, W. Bode, W Bode, 1985, Journal of molecular biology.

CRYSTAL STRUCTURE OF INSECT DERIVED DOUBLE DOMAIN KAZAL INHIBITOR RHODNIIN IN COMPLEX WITH THROMBIN

W. Bode, D. Lamba, A. Locht, 1996 .

Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction.

R. Huber, W. Bode, R. Engh, 1990, Biological chemistry Hoppe-Seyler.

Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin(1-51).

R. Huber, K. Wüthrich, P. Güntert, 1992, Journal of molecular biology.

Structural basis for the Zn2+ inhibition of the zymogen-like kallikrein-related peptidase 10

W. Bode, V. Magdolen, P. Goettig, 2016, Biological chemistry.

Structures and specificity of the human kallikrein-related peptidases KLK 4, 5, 6, and 7

Manfred Schmitt, C. Craik, W. Bode, 2008, Biological chemistry.

Chymotryptic specificity determinants in the 1.0 Å structure of the zinc-inhibited human tissue kallikrein 7

R. Huber, W. Bode, V. Magdolen, 2007, Proceedings of the National Academy of Sciences.

X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases.

Robert Huber, R. Huber, W. Bode, 2003, Journal of molecular biology.

Specific inhibition of insect alpha-amylases: yellow meal worm alpha-amylase in complex with the amaranth alpha-amylase inhibitor at 2.0 A resolution.

R. Huber, S. Pongor, W. Bode, 2000, Structure.

Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure.

R. Huber, W. Bode, K. Maskos, 2001, Journal of molecular biology.

Size and shape of the fibrinogen molecule: crystalline forms of native and modified human fibrinogen

W. Bode, R. Gollwitzer, 1986 .

Structural Basis for Possible Calcium-Induced Activation Mechanisms of Calpains

W. Bode, D. Reverter, H. Sorimachi, 2001 .

Insights into MMP‐TIMP Interactions

W. Bode, K. Maskos, H. Tschesche, 1999, Annals of the New York Academy of Sciences.

Engineering of Selective TIMPs

K. Brew, W. Bode, K. Maskos, 1999, Annals of the New York Academy of Sciences.

Residue 2 of TIMP-1 Is a Major Determinant of Affinity and Specificity for Matrix Metalloproteinases but Effects of Substitutions Do Not Correlate with Those of the Corresponding P1′ Residue of Substrate*

K. Brew, Yajing Hu, W. Bode, 1999, The Journal of Biological Chemistry.

Thermodynamic Linkage between the S1 Site, the Na+ Site, and the Ca2+ Site in the Protease Domain of Human Activated Protein C (APC)

W. Bode, S. P. Bajaj, K. Padmanabhan, 2002, The Journal of Biological Chemistry.

The three‐dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C.

R. Huber, F. X. Avilés, W. Bode, 1995, The EMBO journal.

Crystal structures, spectroscopic features, and catalytic properties of cobalt(II), copper(II), nickel(II), and mercury(II) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity.

W. Bode, H. Nar, F. Gomis-Rüth, 1994, The Journal of biological chemistry.

The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor

R. Huber, W. Bode, D. Kukla, 1975, Biophysics of structure and mechanism.

X-ray Structures of Free and Leupeptin-complexed Human αI-Tryptase Mutants: Indication for an α→β-Tryptase Transition

R. Huber, W. Bode, T. Selwood, 2006 .

The methyl group of N(alpha)(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage.

R. Huber, W. Bode, T. Steinmetzer, 2002, Journal of molecular biology.

X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design.

R. Huber, P. Reinemer, W. Bode, 1995, European journal of biochemistry.

X‐ray Structures of Human Neutrophil Collagenase Complexed with Peptide Hydroxamate and Peptide Thiol Inhibitors

R. Huber, P. Reinemer, W. Bode, 1995 .

The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution.

