Dr. Uttam Pal, PhD - S. N. Bose National Centre for Basic Sciences - Project Scientist

Dr. Uttam Pal

PhD

S. N. Bose National Centre for Basic Sciences

Project Scientist

Kolkata, West Bengal | India

Main Specialties: Chemistry

Additional Specialties: Computational Chemistry

ORCID logohttps://orcid.org/0000-0003-2110-4610


Top Author

Dr. Uttam Pal, PhD - S. N. Bose National Centre for Basic Sciences - Project Scientist

Dr. Uttam Pal

PhD

Introduction

I develop the computational models of small molecules and chemical processes using quantum or classical mechanics. I also study the biomolecules such as proteins and nucleic acids and their interactions with small molecules. How the drug molecules work, how do they cease to work and how we can develop new drugs are the areas I am exploring through my research.

Primary Affiliation: S. N. Bose National Centre for Basic Sciences - Kolkata, West Bengal , India

Specialties:

Additional Specialties:

Research Interests:


View Dr. Uttam Pal’s Resume / CV

Education

Jan 2011 - Aug 2016
Jadavpur University
Ph.D.
Chemistry
Aug 2008 - Jul 2010
University of Calcutta
M.Sc.
Biophysics & Molecular Biology
Jul 2005 - Jul 2008
Presidency University
B.Sc.
Physiology

Experience

Jun 2018
Saha Institute of Nuclear Physics
Research Assistant
Chemical Sciences Division
Nov 2016
CSIR-Indian Institute of Chemical Biology
Project Assistant
Structural Biology
Feb 2011 - Feb 2016
CSIR-Indian Institute of Chemical Biology
DST-INSPIRE (Innovation in Science Pursuit for Inspired Research) Fellow
Structural Biology
Feb 2011 - Jan 2016
Indian Institute of Chemical Biology CSIR
INSPIRE (Innovation in Science Pursuit for Inspired Research) Fellow
Structural Biology & Bioinformatics
Jan 2011 - Jan 2011
CSIR-Indian Institute of Chemical Biology
CSIR-Junior Research Fellow
Structural Biology
May 2009 - Jul 2009
Saha Institute of Nuclear Physics
Summer Intern
Biophysics Division
Jul 2018
SN Bose National Centre for Basic Sciences
Project Scientist
Technical Research Centre

Publications

84Publications

630Reads

23Profile Views

70PubMed Central Citations

Encapsulation of Thymol in cyclodextrin nano-cavities: A multi spectroscopic and theoretical study.

Spectrochim Acta A Mol Biomol Spectrosc 2019 Feb 12;208:339-348. Epub 2018 Oct 12.

Department of Chemistry, University of Calcutta, 92, A. P. C. Road, Kolkata 700 009, India.

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http://dx.doi.org/10.1016/j.saa.2018.10.011DOI Listing
February 2019
4 Reads
2.353 Impact Factor

STRUCTURAL INTRICACY OF DISORDERED REGIONS IN TRANSCRIPTION FACTORS IMPARTING COLON CANCER

Transcription factors (TFs) linked to cancer contains a significant amount of disordered segments and the dynamics as well as coupling of it with partner molecules are keys in the processes of recognization and many other cellular activities. However, the sequence distribution, composition and the structural adaptability of TFs in the presence of other interacting small and large macromolecules such as nucleic acids, lipids and other proteins are not well understood. In a recent article (Specific DNA Sequences Allosterically Enhance Protein–Protein Interaction in a Transcription Factor, Phys. Chem. Chem. Phys.) we showed that a small fluctuation in energetic and related conformational adaptation is a key in the recognition of multiple DNA sequences by TFs. In the current investigation we determined and showed the amino acid residue distribution, intrinsic characteristics, conformational adaptability of the disorder regions and their similarity among the TFs which are linked to colon cancer. About 38% of the residues in TFs in average found to belong in the disordered region (DoR) and the abundance of these DoRs follows a Poisson distribution pattern with an expectancy value of 12. Interestingly, the size (length) distribution of the individual DoR also follows a similar statistical pattern. The computational analysis further establishes the tertiary structure of many of the TFs by homology modeling and, it was observed that the TFs with disordered content less than 70% can attain different kind of tertiary folds. However, a significant segments preferred to remain as disordered (coiled coil) and found to localize preferentially on the surface of the proteins. This surface localization suggested interactive and functional links of the disordered regions with proteins and genomic materials involves in cell function and other biological activities. The presence and their localization may thus aid in the understanding of eukaryotic gene transcription machinery as well as developing new drugs targeting the disorder prone regions in the TFs to cure cancers and related human diseases.

