Dear Member of Recruiter Committee, I am writing this letter for a position of Assistant Professor/ Research Scientist in Biochemistry, Clinical-Biochemistry, Biotechnology and Molecular Biology. In brief, I am PhD in Medicinal Biochemistry and completed several successful projects as a Postdoctoral Scientist in different discipline of Biochemistry like Molecular Biology of Aging, Alternative splicing in human diseases, Epigenetic regulation in liver and breast cancer from India and USA. I came back to India in April 2010 and worked as a CSIR-Pool Scientist in the area of chromatin remodeling in breast cancer. My tenure has been completed recently. Thus, I am looking for a faculty position of Assistant Professor/ Research Scientist in Biochemistry, Clinical-Biochemistry, Biotechnology and Molecular Biology. I am highly interested to trend the graduate students in Biochemistry, Biotechnology and Molecular Biology. Besides, I am very much motivated to lead projects in the area of Cancer Biology. Thus, I respectfully submit this letter of application, for I believe my experiences and commitment for teaching and research make me well qualified to meet the needs of Assistant Professor/ Research Scientist in Biochemistry, Clinical-Biochemistry, Biotechnology and Molecular Biology. I am well acquainted with the molecular techniques associated with DNA, RNA and proteins research. Besides, I am expertise in planning and execution of experiments, mentoring PhD students, interpreting data, as well as writing and data preparation for manuscript publication. During my doctorate and post doctorate time, I taught graduate and postgraduate students on behalf of my mentors. I am well organized, goal oriented; self motivated research scientist and committed to train the student in area of Clinical Biochemistry and Molecular Biology along with lead research work in the area of Cancer Biology. I would appreciate for an interview opportunity to discuss about my background, qualification and expertise that may fit for the position.

1. Dr. Ravi S Pandey
Objective
I am looking for a Faculty/Research Scientist position in the area epigenetic regulation in breast
cancer along with teaching opportunity to trend the graduate student in Biochemistry, Biotechnology
and Molecular Biology
Educational Qualification
Doctor of Philosophy in Medicinal Biochemistry* : November 2004
Institute of Medical Sciences Banaras Hindu University, India.
Master of Science in Biochemistry 74.94% : May 1999
School of Biochemistry, Devi Ahilya University, India.
Bachelor of Science in Botany and Chemistry 56.61% : June 1996
Udai Pratap College, Purvanchal University, India.
CSIR-National Eligibility Test (NET)-Lectureship : July 2001
Council of Scientific & Industrial Research, New Delhi. India.
Graduate Aptitude Test in Engineering GATE-Fellowship : March 2001
Indian Institute of Technology, Kanpur, India
*Thesis Title: Biochemical study of macrophage function in terms of atherosclerosis and
inflammation with reference to dietary components and medicinal plants
Employment Experience/ Postdoctoral Affiliation
Pool Scientist : December 2010- December 2012
Cancer Research Lab, Institute of Life Sciences, India
Senior Research Associate : May 2010- August 2010
Cancer Research Lab, Institute of Life Sciences, India
Postdoctoral fellow : September 2008- March 2010
School of Medicine-University of Missouri, USA
Postdoctoral Associate : November 2007-August 2008
Department of Biomedical Sciences, Iowa State University, USA
Senior Research Fellow/ Research Associate : November 2004-October 2007
Gene Function & Regulation, Institute of Life Sciences, India
Technical experience
• Primary and cell line culture, transfection of siRNA, anti-sense oligos, isolation of RNA,
DNA and proteins
Dr. R. S. Pandey- Bio-data Tuesday, March 19, 2013 Page 1
Ex-Pool Scientist
Kushahan Adalpura
Mirzapur 231 304 UP INDIA
Mobile : + 91-872-652-1684
EmailEmail : dr.spandey@yahoo.com