R. Huber, D. Turk, W. Bode, 1994, The Journal of biological chemistry.

Geometry of binding of the N alpha-tosylated piperidides of m-amidino-, p-amidino- and p-guanidino phenylalanine to thrombin and trypsin. X-ray crystal structures of their trypsin complexes and modeling of their thrombin complexes.

D. Turk, W. Bode, W Bode, 1991, FEBS letters.

X-Ray Structure of the Light-Harvesting Biliprotein C-Phycocyanin from M. laminosus

R. Huber, W. Bode, H. Zuber, 1987 .

The 2.3 A crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator.

D Lamba, R. Huber, Stefan Fischer, 1996, Journal of molecular biology.

Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain.

R. Huber, W. Bode, P. Deddish, 2007, Journal of molecular biology.

Crystallographic determination of thrombin complexes with small synthetic inhibitors as a starting point for the receptor-based design of antithrombotics.

D. Turk, W. Bode, H. Brandstetter, 1993, Seminars in thrombosis and hemostasis.

Inhibition of trypsin by carbobenzyloxylysyl chloromethyl ketone: 13C NMR and x-ray diffraction analyses of the enzyme-inhibitor complex

W. Bode, A. Scott, N. Mackenzie, 1986 .

Crystal structure of an oligomer of proteolytic zymogens: detailed conformational analysis of the bovine ternary complex and implications for their activation.

R. Huber, W. Bode, F. Avilés, 1997, Journal of molecular biology.

Cutting at the right place--the importance of selective limited proteolysis in the activation of proproteinase E.

R. Huber, W. Bode, F. Avilés, 1998, European journal of biochemistry.

A withproproteinase Eand chymotrypsinogen C

R. Huber, W. Bode, M. Gomez, 1995 .

Identification of a Hydrophobic Exosite on Tissue Type Plasminogen Activator That Modulates Specificity for Plasminogen*

W. Bode, D. Lamba, E. Madison, 1997, The Journal of Biological Chemistry.

Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy.

R. Huber, W. Bode, R. Engh, 1993, Journal of molecular biology.

Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity.

I. Lindberg, W. Bode, M. Than, 2005, Journal of molecular biology.

The X‐ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.

R. Huber, P. Reinemer, W. Bode, 1994, The EMBO journal.

Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution.

G. Schneider, Y. Lindqvist, E. Morgunova, 1998, Journal of molecular biology.

Three-dimensional Structure of Human Tissue Inhibitor of Metalloproteinases-2 at 2 . 1 AÊ Resolution

G. Schneider, Y. Lindqvist, E. Morgunova, 1998 .

The factor V C1 domain is involved in membrane binding: identification of functionally important amino acid residues within the C1 domain of factor V using alanine scanning mutagenesis

W. Bode, W. Peng, M. Quinn-Allen, 2003, Thrombosis and Haemostasis.

Crystal structures of the membrane-binding C2 domain of human coagulation factor V

R. Huber, T. Ortel, W. Bode, 1999, Nature.

The 1.8-Å Crystal Structure of a Matrix Metalloproteinase 8-Barbiturate Inhibitor Complex Reveals a Previously Unobserved Mechanism for Collagenase Substrate Recognition*

H Brandstetter, R. Huber, H. Krell, 2001, The Journal of Biological Chemistry.

Expression, Purification, Characterization, and X-Ray Analysis of Selenomethionine 215 Variant of Leukocyte Collagenase

W. Bode, N. Budisa, H. Tschesche, 1997, Journal of protein chemistry.

Design and synthesis of heterotrimeric collagen peptides with a built‐in cystine‐knot Models for collagen catabolism by matrix‐metalloproteases

W. Bode, L. Moroder, H. Tschesche, 1996, FEBS letters.

Inhibition of Matrix Metalloproteinases in Rheumatoid Arthritis and the Crystallographic Binding Mode of a Peptide Inhibitor

P. Reinemer, W. Bode, H. Tschesche, 1994, Annals of the New York Academy of Sciences.

Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases

R. Huber, P. Reinemer, W. Bode, 1994, FEBS letters.

Function and Structure of Human Leucocyte Collagenase

P. Reinemer, W. Bode, H. Tschesche, 1995 .

The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region.

