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Results: 1-10 |
Results: 10
FAVORABLE CHANGE IN MAMMOGRAPHIC PARENCHYMAL PATTERNS AND BREAST-CANCER RISK-FACTORS
Authors: SALMINEN T HAKAMA M HEIKKILA M SAARENMAA I
Citation: T. Salminen et al., FAVORABLE CHANGE IN MAMMOGRAPHIC PARENCHYMAL PATTERNS AND BREAST-CANCER RISK-FACTORS, International journal of cancer, 78(4), 1998, pp. 410-414
RELATIONSHIP BETWEEN IMMOBILIZED ARTIFICIAL MEMBRANE CHROMATOGRAPHIC RETENTION AND THE BRAIN PENETRATION OF STRUCTURALLY DIVERSE DRUGS
Authors: SALMINEN T PULLI A TASKINEN J
Citation: T. Salminen et al., RELATIONSHIP BETWEEN IMMOBILIZED ARTIFICIAL MEMBRANE CHROMATOGRAPHIC RETENTION AND THE BRAIN PENETRATION OF STRUCTURALLY DIVERSE DRUGS, Journal of pharmaceutical and biomedical analysis, 15(4), 1997, pp. 469-477
STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF SUBSTITUTIONS AT THE TYROSINE-55 LYSINE-104 HYDROGEN-BOND IN ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE
Authors: FABRICHNIY IP KASHO VN HYYTIA T SALMINEN T HALONEN P DUDARENKOV VY HEIKINHEIMO P CHERNYAK VY GOLDMAN A LAHTI R COOPERMAN BS BAYKOV AA
Citation: Ip. Fabrichniy et al., STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF SUBSTITUTIONS AT THE TYROSINE-55 LYSINE-104 HYDROGEN-BOND IN ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE, Biochemistry, 36(25), 1997, pp. 7746-7753
EFFECT OF E20D SUBSTITUTION IN THE ACTIVE-SITE OF ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE ON ITS QUATERNARY STRUCTURE AND CATALYTIC PROPERTIES
Authors: VOLK SE DUDARENKOV VY KAPYLA J KASHO VN VOLOSHINA OA SALMINEN T GOLDMAN A LAHTI R BAYKOV AA COOPERMAN BS
Citation: Se. Volk et al., EFFECT OF E20D SUBSTITUTION IN THE ACTIVE-SITE OF ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE ON ITS QUATERNARY STRUCTURE AND CATALYTIC PROPERTIES, Biochemistry, 35(15), 1996, pp. 4662-4669
CRYSTALLOGRAPHIC IDENTIFICATION OF METAL-BINDING SITES IN ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE
Authors: KANKARE J SALMINEN T LAHTI R COOPERMAN BS BAYKOV AA GOLDMAN A
Citation: J. Kankare et al., CRYSTALLOGRAPHIC IDENTIFICATION OF METAL-BINDING SITES IN ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE, Biochemistry, 35(15), 1996, pp. 4670-4677
NEW CRYSTAL FORMS OF ESCHERICHIA-COLI AND SACCHAROMYCES-CEREVISIAE SOLUBLE INORGANIC PYROPHOSPHATASES
Authors: HEIKINHEIMO P SALMINEN T LAHTI R COOPERMAN B GOLDMAN A
Citation: P. Heikinheimo et al., NEW CRYSTAL FORMS OF ESCHERICHIA-COLI AND SACCHAROMYCES-CEREVISIAE SOLUBLE INORGANIC PYROPHOSPHATASES, Acta crystallographica. Section D, Biological crystallography, 51, 1995, pp. 399-401
DISSOCIATION OF HEXAMERIC ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE INTO TRIMERS ON HIS-136-]GLN OR HIS-140-]GLN SUBSTITUTION AND ITS EFFECT ON ENZYME CATALYTIC PROPERTIES
Authors: BAYKOV AA DUDARENKOV VY KAPYLA J SALMINEN T HYYTIA T KASHO VN HUSGAFVEL S COOPERMAN BS GOLDMAN A LAHTI R
Citation: Aa. Baykov et al., DISSOCIATION OF HEXAMERIC ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE INTO TRIMERS ON HIS-136-]GLN OR HIS-140-]GLN SUBSTITUTION AND ITS EFFECT ON ENZYME CATALYTIC PROPERTIES, The Journal of biological chemistry, 270(51), 1995, pp. 30804-30812
STRUCTURE AND FUNCTION-ANALYSIS OF ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE - IS A HYDROXIDE ION THE KEY TO CATALYSIS
Authors: SALMINEN T KAPYLA J HEIKINHEIMO P KANKARE J GOLDMAN A HEINONEN J BAYKOV AA COOPERMAN BS LAHTI R
Citation: T. Salminen et al., STRUCTURE AND FUNCTION-ANALYSIS OF ESCHERICHIA-COLI INORGANIC PYROPHOSPHATASE - IS A HYDROXIDE ION THE KEY TO CATALYSIS, Biochemistry, 34(3), 1995, pp. 782-791
THE STRUCTURE OF ESCHERICHIA-COLI SOLUBLE INORGANIC PYROPHOSPHATASE AT 2.7-ANGSTROM RESOLUTION (VOL 7, PG 823, 1994)
Authors: KANKARE J NEAL GS SALMINEN T GLUMOFF T COOPERMAN BS LAHTI R GOLDMAN A
Citation: J. Kankare et al., THE STRUCTURE OF ESCHERICHIA-COLI SOLUBLE INORGANIC PYROPHOSPHATASE AT 2.7-ANGSTROM RESOLUTION (VOL 7, PG 823, 1994), Protein engineering, 7(9), 1994, pp. 1173-1173
THE STRUCTURE OF ESCHERICHIA-COLI SOLUBLE INORGANIC PYROPHOSPHATASE AT 2.7-ANGSTROM RESOLUTION
Authors: KANKARE J NEAL GS SALMINEN T GLUMHOFF T COOPERMAN BS LAHTI R GOLDMAN A
Citation: J. Kankare et al., THE STRUCTURE OF ESCHERICHIA-COLI SOLUBLE INORGANIC PYROPHOSPHATASE AT 2.7-ANGSTROM RESOLUTION, Protein engineering, 7(7), 1994, pp. 823-830
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