https://doaj.org/article/7e1abaed242447a88e44bfeaccc61f54

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2018
2 Reads

PATTERN BASED DETECTION OF POTENTIALLY DRUGGABLE BINDING SITES BY LIGAND SCREENING

This article describes an innovative way of finding the potentially druggable sites on a target protein, which can be used for orthosteric and allosteric lead detection in a single virtual screening setup. Druggability estimation for an alternate binding site other than the canonical ligand-binding pocket of an enzyme is rewarding for several inherent benefits. Allostery is a direct and efficient way of regulating biomacromolecule function. The allosteric modulators can fine-tune protein mechanics. Besides, allosteric sites are evolutionarily less conserved/more diverse even in very similarly related proteins, thus, provides high degree of specificity in targeting a particular protein. Therefore, targeting of allosteric sites is gaining attention as an emerging strategy in rational drug design. However, the experimental approaches provide a limited degree of characterization of new allosteric sites. Computational approaches are useful to analyze and select potential allosteric sites for drug discovery. Here, the use of molecular docking, which has become an integral part of the drug discovery process, has been discussed to predict the druggability of novel allosteric sites as well as the active site on target proteins by ligand screening. Genetic algorithm was used for docking and the whole protein was placed in the search space. For each ligand in the library of small molecules, the genetic algorithm was run for multiple times to populate all the druggable sites in the target protein, which was then translated into two dimensional density maps or “patterns”. High density clusters were observed for lead like molecules in these pattern diagrams. Each cluster in such a pattern diagram indicated a plausible binding site and the density gave its druggability score in terms of weighted probabilities. The patterns were filtered to find the leads for each of the druggable sites on the target protein. Such a novel pattern based analysis of the clusters provides a way to probe new druggable sites on a target protein in a much simpler setup. This structure based analysis method might help researchers to develop allosteric modulators and to identify novel target sites on drug resistant proteins.

https://doaj.org/article/3c67649a0d294ef4b5759ffca404bc18

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2018
2 Reads

Correction: Crystal-defect-induced facet-dependent electrocatalytic activity of 3D gold nanoflowers for the selective nanomolar detection of ascorbic acid.

Nanoscale 2018 Jul;10(28):13792

Chemical Sciences Division, Saha Institute of Nuclear Physics, HBNI, 1/AF Bidhannagar, Kolkata 700064, India.

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http://dx.doi.org/10.1039/c8nr90141dDOI Listing
July 2018
7 Reads
7.394 Impact Factor

Crystal-defect-induced facet-dependent electrocatalytic activity of 3D gold nanoflowers for the selective nanomolar detection of ascorbic acid.

Nanoscale 2018 Jun;10(23):11091-11102

Chemical Science Division, Saha Institute of Nuclear Physics, Kolkata, West Bengal, India.

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http://dx.doi.org/10.1039/c8nr03087aDOI Listing
June 2018
18 Reads
7.394 Impact Factor

Curcumin stably interacts with DNA hairpin through minor groove binding and demonstrates enhanced cytotoxicity in combination with FdU nucleotides.

Biochim Biophys Acta Gen Subj 2018 Mar 28;1862(3):485-494. Epub 2017 Oct 28.

Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA.

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http://dx.doi.org/10.1016/j.bbagen.2017.10.018DOI Listing
March 2018
24 Reads
4.381 Impact Factor

Structural Insight of Amyloidogenic Intermediates of Human Insulin.

ACS Omega 2018 Feb;3(2):2452-2462

Structural Biology and Bioinformatics Division, Indian Institute of Chemical Biology, Council of Scientific and Industrial Research, 4, Raja S.C. Mullick Road, Kolkata 700032, India.

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http://dx.doi.org/10.1021/acsomega.7b01776DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6045404PMC
February 2018
11 Reads

DNA Damage and Apoptosis Induction in Cancer Cells by Chemically Engineered Thiolated Riboflavin Gold Nanoassembly.

ACS Appl Mater Interfaces 2018 Feb 27;10(5):4582-4589. Epub 2018 Jan 27.