R. Huber, W. Bode, C. Sommerhoff, 2002, Journal of molecular biology.

Thermal transitions of Proteus mirabilis flagellin as studied by circular dichroism and adiabatic differential calorimetry

W. Bode, 1973, FEBS letters.

Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases.

W. Bode, F. Gomis-Rüth, F. Gomis-ruth, 1993, European journal of biochemistry.

Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features.

J. Foidart, W. Bode, A. Noel, 2004, Journal of molecular biology.

Bis-substituted malonic acid hydroxamate derivatives as inhibitors of human neutrophil collagenase (MMP8).

W. Bode, R. Engh, H. Brandstetter, 1998, Journal of medicinal chemistry.

Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin.

R. Huber, W. Bode, F. Gomis-Rüth, 1994, Journal of molecular biology.

Sequence and structure similarities of cathepsin B from the parasite Schistosoma mansoni and human liver

W. Bode, V. Turk, E. Shaw, 1994, FEBS letters.

Spatial Structure of Thrombin as a Guide to Its Multiple Sites of Interaction

W. Bode, M. Stubbs, 1993, Seminars in thrombosis and hemostasis.

Crystal structure of the E. coli dipeptidyl carboxypeptidase Dcp: further indication of a ligand-dependent hinge movement mechanism.

W. Bode, K. Maskos, W Bode, 2005, Journal of molecular biology.

A standard orientation for metallopeptidases.

W. Bode, F. Gomis-Rüth, T. Botelho, 2012, Biochimica et biophysica acta.

Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin

C. Craik, W. Bode, O. Schilling, 2018, Scientific Reports.

The variable region-1 from tissue-type plasminogen activator confers specificity for plasminogen activator inhibitor-1 to thrombin by facilitating catalysis: release of a kinetic block by a heterologous protein surface loop.

W. Bode, R. Dekker, A. Horrevoets, 1999, Journal of molecular biology.

Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2.

W. Bode, K. Maskos, H. Tschesche, 2007, Journal of molecular biology.

The single calcium-binding site of crystallin bovin beta-trypsin.

W. Bode, P. Schwager, 1975, FEBS Letters.

The structure of calcium-free human m-calpain: implications for calcium activation and function.

W. Bode, D. Reverter, H. Sorimachi, 2001, Trends in cardiovascular medicine.

Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin

C. Craik, W. Bode, O. Schilling, 2018, Scientific Reports.

Interactions of thrombin with benzamidine-based inhibitors.

D. Turk, W. Bode, W Bode, 1992, Biological chemistry Hoppe-Seyler.

Role of tachylectins in host defense of the Japanese horseshoe crab Tachypleus tridentatus.

R. Huber, W. Bode, S. Wai, 2001, Advances in experimental medicine and biology.

Crystal Structure of the Antihaemophilic Clotting Factor IXa

R. Huber, W. Bode, H. Brandstetter, 1996 .

Involvement of tyrosine residues in the protomer-protomer interaction of Proteus mirabilis flagella as studied by spectroscopic methods, chemical modification and aggregation experiments.

W. Bode, W. Schalch, 1975, Biochimica et biophysica acta.

A model of bacterial flagella based on small-angle x-ray scattering and hydrodynamic data which indicated an elongated shape of the flagellin protomer.

W. Bode, J. Engel, W. Bode, 1972, European journal of biochemistry.

Cyanogen bromide cleavage of Proteus mirabilis flagellin. Maleylation of cyanogen bromide peptides.

W. Bode, H. Glossmann, 1972, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

Crystallization of chicken egg white cystatin, a low molecular weight protein inhibitor of cysteine proteinases, and preliminary X-ray diffraction data.

W. Bode, V. Turk, J. Brzin, 1985, Journal of molecular biology.

Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.

W. Bode, D. Reverter, R. Skidgel, 2004, Journal of molecular biology.

Structural studies on MMPs and TIMPs.

W. Bode, K. Maskos, 2001, Methods in molecular biology.