PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY

BECKMANN J, MEHLICH A, SCHRODER W, Wenzel H, Tschesche H (1988)
EUROPEAN JOURNAL OF BIOCHEMISTRY 176(3): 675-682.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Autor*in
BECKMANN, J; MEHLICH, A; SCHRODER, W; Wenzel, HerbertUniBi; Tschesche, HaraldUniBi
Erscheinungsjahr
1988
Zeitschriftentitel
EUROPEAN JOURNAL OF BIOCHEMISTRY
Band
176
Ausgabe
3
Seite(n)
675-682
ISSN
0014-2956
eISSN
1432-1033
Page URI
https://pub.uni-bielefeld.de/record/1653768

Zitieren

BECKMANN J, MEHLICH A, SCHRODER W, Wenzel H, Tschesche H. PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY. EUROPEAN JOURNAL OF BIOCHEMISTRY. 1988;176(3):675-682.
BECKMANN, J., MEHLICH, A., SCHRODER, W., Wenzel, H., & Tschesche, H. (1988). PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY. EUROPEAN JOURNAL OF BIOCHEMISTRY, 176(3), 675-682. https://doi.org/10.1111/j.1432-1033.1988.tb14330.x
BECKMANN, J, MEHLICH, A, SCHRODER, W, Wenzel, Herbert, and Tschesche, Harald. 1988. “PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY”. EUROPEAN JOURNAL OF BIOCHEMISTRY 176 (3): 675-682.
BECKMANN, J., MEHLICH, A., SCHRODER, W., Wenzel, H., and Tschesche, H. (1988). PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY. EUROPEAN JOURNAL OF BIOCHEMISTRY 176, 675-682.
BECKMANN, J., et al., 1988. PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY. EUROPEAN JOURNAL OF BIOCHEMISTRY, 176(3), p 675-682.
J. BECKMANN, et al., “PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY”, EUROPEAN JOURNAL OF BIOCHEMISTRY, vol. 176, 1988, pp. 675-682.
BECKMANN, J., MEHLICH, A., SCHRODER, W., Wenzel, H., Tschesche, H.: PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY. EUROPEAN JOURNAL OF BIOCHEMISTRY. 176, 675-682 (1988).
BECKMANN, J, MEHLICH, A, SCHRODER, W, Wenzel, Herbert, and Tschesche, Harald. “PREPARATION OF CHEMICALLY MUTATED APROTININ HOMOLOGS BY SEMISYNTHESIS - P1 SUBSTITUTIONS CHANGE INHIBITORY SPECIFICITY”. EUROPEAN JOURNAL OF BIOCHEMISTRY 176.3 (1988): 675-682.

18 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Fluorine teams up with water to restore inhibitor activity to mutant BPTI.
Ye S, Loll B, Berger AA, Mülow U, Alings C, Wahl MC, Koksch B., Chem Sci 6(9), 2015
PMID: 29449928
Evidence-based review of the role of aprotinin in blood conservation during orthopaedic surgery.
Kokoszka A, Kuflik P, Bitan F, Casden A, Neuwirth M., J Bone Joint Surg Am 87(5), 2005
PMID: 15866981
Remarkable phylum selectivity of a Schistocerca gregaria trypsin inhibitor: the possible role of enzyme-inhibitor flexibility.
Patthy A, Amir S, Malik Z, Bódi A, Kardos J, Asbóth B, Gráf L., Arch Biochem Biophys 398(2), 2002
PMID: 11831848
Design, docking, and evaluation of multiple libraries against multiple targets.
Lamb ML, Burdick KW, Toba S, Young MM, Skillman AG, Zou X, Arnold JR, Kuntz ID., Proteins 42(3), 2001
PMID: 11151003
Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library.
McBride JD, Freeman HN, Leatherbarrow RJ., Eur J Biochem 266(2), 1999
PMID: 10561580
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
Binding of amino acid side-chains to S1 cavities of serine proteinases.
Lu W, Apostol I, Qasim MA, Warne N, Wynn R, Zhang WL, Anderson S, Chiang YW, Ogin E, Rothberg I, Ryan K, Laskowski M., J Mol Biol 266(2), 1997
PMID: 9047374
Directed evolution of a protein: selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage.
Roberts BL, Markland W, Ley AC, Kent RB, White DW, Guterman SK, Ladner RC., Proc Natl Acad Sci U S A 89(6), 1992
PMID: 1549606
Protease inhibitor display M13 phage: selection of high-affinity neutrophil elastase inhibitors.
Roberts BL, Markland W, Siranosian K, Saxena MJ, Guterman SK, Ladner RC., Gene 121(1), 1992
PMID: 1385268
Enzymatic semisynthesis of aprotinin homologues mutated in P' positions.
Groeger C, Wenzel HR, Tschesche H., J Protein Chem 10(2), 1991
PMID: 1718310
Chemical semisynthesis of aprotinin homologues and derivatives mutated in P' positions.
Groeger C, Wenzel HR, Tschesche H., J Protein Chem 10(5), 1991
PMID: 1724726
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

44 References

Daten bereitgestellt von Europe PubMed Central.


