Pathogenicity |
Evaluating antimicrobial and antioxidant capacity of endemic Phlomis russeliana from Turkey and its antiproliferative effect on Human Caco-2 Cell Lines. |
Alpay M, Dulger G, Sahin IE, Dulger B |
An Acad Bras Cienc |
10.1590/0001-3765201920180404 |
2019 |
* |
Pathogenicity |
Synthesis, spectroscopic and biological studies on the new symmetric Schiff base derived from 2,6-diformyl-4-methylphenol with N-aminopyrimidine. |
Sonmez M, Celebi M, Berber I |
Eur J Med Chem |
10.1016/j.ejmech.2010.01.035 |
2010 |
* |
Biotechnology |
Determination of the antimicrobial properties of oligo-2-hydroxy-1-naphthaldehyde. |
Yapici BM, Kaya I, Senol D |
Drug Metabol Drug Interact |
|
2005 |
* |
Pathogenicity |
Synthesis and antibacterial activity of 4-benzoyl-1-methyl-5-phenyl-1H-pyrazole-3-carboxylic acid and derivatives. |
Akbas E, Berber I, Sener A, Hasanov B |
Farmaco |
10.1016/j.farmac.2004.09.003 |
2004 |
* |
Enzymology |
Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6-glucosidase. |
Watanabe K, Miyake K, Suzuki Y |
Biosci Biotechnol Biochem |
10.1271/bbb.65.2058 |
2001 |
* |
Enzymology |
Clustered proline residues around the active-site cleft in thermostable oligo-1,6-glucosidase of Bacillus flavocaldarius KP1228. |
Kashiwabara S, Matsuki Y, Kishimoto T, Suzuki Y |
Biosci Biotechnol Biochem |
10.1271/bbb.62.1093 |
1998 |
* |
Enzymology |
The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization. |
Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y |
J Mol Biol |
10.1006/jmbi.1997.1018 |
1997 |
* |
Enzymology |
Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues. |
Watanabe K, Kitamura K, Suzuki Y |
Appl Environ Microbiol |
10.1128/aem.62.6.2066-2073.1996 |
1996 |
* |
Enzymology |
Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule. |
Watanabe K, Masuda T, Ohashi H, Mihara H, Suzuki Y |
Eur J Biochem |
10.1111/j.1432-1033.1994.tb20051.x |
1994 |
* |
Proteome |
Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis. |
Kizaki H, Hata Y, Watanabe K, Katsube Y, Suzuki Y |
J Biochem |
10.1093/oxfordjournals.jbchem.a124097 |
1993 |
* |
Enzymology |
Assignment of Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase I to an exo-alpha-1,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in N-terminal sequence and in structural parameters calculated from the amino acid composition. |
Suzuki Y, Yonezawa K, Hattori M, Takii Y |
Eur J Biochem |
10.1111/j.1432-1033.1992.tb16775.x |
1992 |
* |
Enzymology |
Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006. |
Watanabe K, Chishiro K, Kitamura K, Suzuki Y |
J Biol Chem |
S0021-9258(18)54226-5 |
1991 |
* |
Enzymology |
Overproduction, purification and crystallization of Bacillus cereus oligo-1,6-glucosidase. |
Watanabe K, Kitamura K, Hata Y, Katsube Y, Suzuki Y |
FEBS Lett |
10.1016/0014-5793(91)81264-9 |
1991 |
* |
Enzymology |
Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene. |
Watanabe K, Kitamura K, Iha H, Suzuki Y |
Eur J Biochem |
10.1111/j.1432-1033.1990.tb19267.x |
1990 |
* |
Enzymology |
Purification and characterization of Bacillus coagulans oligo-1,6-glucosidase. |
Suzuki Y, Tomura Y |
Eur J Biochem |
10.1111/j.1432-1033.1986.tb09723.x |
1986 |
* |