398 Form Pages

BIOGRAPHICAL SKETCH[JG1] Provide the following information for the key personnel in the order listed for Form Page 2. Follow the sample format for each person. DO NOT EXCEED FOUR PAGES.

NAME Irina I. Serysheva		POSITION TITLE Assistant Professor
EDUCATION/TRAINING (Begin with baccalaureate or other initial professional education, such as nursing, and include postdoctoral training.)
INSTITUTION AND LOCATION	DEGREE (if applicable)		YEAR(s)	FIELD OF STUDY
M.V. Lomonosov State University, Moscow	B.S.		1976	Biochemistry
Russia	M.Sc.		1978	Virology
A.N.Bach Institute of Biochemistry, Moscow
Russia	Ph.D.		1984	Biochemistry
	Postdoc.		1984-1986	Molecular Biology

Positions and Honors

1984-1992 Postdoctoral Fellow, Research Scientist, Senior Research Fellow, Senior Scientist,

A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia

02/1990 -

08/1990 Visiting Scientist, Department of Microbiology, UCLA, Los Angeles, CA

1990-1991 Visiting Scientist, Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA

1992-1994 Research Associate, Department of Biochemistry, Baylor College of Medicine,
Houston, TX

1994-1997 Instructor, Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, TX

1994 -1996 Baylor College of Medicine Junior Faculty Seed Grant Award Recipient

1997-present Assistant Professor, Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, TX

1998-2002 American Heart Association, National Scientist Development Grant recipient

2001-2005 Muscular Dystrophy Association Research Grants Recipient

Selected peer-reviewed publications

Serysheva, I. I., D. J. Bare, S. L. J. Ludtke, C. A. Kettlun, W. Chiu & G. L. Mignery (2003). Structure of the Type 1 Inositol 1,4,5-trisphosphate Receptor Revealed by Electron Cryomicroscopy. J.Biol.Chem., 278, 21319-21322.

Baker M. L., I. I. Serysheva, S. Sencer, Y. Wu, S. L. Ludtke, W. Jiang, S. L. Hamilton & W. Chiu (2002). The skeletal muscle Ca²⁺ release channel has an oxidoreductase-like domain. PNAS, 99, 12155 -12160.

Serysheva, I. I., S. L. Ludtke, M. R. Baker, W. Chiu & S. L. Hamilton (2002). Structure of the voltage-gated L-type Ca²⁺ channel by electron cryo-microscopy. PNAS, 99, 10370-10375.

Pate, P., Mocha-Morales, J., Wu, Y., Zhang, J. Z., Rodney, G. G., Serysheva, I. I., Williams, B.Y.,

Anderson, M. E. & S. L. Hamilton (2000). Determinants for Calmodulin Binding on Voltage-dependent Ca²⁺ Channels. J.Biol.Chem., 275, 39786-39782.

Serysheva, I. I., M. Schatz, M. Van Heel, W. Chiu & S. L. Hamilton (1999). Structure of the Skeletal Muscle Calcium Release Channel Activated with Ca²⁺ and AMP-PCP. Biophys. J., 77, 1936-1944

Orlova, E. V., I. I. Serysheva, M.van Heel, S. L. Hamilton & W.Chiu (1996). Two structural configurations of the skeletal muscle calcium release channel. Nature Struct. Biol., 3 no.16 , 547 - 552.

Serysheva I. I., E. V. Orlova, W. Chiu, M. B. Sherman, S. L. Hamilton & M. van Heel (1995). Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel. Nature Struct. Biol., 2, no.1, 18-24.

Chang, Z., T. P. Primm, J. Jakana, I. H. Lee, I. I. Serysheva, W. Chiu, H. F. Gilbert & F. A. Quiocho (1996). Mycobacterium tuberculosis 16-kDa antigen (Hsp 16.3) functions as oligomeric structure in vitro to supress thermal aggregation. J.Biol.Chem., 271, 7218 - 7223.

Serysheva, I. I., A. I. Tourkin, I. V. Bartish & B. F. Poglazov (1992). GTP-ase activity of bacteriophage T4 sheath protein. J. Mol. Biol.,223, 23-25.

Research Support (during the last three years)

9730258N (SDG, American Heart Association, National) (PI: Serysheva) 01/01/98 – 12/31/02

Structural Analysis of Cardiac Ca²⁺ Release channel in Different Functional States

The major goal of this project is to define the 3D structure of the Ca²⁺ release channel from the sarcoplasmic reticulum of the cardiac muscle.

AR41729 (NIH/NIAMS) (Co-Investigator: Serysheva) 06/01/96 – 03/31/03

Structural Analysis of Ca²⁺ Release Channel

The major goals of this project is to correlate the 3D structure of the Ca²⁺ release channel with its functions and to elucidate the mechanisms by which mutations in the skeletal muscle Ca²⁺ release channel produce modulation of channel.

Research Grant (PI: Serysheva) 01/01/01 – 12/31/02 Muscular Dystrophy Association

Structural analysis of the skeletal muscle dihydropyridine receptor

This project aims to resolve the 3D structure of the skeletal muscle L-type Ca²⁺ channel by using electron cryomicroscopy and computer reconstruction techniques.

Research Grant (PI: Serysheva) 01/01/03 – 12/31/05 Muscular Dystrophy Association

Structure-function correlations within skeletal muscle L-type Ca²⁺ channel

The major goal of this project is to determine the membrane topology of the L-type Ca²⁺ channel and to map the interaction sites of with the ryanodine receptor (Ca²⁺ release channel) from the skeletal muscle SR.