2. • Gene microarray analysis, real-time PCR, western and northern blot analysis
• Identification of differential expression of genes using Differential display-PCR, sequencing
• Cloning, expression, purification and in-gel enzyme assay of recombinant protein.
• Molecular characterization of gene-promoters by DNase I footprinting, transient
transfection and luciferase assay of promoter-reporter constructs, and DNA-protein
interactions (EMSA and super shift assay).
• Animal model experience- Versed with albino rats and rabbits for in vivo model of
atherosclerosis.
Memberships in Scientific organizations
References
Shivendra D. Shukla, Margaret Proctor Mulligan Professor
Department of Medical Pharmacology & Physiology, University of Missouri-School of Medicine,
Columbia MO- 65212 USA
: 001/ 573/ 882/ 2740 : 001/ 573/ 882/ 4276 : shuklasd@missouri.edu
Nani G. Ghoshal, Emeritus Professor
Dept. of Biomedical Sciences, 2086 College of Veterinary Medicine, Iowa State University
Ames, IA 50011 USA
: 001/ 515/ 294/2433 : 001/ 294/ 2315 : nghoshal@iastate.edu
Yamini B. Tripathi, Professor
Department of Medicinal Chemistry, Banaras Hindu University, Varanasi -751023 India
: 0091/ 542 / 230/ 7547 : 0091/ 542/ 236/ 6566 : yaminiok@yahoo.com
Deepak Bhatnagar, Professor
School of Biochemistry,Khandwa Road, D.A.University- Indore 452017 India
: 0091/ 731/ 2367262 : 0091/ 731/ 2470372 : dbhatnagar1@rediffmail.com
Dr. R. S. Pandey- Bio-data Tuesday, March 19, 2013 Page 2
 American Society of Biochemistry & Molecular Biology : October 2008- present
 American Society for Pharmacology & Experimental Therapeutics : October 2008- present
 The Science Advisory Board : March 2007- present
 International Atherosclerosis Society : September 2002- present
 Indian Society for Atherosclerosis Research : September 2002- present
 Indian Society of Cell Biology : February 2006- present

3. Publications
Choudhury M, Pandey RS, Clemens DL, Davis JW, Lim RW, Shukla SD: Knockdown of gcn5
histone acetyltransferase diminishes ethanol induced histone acetylation and affects differential
expression of genes in human hepatoma cells. Alcohol, 2011; 45: 311-324.IF: 2.41
Rath B, Pandey RS, Debata PR, Maruyama N, Supakar PC: Molecular characterization of senescence
marker protein-30 gene promoter: Identification of repressor elements and functional nuclear
factor binding sites. BMC Mol Biol. 2008; 9:43. IF: 2.86
Panda H, Pandey RS, Debata PR, Supakar PC: Cloning, expression, functional analysis of rat liver
cytosolic inorganic pyrophosphatase gene and characterization of its functional promoter. Gene
Expr. 2007, 14: 13-22. IF: 1.31
Panda H, Pandey RS, Debata PR, Supakar PC: Age-dependent differential expression and activity of
rat liver cytosolic inorganic pyrophosphatase gene. Biogerontology 2007; 8: 517-525. IF: 3.34
Pandey SK, Sahay A, Pandey RS, Tripathi YB: Effect of Asparagus racemosus rhizome (Shatavari) on
mammary gland and genital organs of pregnant rat. Phytother. Res., 2005; 19: 721-724. IF:
2.09
Pandey RS, Singh BK, Tripathi YB: Extract of gum resins of Boswellia serrata L. inhibits
lypopolysaccharide induced nitric oxide production in rat macrophages along with
hypolipidemic property. Indian J. Exp. Biol., 2005; 43: 509-516. IF: 1.29
Tripathi YB, Singh BK, Pandey RS, Kumar M: BHUx: a patent polyherbal formulation to prevent
atherosclerosis. Evid. Based Complement. Alternat. Med., 2005; 2: 217- 221. IF: 4.77
Tripathi YB, Reddy MM, Pandey RS, Tiwari OP, Singh BK, and Reddanna P: Anti-inflammatory
property of BHUx: a polyherbal formulation to prevent atherosclerosis.
Inflammopharmacology, 2004; 12: 131-152.
Tripathi YB, Pandey RS: Semecarpus anacardium L, nuts inhibit lipopolysaccharide induced NO
Production in rat macrophages along with its hypolipidemic property. Indian J. Exp. Biol.,
2004; 42: 432-436. IF: 1.29
Dr. R. S. Pandey- Bio-data Tuesday, March 19, 2013 Page 3

