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Pankaj Vidyadhar Alone
Pankaj Vidyadhar Alone, Assistant Professor Ph.D. in 2001 from National Institute of Immunology, New Delhi |
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Specialisation
Molecular biology of protein biosynthesis.
Research Interest
Protein translation is an important step in the life cycle of cells where
genetic information is converted into functional protein information.
Protein biosynthesis is a sophisticate multistep, multifactorial process
and consumes 30-50% of cellular energy. It was thought that all the
problems in protein biosynthesis had been addressed in 1970s. However, the
emergence of new technologies, refinement in ribosome structure by cryo-EM and X-ray methods and discoveries of new translation factors and their structures are contributing to new understanding of the fundamentals of the information decoding pathway. The discoveries of IRES in pathogenic viral protein synthesis, the presence of translation control element at the 5' or 3' UTR of mRNA, miRNA, siRNA and P-bodies which controls the dynamics of protein expression have given new dimensions to this field.
Protein biosynthesis is now-a-days increasingly linked to inherited
diseases, cancer, diabetes, obesity, embryonic development, learning and
memory formation. Numerous antibiotics and toxins are known to target the
translation apparatus. In order to translate the knowledge acquired into
"translational research" we need an in-depth understanding of mechanism of
protein biosynthesis.
My research interest is to understand the regulation and mechanism of
open reading frame selection in yeast model using range of genetic,
biochemical and biophysical techniques.
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Selected publications
- Alone PV, Cao C and Dever TE. Translation initiation factor eIF2γ mutants alter start codon selection independent of Met-tRNAiMet binding. (2008) Mol Cell Biol. 28 (22): 6877-88.
- Alone PV and Garg LC. Secretory and GM1 receptor binding role of N-Terminal end of LTB in Vibrio Cholerae. (2008) Biochem Biophy Res Comm. 376 (4): 770-4.
- Alone PV, Malik G, Krishnan A and Garg LC. Deletion mutations in N-terminal α1 helix render heat labile enterotoxin B subunit susceptible
to degradation. (2007) Proc Natl Acad Sci (USA). 104 (41): 16056-61
- Alone PV and Dever TE. Direct binding of translation initiation factor eIF2γ -G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2Bε. (2006) J Biol Chem. 281(18):12636-44.
- Roll-Mecak A, Alone P, Cao C, Dever TE and Burley SK. X-ray structure of translation initiation factor eIF2γ: implications for tRNA and eIF2α binding, (2004) J Biol Chem. 279 (11):10634-42.
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