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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DOI
Autor*in
Tschesche, HaraldUniBi; BECKMANN, J; MEHLICH, A; SCHNABEL, E; TRUSCHEIT, E; Wenzel, HerbertUniBi
Einrichtung
Fakultät für Chemie > Biochemie I
Erscheinungsjahr
1987
Zeitschriftentitel
BIOCHIMICA ET BIOPHYSICA ACTA
Band
913
Ausgabe
1
Seite(n)
97-101
ISSN
0167-4838
Page URI
https://pub.uni-bielefeld.de/record/1655390

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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. https://doi.org/10.1016/0167-4838(87)90238-X
Tschesche, Harald, BECKMANN, J, MEHLICH, A, SCHNABEL, E, TRUSCHEIT, E, and Wenzel, Herbert. 1987. “SEMISYNTHETIC ENGINEERING OF PROTEINASE-INHIBITOR HOMOLOGS”. BIOCHIMICA ET BIOPHYSICA ACTA 913 (1): 97-101.
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.

17 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Three-dimensional Structure of a Kunitz-type Inhibitor in Complex with an Elastase-like Enzyme.
García-Fernández R, Perbandt M, Rehders D, Ziegelmüller P, Piganeau N, Hahn U, Betzel C, Chávez Mde L, Redecke L., J Biol Chem 290(22), 2015
PMID: 25878249
Polar Desolvation and Position 226 of Pancreatic and Neutrophil Elastases Are Crucial to their Affinity for the Kunitz-Type Inhibitors ShPI-1 and ShPI-1/K13L.
Hernández González JE, García-Fernández R, Valiente PA., PLoS One 10(9), 2015
PMID: 26372354
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
Structure-function analysis of the reactive site in the first Kunitz-type domain of human tissue factor pathway inhibitor-2.
Chand HS, Schmidt AE, Bajaj SP, Kisiel W., J Biol Chem 279(17), 2004
PMID: 14970225
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
Binding of native and [homoserine lactone-52]-52,53-seco-bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor) to porcine pancreatic beta-kallikrein-B and bovine alpha-chymotrypsin: thermodynamic study.
Oddone R, Barra D, Amiconi G, Ascenzi P, Tarricone C, Bolognesi M, Bortolotti F, Menegatti E., J Mol Recognit 7(1), 1994
PMID: 7527234
Binding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues.
Bigler TL, Lu W, Park SJ, Tashiro M, Wieczorek M, Wynn R, Laskowski M., Protein Sci 2(5), 1993
PMID: 8495199
Rapid purification of DesPro(2)-Val15-Leu17-aprotinin from the culture broth of a recombinant Saccharomyces cerevisiae.
Barthel T, Kula MR., Biotechnol Bioeng 42(11), 1993
PMID: 18612961
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
The refined 2.3 A crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor.
Wei AZ, Mayr I, Bode W., FEBS Lett 234(2), 1988
PMID: 3391280
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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