4. Pattanaik N, Singh AV, Pandey RS, Singh BK, Kumar M, Dixit SK, Tripathi YB: Toxicology And
Free Radicals Scavenging Property Of Tamra Bhasma. Indian J. Clin. Biochem., 2003;18:181-
189.
Nucleic Acid Sequence
Panda H, Pandey RS, Debata PR, Supakar PC: Rattus norvegicus cytosolic inorganic pyrophosphatase
gene, promoter region and exon 1. 2006: GenBank accession number DQ978330.
Presentation
Aroor AR, Pandey RS and Shukla SD: Histone acetylation, expression of histone acetyltransferases
and histone deacetylases by ethanol binge after chronic ethanol intake (poster). ISBRA World
Congress, Paris, France Alcohol. Clin. Exp. Res., 2010; 34:
Choudhury M, Pandey RS, Clemens DL, Davis JW, Lim RW, Shukla SD: Silencing of histone
acetyltransferase GCN5 affects gene expression in human hepatoma cells: A gene array analysis
(Poster). Experimental Biology Meeting FASEB J.; 2009; 23: 585.8.
Farrell DJ, Pandey RS, Singh NN, Singh RN: In vivo selections to antisense technology: A powerful
approach to understand and correct aberrant pre-mRNA splicing (Poster). Center for Integrated
Animal Genomics, Faculty Meeting, April 24, 2008 at Iowa State University, Ames, USA .
Debata PR, Panda H, Pandey RS Supakar PC: Gene expression profiling of rat liver and kidney during
aging. 29Th
All india cell biology conference (AICBC), January 18-20, 2006, ITRC,
Lucknow: Abstract book pp. 83.
Pandey RS, Tripathi YB: Evaluation of antiatherogenic mechanism of commiphora mukul and
Terminalia arjuna. 2nd
International conference of the international society for ayurveda &
health (ISAH), November 20-22, 2005, BHU, Varanasi: Abstract book pp. 44.
Pandey RS, Tripathi YB: Role of saturated fat rich diet on stress induced changes in antioxidant
parameters in rats. 16th
Annual conference of indian society for atherosclerosis research (ISAR)
December 1-3, 2003 BHU, Varanasi: Abstract book pp. 57-58.
Tripathi YB, Pandey RS, Singh BK, Kumar M, Reddy M, Reddana P: Anti-inflammatory action of
BHUx: a patented polyherbal formulation to prevent atherosclerosis. (ISAR) December 1-3,
2003, BHU, Varanasi: Abstract book pp. 57.
Dr. R. S. Pandey- Bio-data Tuesday, March 19, 2013 Page 4

5. Tripathi YB, Singh BK, Gadam P, Pandey RS, Upadhyay AK, Aprajita, Kumar M: The response of
BHUx on smoking induced atherosclerosis in cholesterol fed rabbits. 2nd
WATCH September
29- October 3, 2002 New Delhi: Abstract book pp. 40.
Ravi S. Pandey
Dr. R. S. Pandey- Bio-data Tuesday, March 19, 2013 Page 5