Holzer, 1979
Ovomucoid third domains from 100 avian species: isolation, sequences, and hypervariability of enzyme-inhibitor contact residues.
Laskowski M Jr, Kato I, Ardelt W, Cook J, Denton A, Empie MW, Kohr WJ, Park SJ, Parks K, Schatzley BL., Biochemistry 26(1), 1987
PMID: 3828298
On the size of the active site in proteases. I. Papain.
Schechter I, Berger A., Biochem. Biophys. Res. Commun. 27(2), 1967
PMID: 6035483
Covalent hybrids of ovomucoid third domains made from one synthetic and one natural peptide chain.
Wieczorek M, Park SJ, Laskowski M Jr., Biochem. Biophys. Res. Commun. 144(1), 1987
PMID: 3555488

AUTHOR UNKNOWN, 0
Protein inhibitors of proteinases.
Laskowski M Jr, Kato I., Annu. Rev. Biochem. 49(), 1980
PMID: 6996568

Wenzel, Angew. Chem. Int. Ed. Engl. 20(), 1981

Odani, J. Biochem. (Tokyo) 84(), 1978

Odani, J. Biochem. (Tokyo) 88(), 1980

Kurokawa, J. Biochem. (Tokyo) 101(), 1987

Kurokawa, J. Biochem. (Tokyo) 102(), 1987
Recombinant DNA-derived forms of human alpha 1-proteinase inhibitor. Studies on the alanine 358 and cysteine 358 substituted mutants.
Matheson NR, Gibson HL, Hallewell RA, Barr PJ, Travis J., J. Biol. Chem. 261(22), 1986
PMID: 3525544
A synthetic operon containing 14 bovine pancreatic trypsin inhibitor genes is expressed in E. coli.
von Wilcken-Bergmann B, Tils D, Sartorius J, Auerswald EA, Schroder W, Muller-Hill B., EMBO J. 5(12), 1986
PMID: 2434325
Synthesis, cloning and expression of recombinant aprotinin.
Auerswald EA, Schroder W, Kotick M., Biol. Chem. Hoppe-Seyler 368(10), 1987
PMID: 2447912
Immunofluorescence studies indicate that the basic trypsin-kallikrein-inhibitor of bovine organs (Trasylol) originates from mast cells.
Fritz H, Kruck J, Russe I, Liebich HG., Hoppe-Seyler's Z. Physiol. Chem. 360(3), 1979
PMID: 374218
The disulfide linkages in kallikrein inactivator of bovine lung.
Anderer FA, Hornle S., J. Biol. Chem. 241(7), 1966
PMID: 5296424

Fritz, Arzneim.-Forsch. Drug Res. 33(), 1983
Semisynthetic engineering of proteinase inhibitor homologues.
Tschesche H, Beckmann J, Mehlich A, Schnabel E, Truscheit E, Wenzel HR., Biochim. Biophys. Acta 913(1), 1987
PMID: 2437960
Separation of the human leucocyte enzymes alanine aminopeptidase, cathepsin G, collagenase, elastase and myeloperoxidase.
Engelbrecht S, Pieper E, Macartney HW, Rautenberg W, Wenzel HR, Tschesche H., Hoppe-Seyler's Z. Physiol. Chem. 363(3), 1982
PMID: 6122635

Taschner, Ann. Chem. 646(), 1961

Biernat, Ann. Chem. 646(), 1961
Advantages of picrate fixation for staining polypeptides in polyacrylamide gels.
Stephano JL, Gould M, Rojas-Galicia L., Anal. Biochem. 152(2), 1986
PMID: 2421602
A gas-liquid solid phase peptide and protein sequenator.
Hewick RM, Hunkapiller MW, Hood LE, Dreyer WJ., J. Biol. Chem. 256(15), 1981
PMID: 7263636

AUTHOR UNKNOWN, 0

Bergmeyer, 1984
Pancreatic trypsin inhibitor. II. Reaction with trypsin.
GREEN NM, WORK E., Biochem. J. 54(2), 1953
PMID: 13058883

AUTHOR UNKNOWN, 0

AUTHOR UNKNOWN, 0
The basic trypsin inhibitor of bovine pancreas. I. Structure analysis and conformation of the polypeptide chain.
Huber R, Kukla D, Ruhlmann A, Epp O, Formanek H., Naturwissenschaften 57(8), 1970
PMID: 5447861
Stopped-flow kinetics of the resynthesis of the reactive site peptile bond in kallikrein inhibitor (Kunitz) by beta-trypsin.
Quast U, Engel J, Steffen E, Tschesche H, Kupfer S., Biochemistry 17(9), 1978
PMID: 26384
Selective oxidation of methionine residues in proteins.
Shechter Y, Burstein Y, Patchornik A., Biochemistry 14(20), 1975
PMID: 1174512

Liardon, Int. J. Peptide Protein Res. 18(), 1981

AUTHOR UNKNOWN, 0

Tschesche, Bayer Symp. (), 1974
Studies on the basic trypsin inhibitor of bovine pancreas and its interaction with trypsin.
Avineri-Goldman R, Snir I, Blauer G, Rigbi M., Arch. Biochem. Biophys. 121(1), 1967
PMID: 6035058
The inhibition of human leukocyte elastase by basic pancreatic trypsin inhibitor.
Lestienne P, Bieth JG., Arch. Biochem. Biophys. 190(1), 1978
PMID: 568456
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 2458925
PubMed | Europe PMC

Suchen in

Google Scholar