Schlott B - Search Results

1

NMR secondary structure of the plasminogen activator protein staphylokinase.

Ohlenschläger O, Ramachandran R, Flemming J, Gührs KH, Schlott B, Brown LR. Ohlenschläger O, et al. Among authors: schlott b. J Biomol NMR. 1997 Apr;9(3):273-86. doi: 10.1023/a:1018678925512. J Biomol NMR. 1997. PMID: 9204556

2

Functional significance of NH2- and COOH-terminal regions of staphylokinase in plasminogen activation.

Gase A, Hartmann M, Gührs KH, Röcker A, Collen D, Behnke D, Schlott B. Gase A, et al. Among authors: schlott b. Thromb Haemost. 1996 Nov;76(5):755-60. Thromb Haemost. 1996. PMID: 8950786

3

Staphylokinase requires NH2-terminal proteolysis for plasminogen activation.

Schlott B, Gührs KH, Hartmann M, Röcker A, Collen D. Schlott B, et al. J Biol Chem. 1997 Feb 28;272(9):6067-72. doi: 10.1074/jbc.272.9.6067. J Biol Chem. 1997. PMID: 9038231 Free article.

4

Nuclear magnetic resonance solution structure of the plasminogen-activator protein staphylokinase.

Ohlenschläger O, Ramachandran R, Gührs KH, Schlott B, Brown LR. Ohlenschläger O, et al. Among authors: schlott b. Biochemistry. 1998 Jul 28;37(30):10635-42. doi: 10.1021/bi980673i. Biochemistry. 1998. PMID: 9692953

5

NH2-terminal structural motifs in staphylokinase required for plasminogen activation.

Schlott B, Gührs KH, Hartmann M, Röcker A, Collen D. Schlott B, et al. J Biol Chem. 1998 Aug 28;273(35):22346-50. doi: 10.1074/jbc.273.35.22346. J Biol Chem. 1998. PMID: 9712854 Free article.

Staphylokinase (Sak) forms an inactive 1:1 stoichiometric complex with plasminogen which requires both conversion of plasminogen to plasmin and hydrolysis of the Lys10-Lys11 peptide bond of Sak to become a potent plasminogen activator (Schlott, B., Guhrs, K.-H., Har …

Staphylokinase (Sak) forms an inactive 1:1 stoichiometric complex with plasminogen which requires both conversion of plasminogen to plasmin …

6

Interaction of Kazal-type inhibitor domains with serine proteinases: biochemical and structural studies.

Schlott B, Wöhnert J, Icke C, Hartmann M, Ramachandran R, Gührs KH, Glusa E, Flemming J, Görlach M, Grosse F, Ohlenschläger O. Schlott B, et al. J Mol Biol. 2002 Apr 26;318(2):533-46. doi: 10.1016/S0022-2836(02)00014-1. J Mol Biol. 2002. PMID: 12051857

7

Fusion proteins with anticoagulant and fibrinolytic properties: functional studies and structural considerations.

Icke C, Schlott B, Ohlenschläger O, Hartmann M, Gührs KH, Glusa E. Icke C, et al. Among authors: schlott b. Mol Pharmacol. 2002 Aug;62(2):203-9. doi: 10.1124/mol.62.2.203. Mol Pharmacol. 2002. PMID: 12130670

8

High yield production and purification of recombinant staphylokinase for thrombolytic therapy.

Schlott B, Hartmann M, Gührs KH, Birch-Hirschfeid E, Pohl HD, Vanderschueren S, Van de Werf F, Michoel A, Collen D, Behnke D. Schlott B, et al. Biotechnology (N Y). 1994 Feb;12(2):185-9. doi: 10.1038/nbt0294-185. Biotechnology (N Y). 1994. PMID: 7764434

9

Functional properties of recombinant staphylokinase variants obtained by site-specific mutagenesis of methionine-26.

Schlott B, Hartmann M, Gührs KH, Birch-Hirschfeld E, Gase A, Vettermann S, Collen D, Lijnen HR. Schlott B, et al. Biochim Biophys Acta. 1994 Feb 16;1204(2):235-42. doi: 10.1016/0167-4838(94)90013-2. Biochim Biophys Acta. 1994. PMID: 8142464

10

The fibrinolytic activity of staphylokinase mutants in the fibrin plate assay.

Hauptmann J, Gührs KH, Hartmann M, Schlott B. Hauptmann J, et al. Among authors: schlott b. Haemostasis. 1995 Nov-Dec;25(6):272-6. doi: 10.1159/000217172. Haemostasis. 1995. PMID: 8586317

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