Wolfram Bode

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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.

Natural protein proteinase inhibitors and their interaction with proteinases.

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

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.

The clot thickens: clues provided by thrombin structure.

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

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.

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

W. Bode, K. Maskos, K. Maskos, 2003, 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.

(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.

Molecular mechanisms of plasminogen activation: bacterial cofactors provide clues.

X C Zhang, M A Parry, I Bode, 2000, Trends in biochemical sciences.

The metzincin-superfamily of zinc-peptidases.

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

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.

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.

Thrombin-induced fibrinopeptide release from a fibrinogen variant (fibrinogen Sydney I) with an Aalpha Arg-16----His substitution.

Wolfram Bode, Chris Southan, David A. Lane, 2008, European journal of biochemistry.

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.

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.

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

W. Bode, Wolfram Bode, 1995, Structure.

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.

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.

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.

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

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

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.

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 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.

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.

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.

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.

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.

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

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

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.

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.

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.

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.

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

P. Fuentes-Prior, M. Quinn-Allen, Wolfram Bode, 2003, Thrombosis and Haemostasis.