Bode W - Search Results

1

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

Turk D, Podobnik M, Popovic T, Katunuma N, Bode W, Huber R, Turk V. Turk D, et al. Among authors: bode w. Biochemistry. 1995 Apr 11;34(14):4791-7. doi: 10.1021/bi00014a037. Biochemistry. 1995. PMID: 7718586

2

Natural protein proteinase inhibitors and their interaction with proteinases.

Bode W, Huber R. Bode W, et al. Eur J Biochem. 1992 Mar 1;204(2):433-51. doi: 10.1111/j.1432-1033.1992.tb16654.x. Eur J Biochem. 1992. PMID: 1541261 Free article. Review.

3

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

Stubbs MT, Oschkinat H, Mayr I, Huber R, Angliker H, Stone SR, Bode W. Stubbs MT, et al. Among authors: bode w. Eur J Biochem. 1992 May 15;206(1):187-95. doi: 10.1111/j.1432-1033.1992.tb16916.x. Eur J Biochem. 1992. PMID: 1587268 Free article.

4

Geometry of binding of the benzamidine- and arginine-based inhibitors N alpha-(2-naphthyl-sulphonyl-glycyl)-DL-p-amidinophenylalanyl-pipe ridine (NAPAP) and (2R,4R)-4-methyl-1-[N alpha-(3-methyl-1,2,3,4-tetrahydro-8- quinolinesulphonyl)-L-arginyl]-2-piperidine carboxylic acid (MQPA) to human alpha-thrombin. X-ray crystallographic determination of the NAPAP-trypsin complex and modeling of NAPAP-thrombin and MQPA-thrombin.

Bode W, Turk D, Stürzebecher J. Bode W, et al. Eur J Biochem. 1990 Oct 5;193(1):175-82. doi: 10.1111/j.1432-1033.1990.tb19320.x. Eur J Biochem. 1990. PMID: 2226434 Free article.

(Tokyo) 105, 949-952] were transferred in their trypsin-binding conformations to human alpha-thrombin [Bode, W., Mayr, I., Baumann, U., Huber, R., Stone, S. R. & Hofsteenge, J. (1989) EMBO J. 8. 3467 - 3475] and energy minimized. ...

(Tokyo) 105, 949-952] were transferred in their trypsin-binding conformations to human alpha-thrombin [Bode, W., Mayr, I., Bau …

5

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.

Bode W, Walter J, Huber R, Wenzel HR, Tschesche H. Bode W, et al. Eur J Biochem. 1984 Oct 1;144(1):185-90. doi: 10.1111/j.1432-1033.1984.tb08447.x. Eur J Biochem. 1984. PMID: 6207021 Free article.

Large orthorhombic crystals of the complex formed by bovine trypsinogen and a semisynthetic homologous bovine pancreatic trypsin inhibitor with the reactive-site lysine residue replaced by an arginine residue [( Arg15]PTI) have been obtained which are isomorphous with the crystal …

Large orthorhombic crystals of the complex formed by bovine trypsinogen and a semisynthetic homologous bovine pancreatic trypsin inhibitor w …

6

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

Grams F, Reinemer P, Powers JC, Kleine T, Pieper M, Tschesche H, Huber R, Bode W. Grams F, et al. Among authors: bode w. Eur J Biochem. 1995 Mar 15;228(3):830-41. doi: 10.1111/j.1432-1033.1995.tb20329.x. Eur J Biochem. 1995. PMID: 7737183 Free article.

7

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

Lin G, Bode W, Huber R, Chi C, Engh RA. Lin G, et al. Among authors: bode w. Eur J Biochem. 1993 Mar 1;212(2):549-55. doi: 10.1111/j.1432-1033.1993.tb17692.x. Eur J Biochem. 1993. PMID: 8444191 Free article.

8

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

Renatus M, Stubbs MT, Huber R, Bringmann P, Donner P, Schleuning WD, Bode W. Renatus M, et al. Among authors: bode w. Biochemistry. 1997 Nov 4;36(44):13483-93. doi: 10.1021/bi971129x. Biochemistry. 1997. PMID: 9354616

9

The cystatins: protein inhibitors of cysteine proteinases.

Turk V, Bode W. Turk V, et al. Among authors: bode w. FEBS Lett. 1991 Jul 22;285(2):213-9. doi: 10.1016/0014-5793(91)80804-c. FEBS Lett. 1991. PMID: 1855589 Free article. Review.

10

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

Richardson JL, Fuentes-Prior P, Sadler JE, Huber R, Bode W. Richardson JL, et al. Among authors: bode w. Biochemistry. 2002 Feb 26;41(8):2535-42. doi: 10.1021/bi011605q. Biochemistry. 2002. PMID: 11851400

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