6. Future Research Interest
Chromatin Remodeling in Breast Cancer
Alcohol consumption is an increased risk factor for hormone-dependent breast cancer but
the underlying molecular mechanisms are unknown. Several studies suggested that ethanol could activate
the estrogen signaling pathway. During my tenure as a pool scientist, in an in vitro analysis, exposure of
MCF-7 breast cancer cells to ethanol induced an increase in the mRNA level of ER-α, ER-β, E2F1, while no
significant change was observed in E2F4, AMPK-α2. The transcription factor E2F regulates the expression
of genes essential for cell proliferation and apoptosis. During normal proliferation, PI3K/Akt signaling
blocks E2F1 induced apoptosis. Estrogen Receptor blocker ICI 182 780 may antagonize the effect of E2 and
ethanol by reducing the expression of E2F1 more than 80%. Thus, it has been hypothesize that ethanol might
be inducing E2F1 expression by ER signaling pathways. However, the initial finding require to confirm at
protein level followed by silencing and over expression of ER-α before estrogen and/or ethanol treatment. In
same experimental condition, GCN5 mRNA was found to be induced by ethanol and estrogen and the effect
was down-regulated by ER-α antagonist ICI 182 780. In late G1 and early S phase, CDC6 is found in a
complex also containing Cyclin A, cyclin-dependent kinase (CDK)-2 and the acetyltransferase general
control nonderepressible 5 (GCN5). Previous studies depict that GCN5 specifically acetylates CDC6 at three
lysine residues flanking its cyclin-docking motif, and this modification is crucial for the subsequent
phosphorylation of the protein by Cyclin A–CDKs at a specific residue close to the acetylation site. GCN5-
mediated acetylation and site-specific phosphorylation of CDC6 are both necessary for the relocalization of
the protein to the cell cytoplasm in the S phase, as well as to regulate its stability. Further study on alteration
in the balance of the E2F1 regulated genes could help in deciphering the molecular mechanism of ethanol
and estrogen action in breast cancer cells.
Three major areas will be focused:
1. Molecular mechanism of GCN5 activation by ethanol and 17β- estradiol in MCF-7 cells
2. Identification and functional analysis of maximally acetylated protein in MCF-7 cells
3. Identification of molecular mechanism of E2F1 activation and it functional role in breast
cancer cells.
Ravi S. Pandey
Dr. R. S. Pandey- Bio-data Tuesday, March 19, 2013 Page 6

7. Future Research Interest
Chromatin Remodeling in Breast Cancer
Alcohol consumption is an increased risk factor for hormone-dependent breast cancer but
the underlying molecular mechanisms are unknown. Several studies suggested that ethanol could activate
the estrogen signaling pathway. During my tenure as a pool scientist, in an in vitro analysis, exposure of
MCF-7 breast cancer cells to ethanol induced an increase in the mRNA level of ER-α, ER-β, E2F1, while no
significant change was observed in E2F4, AMPK-α2. The transcription factor E2F regulates the expression
of genes essential for cell proliferation and apoptosis. During normal proliferation, PI3K/Akt signaling
blocks E2F1 induced apoptosis. Estrogen Receptor blocker ICI 182 780 may antagonize the effect of E2 and
ethanol by reducing the expression of E2F1 more than 80%. Thus, it has been hypothesize that ethanol might
be inducing E2F1 expression by ER signaling pathways. However, the initial finding require to confirm at
protein level followed by silencing and over expression of ER-α before estrogen and/or ethanol treatment. In
same experimental condition, GCN5 mRNA was found to be induced by ethanol and estrogen and the effect
was down-regulated by ER-α antagonist ICI 182 780. In late G1 and early S phase, CDC6 is found in a
complex also containing Cyclin A, cyclin-dependent kinase (CDK)-2 and the acetyltransferase general
control nonderepressible 5 (GCN5). Previous studies depict that GCN5 specifically acetylates CDC6 at three
lysine residues flanking its cyclin-docking motif, and this modification is crucial for the subsequent
phosphorylation of the protein by Cyclin A–CDKs at a specific residue close to the acetylation site. GCN5-
mediated acetylation and site-specific phosphorylation of CDC6 are both necessary for the relocalization of
the protein to the cell cytoplasm in the S phase, as well as to regulate its stability. Further study on alteration
in the balance of the E2F1 regulated genes could help in deciphering the molecular mechanism of ethanol
and estrogen action in breast cancer cells.
Three major areas will be focused:
1. Molecular mechanism of GCN5 activation by ethanol and 17β- estradiol in MCF-7 cells
2. Identification and functional analysis of maximally acetylated protein in MCF-7 cells
3. Identification of molecular mechanism of E2F1 activation and it functional role in breast
cancer cells.
Ravi S. Pandey
Dr. R. S. Pandey- Bio-data Tuesday, March 19, 2013 Page 6