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Eduard Sergienko

Eduard Sergienko, Ph.D.[La Jolla]

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Director, Assay Development

(858)646-3100 ext. 3462 (phone)
esergien@sanfordburnham.org

Research

Eduard provides scientific oversight of the HTS assay development and molecular pharmacology.
Biography

Eduard recieved his Ph.D. at Lomonosov Moscow University and his postdoctoral training at Henry Poincare University and Rutgers University.

Publications

High-throughput screening of tissue-nonspecific alkaline phosphatase for identification of effectors with diverse modes of action.

Sergienko EA, Millán JL

Nat Protoc. 2010 Aug;5(8):1431-9

Identification and characterization of novel tissue-nonspecific alkaline phosphatase inhibitors with diverse modes of action.

Sergienko E, Su Y, Chan X, Brown B, Hurder A, Narisawa S, Millán JL

J Biomol Screen. 2009 Aug;14(7):824-37

New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme.

Sergienko EA, Jordan F

Biochemistry. 2002 Mar 26;41(12):3952-67

Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values.

Sergienko EA, Jordan F

Biochemistry. 2001 Jun 26;40(25):7382-403

Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products.

Sergienko EA, Jordan F

Biochemistry. 2001 Jun 26;40(25):7369-81

Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase.

Sergienko EA, Wang J, Polovnikova L, Hasson MS, McLeish MJ, Kenyon GL, Jordan F

Biochemistry. 2000 Nov 14;39(45):13862-9

Kinetic mechanism of the glycogen-phosphorylase-catalysed reaction in the direction of glycogen synthesis: co-operative interactions of AMP and glucose 1-phosphate during catalysis.

Sergienko EA, Srivastava DK

Biochem J. 1997 Nov 15;328 ( Pt 1):83-91

A continuous spectrophotometric method for the determination of glycogen phosphorylase-catalyzed reaction in the direction of glycogen synthesis.

Sergienko EA, Srivastava DK

Anal Biochem. 1994 Sep;221(2):348-55

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Eduard Sergienko's Research Focus

Eduard provides scientific oversight of the HTS assay development and molecular pharmacology at the Conrad Prebys Center for Chemical Genomics. He brings diverse expertise and skills acquired in drug discovery and chemical biology fields. Eduard joined Sanford-Burnham Medical Research Institute in 2005 to establish and lead the assay development facility that is an integral part of the Conrad Prebys Center for Chemical Genomics. The facility could also be accessed directly on a fee-for-service basis.

About Eduard Sergienko

Experience

Prior to joining Sanford-Burnham Eduard Sergienko was at Triad Therapeutics Inc., a company pioneering NMR- and enzymology-guided fragment-based drug discovery approaches. Dr. Sergienko joined Triad Therapeutics in 2001 and served as Enzymology group leader and member of several drug discovery project teams. The work of his group was instrumental in identification, optimization and characterization of a preclinical candidate sold by Triad Therapeutics to Novartis Pharma AG (Switzerland) currently undergoing clinical trials. Dr. Sergienko has over 20 years of experience in the field of biochemistry, with an emphasis on assay design and mechanistic enzymology. He received his Ph.D. in Biochemistry from the Lomonosov Moscow University (Russia), where his doctoral thesis focused on the role of posttranslational modifications in regulation of glycolytic enzymes. He furthered his expertise through training as a post-doctoral fellow at Henry Poincare University, France, and Rutgers University, New Jersey focusing on mechanistic enzymology, enzyme kinetics and assay design and development.

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Eduard Sergienko

Eduard Sergienko, Ph.D.[La Jolla]

Research

Biography

Publications

High-throughput screening of tissue-nonspecific alkaline phosphatase for identification of effectors with diverse modes of action.

Identification and characterization of novel tissue-nonspecific alkaline phosphatase inhibitors with diverse modes of action.

New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme.

Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values.

Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products.

Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase.

Kinetic mechanism of the glycogen-phosphorylase-catalysed reaction in the direction of glycogen synthesis: co-operative interactions of AMP and glucose 1-phosphate during catalysis.

A continuous spectrophotometric method for the determination of glycogen phosphorylase-catalyzed reaction in the direction of glycogen synthesis.

Discovery of a Plasmodium falciparum glucose-6-phosphate dehydrogenase 6-phosphogluconolactonase inhibitor (R,Z)-N-((1-ethylpyrrolidin-2-yl)methyl)-2-(2-fluorobenzylidene)-3-oxo-3,4-dihydro-2H-benzo[b][1,4]thiazine-6-carboxamide (ML276) that reduces parasite growth in vitro.

Eduard Sergienko's Research Focus

About Eduard Sergienko

Experience

Become a Partner / Donate

Social Media

Contact

(858)646-3100 ext. 3462 (phone)
esergien@sanfordburnham.org

Mailing List

Eduard Sergienko

Eduard Sergienko, Ph.D.[La Jolla]

Research

Biography

Publications

High-throughput screening of tissue-nonspecific alkaline phosphatase for identification of effectors with diverse modes of action.

Identification and characterization of novel tissue-nonspecific alkaline phosphatase inhibitors with diverse modes of action.

New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme.

Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values.

Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products.

Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase.

Kinetic mechanism of the glycogen-phosphorylase-catalysed reaction in the direction of glycogen synthesis: co-operative interactions of AMP and glucose 1-phosphate during catalysis.

A continuous spectrophotometric method for the determination of glycogen phosphorylase-catalyzed reaction in the direction of glycogen synthesis.

Discovery of a Plasmodium falciparum glucose-6-phosphate dehydrogenase 6-phosphogluconolactonase inhibitor (R,Z)-N-((1-ethylpyrrolidin-2-yl)methyl)-2-(2-fluorobenzylidene)-3-oxo-3,4-dihydro-2H-benzo[b][1,4]thiazine-6-carboxamide (ML276) that reduces parasite growth in vitro.

Eduard Sergienko's Research Focus

About Eduard Sergienko

Experience

Become a Partner / Donate

Social Media

Contact

(858)646-3100 ext. 3462 (phone)esergien@sanfordburnham.org

Mailing List

(858)646-3100 ext. 3462 (phone)
esergien@sanfordburnham.org