SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS

Tschesche H, BECKMANN J, MEHLICH A, SCHNABEL E, TRUSCHEIT E, Wenzel H (1987)
BIOCHIMICA ET BIOPHYSICA ACTA 913(1): 97-101.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Erscheinungsjahr
Zeitschriftentitel
BIOCHIMICA ET BIOPHYSICA ACTA
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913
Zeitschriftennummer
1
Seite
97-101
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Tschesche H, BECKMANN J, MEHLICH A, SCHNABEL E, TRUSCHEIT E, Wenzel H. SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS. BIOCHIMICA ET BIOPHYSICA ACTA. 1987;913(1):97-101.
Tschesche, H., BECKMANN, J., MEHLICH, A., SCHNABEL, E., TRUSCHEIT, E., & Wenzel, H. (1987). SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS. BIOCHIMICA ET BIOPHYSICA ACTA, 913(1), 97-101. doi:10.1016/0167-4838(87)90238-X
Tschesche, H., BECKMANN, J., MEHLICH, A., SCHNABEL, E., TRUSCHEIT, E., and Wenzel, H. (1987). SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS. BIOCHIMICA ET BIOPHYSICA ACTA 913, 97-101.
Tschesche, H., et al., 1987. SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS. BIOCHIMICA ET BIOPHYSICA ACTA, 913(1), p 97-101.
H. Tschesche, et al., “SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS”, BIOCHIMICA ET BIOPHYSICA ACTA, vol. 913, 1987, pp. 97-101.
Tschesche, H., BECKMANN, J., MEHLICH, A., SCHNABEL, E., TRUSCHEIT, E., Wenzel, H.: SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS. BIOCHIMICA ET BIOPHYSICA ACTA. 913, 97-101 (1987).
Tschesche, Harald, BECKMANN, J, MEHLICH, A, SCHNABEL, E, TRUSCHEIT, E, and Wenzel, Herbert. “SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS”. BIOCHIMICA ET BIOPHYSICA ACTA 913.1 (1987): 97-101.

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Three-dimensional Structure of a Kunitz-type Inhibitor in Complex with an Elastase-like Enzyme.
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PMID: 25878249
A spider-derived Kunitz-type serine protease inhibitor that acts as a plasmin inhibitor and an elastase inhibitor.
Wan H, Lee KS, Kim BY, Zou FM, Yoon HJ, Je YH, Li J, Jin BR., PLoS One 8(1), 2013
PMID: 23308198
Simukunin from the salivary glands of the black fly Simulium vittatum inhibits enzymes that regulate clotting and inflammatory responses.
Tsujimoto H, Kotsyfakis M, Francischetti IM, Eum JH, Strand MR, Champagne DE., PLoS One 7(2), 2012
PMID: 22383955
Inhibition of six serine proteinases of the human coagulation system by mutants of bovine pancreatic trypsin inhibitor.
Grzesiak A, Krokoszynska I, Krowarsch D, Buczek O, Dadlez M, Otlewski J., J Biol Chem 275(43), 2000
PMID: 10930417
Strong crossreaction of human anti-aprotinin antibodies from heart transplant patient with [Arg15]aprotinin.
Brinkmann T, Körfer R, Wenzel HR, Tschesche H, Kleesiek K., Immunopharmacology 35(3), 1997
PMID: 9043935
Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.
Capasso C, Rizzi M, Menegatti E, Ascenzi P, Bolognesi M., J Mol Recognit 10(1), 1997
PMID: 9179777
Recombinant aprotinin homologue with new inhibitory specificity for cathepsin G.
Brinkmann T, Schnierer S, Tschesche H., Eur J Biochem 202(1), 1991
PMID: 1718753
Interaction of the peptide CF3-Leu-Ala-NH-C6H4-CF3 (TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 A.
Li de la Sierra I, Papamichael E, Sakarellos C, Dimicoli JL, Prangé T., J Mol Recognit 3(1), 1990
PMID: 2354062
Semisynthesis of Arg15, Glu15, Met15, and Nle15-aprotinin involving enzymatic peptide bond resynthesis.
Beckmann J, Mehlich A, Schröder W, Wenzel HR, Tschesche H., J Protein Chem 8(1), 1989
PMID: 2475133
Molecular genetic approaches to Alzheimer's disease.
Tanzi RE, St George-Hyslop PH, Gusella JF., Trends Neurosci 12(4), 1989
PMID: 2470173
Preparation of chemically 'mutated' aprotinin homologues by semisynthesis. P1 substitutions change inhibitory specificity.
Beckmann J, Mehlich A, Schröder W, Wenzel HR, Tschesche H., Eur J Biochem 176(3), 1988
PMID: 2458925

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