Fabry M - Search Results

1

Mutagenesis, biochemical characterization and X-ray structural analysis of point mutants of bovine chymosin.

Williams MG, Wilsher J, Nugent P, Mills A, Dhanaraj V, Fabry M, Sedlácek J, Uusitalo JM, Penttila ME, Pitts JE, Blundell TL. Williams MG, et al. Among authors: fabry m. Protein Eng. 1997 Sep;10(9):991-7. doi: 10.1093/protein/10.9.991. Protein Eng. 1997. PMID: 9464563

2

Engineering enzyme subsite specificity: preparation, kinetic characterization, and X-ray analysis at 2.0-A resolution of Val111Phe site-mutated calf chymosin.

Strop P, Sedlacek J, Stys J, Kaderabkova Z, Blaha I, Pavlickova L, Pohl J, Fabry M, Kostka V, Newman M, et al. Strop P, et al. Among authors: fabry m. Biochemistry. 1990 Oct 23;29(42):9863-71. doi: 10.1021/bi00494a016. Biochemistry. 1990. PMID: 2271625

3

Preliminary crystallographic studies of an anti-HIV-1 protease antibody that inhibits enzyme activity.

Lescar J, Stouracova R, Riottot MM, Chitarra V, Brynda J, Fabry M, Horejsi M, Sedlacek J, Bentley GA. Lescar J, et al. Among authors: fabry m. Protein Sci. 1996 May;5(5):966-8. doi: 10.1002/pro.5560050518. Protein Sci. 1996. PMID: 8732768 Free PMC article.

4

Design of synthetic oligonucleotide duplexes for site-directed mutagenesis with recombinant plasmids.

Sedlácek J, Fábry M, Smrt J. Sedlácek J, et al. Among authors: fabry m. Nucleic Acids Symp Ser. 1987;(18):245-8. Nucleic Acids Symp Ser. 1987. PMID: 3697136

5

Myeloblastosis associated virus (MAV) proteinase site-mutated to be HIV-like has a higher activity and allows production of infectious but morphologically altered virus.

Sedlacek J, Fabry M, Coward JE, Horejsi M, Strop P, Luftig RB. Sedlacek J, et al. Among authors: fabry m. Virology. 1993 Feb;192(2):667-72. doi: 10.1006/viro.1993.1085. Virology. 1993. PMID: 7678476

6

The Gag-Pol encoded proteinase of an avian retrovirus expressed in E. coli can produce a novel proteinase (PR + IleGly) that is two amino acids larger at its carboxy-terminal region than the major Gag proteinase (PR).

Brynda J, Fábry M, Horejsí M, Sedlácek J. Brynda J, et al. Among authors: fabry m. Virology. 1995 Feb 20;207(1):185-90. doi: 10.1006/viro.1995.1065. Virology. 1995. PMID: 7871726 Free article.

7

Three-dimensional structure of an Fab-peptide complex: structural basis of HIV-1 protease inhibition by a monoclonal antibody.

Lescar J, Stouracova R, Riottot MM, Chitarra V, Brynda J, Fabry M, Horejsi M, Sedlacek J, Bentley GA. Lescar J, et al. Among authors: fabry m. J Mol Biol. 1997 Apr 18;267(5):1207-22. doi: 10.1006/jmbi.1997.0950. J Mol Biol. 1997. PMID: 9150407

8

Structure of HOE/BAY 793 complexed to human immunodeficiency virus (HIV-1) protease in two different crystal forms--structure/function relationship and influence of crystal packing.

Lange-Savage G, Berchtold H, Liesum A, Budt KH, Peyman A, Knolle J, Sedlacek J, Fabry M, Hilgenfeld R. Lange-Savage G, et al. Among authors: fabry m. Eur J Biochem. 1997 Sep 1;248(2):313-22. doi: 10.1111/j.1432-1033.1997.00313.x. Eur J Biochem. 1997. PMID: 9346283 Free article.

9

Effects of temperature and novobiocin on the expression of calf prochymosin gene and on plasmid copy number in recombinant Escherichia coli.

Kaprálek F, Tichý PJ, Fábry M, Sedlácek J. Kaprálek F, et al. Among authors: fabry m. Folia Microbiol (Praha). 1998;43(1):63-7. doi: 10.1007/BF02815545. Folia Microbiol (Praha). 1998. PMID: 9569630

10

An engineered retroviral proteinase from myeloblastosis associated virus acquires pH dependence and substrate specificity of the HIV-1 proteinase.

Konvalinka J, Horejsí M, Andreánsky M, Novek P, Pichová I, Bláha I, Fábry M, Sedlácek J, Foundling S, Strop P. Konvalinka J, et al. Among authors: fabry m. EMBO J. 1992 Mar;11(3):1141-4. doi: 10.1002/j.1460-2075.1992.tb05154.x. EMBO J. 1992. PMID: 1547777 Free PMC article.

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