Department of Chemistry, Government General Degree College, Singur, Hooghly, West Bengal 712409, India.

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http://pubs.acs.org/doi/10.1021/acsami.7b18837
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http://dx.doi.org/10.1021/acsami.7b18837DOI Listing
February 2018
32 Reads
6.723 Impact Factor

Mesoporous silica for drug delivery: Interactions with model fluorescent lipid vesicles and live cells.

J Photochem Photobiol B 2018 Jan 1;178:19-26. Epub 2017 Nov 1.

Chemical Sciences Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700064, India.

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http://dx.doi.org/10.1016/j.jphotobiol.2017.10.023DOI Listing
January 2018
12 Reads
2.960 Impact Factor

CCDC 1493320: Experimental Crystal Structure Determination

Other ; Related Article: Supriya Das, Uttam Pal, Moumita Chatterjee, Sumit Kumar Pramanik, Biswadip Banerji, and Nakul C. Maiti|2016|J.Phys.Chem.A|120|9829|doi:10.1021/acs.jpca.6b10017 ; Abstract ; An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

https://doi.org/10.5517/ccdc.csd.cc1m3xm8

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January 2018
9 Reads

Formation of Annular Protofibrillar Assembly by Cysteine Tripeptide: Unraveling the Interactions with NMR, FTIR, and Molecular Dynamics.

J Phys Chem B 2017 07 23;121(26):6367-6379. Epub 2017 Jun 23.

Organic and Medicinal Chemistry and ‡Structural Biology and Bio-Informatics Division, CSIR-Indian Institute of Chemical Biology , 4, Raja S.C. Mullick Road, Kolkata, West Bengal 700032, India.

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http://dx.doi.org/10.1021/acs.jpcb.7b04373DOI Listing
July 2017
16 Reads

Constrained Photophysics of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one in the Bioenvironment of Serum Albumins: A Spectroscopic Endeavour Supported by Molecular Docking Analysis.

J Fluoresc 2017 Jul 22;27(4):1547-1558. Epub 2017 Apr 22.

Chemical Sciences Division, Saha Institute of Nuclear Physics, Kolkata, 700064, India.

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http://dx.doi.org/10.1007/s10895-017-2094-2DOI Listing
July 2017
13 Reads
1.930 Impact Factor

Tamarixetin 3-O-β-d-Glucopyranoside from Azadirachta indica Leaves: Gastroprotective Role through Inhibition of Matrix Metalloproteinase-9 Activity in Mice.

J Nat Prod 2017 05 11;80(5):1347-1353. Epub 2017 May 11.

Department of Natural Products, National Institute of Pharmaceutical Education and Research , Kolkata 700032, WB, India.

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http://dx.doi.org/10.1021/acs.jnatprod.6b00957DOI Listing
May 2017
19 Reads
1 Citation
3.800 Impact Factor

CCDC 1400035: Experimental Crystal Structure Determination

Other ; Related Article: Biswadip Banerji, Moumita Chatterjee, Uttam Pal, Nakul Chandra Maiti|2016|J.Phys.Chem.A|120|2330|doi:10.1021/acs.jpca.6b01078 ; Abstract ; An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

https://doi.org/10.5517/ccdc.csd.cc1hzvfr

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January 2017
9 Reads

Envisaging Structural Insight of a Terminally Protected Proline Dipeptide by Raman Spectroscopy and Density Functional Theory Analyses.

J Phys Chem A 2016 Dec 6;120(49):9829-9840. Epub 2016 Dec 6.

Structural Biology & Bio-informatics Division and ‡Organic & Medicinal Chemistry Division, CSIR-Indian Institute of Chemical Biology ; 4, Raja S.C. Mullick Road, Kolkata 700032, West Bengal, India.

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http://dx.doi.org/10.1021/acs.jpca.6b10017DOI Listing
December 2016
21 Reads
2.693 Impact Factor

Orientation of tyrosine side chain in neurotoxic Aβ differs in two different secondary structures of the peptide.

R Soc Open Sci 2016 Oct 5;3(10):160112. Epub 2016 Oct 5.

Structural Biology and Bioinformatics Division , Indian Institute of Chemical Biology, Council of Scientific and Industrial Research , 4, Raja S.c. Mullick Road, Kolkata 700032 , India.

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http://dx.doi.org/10.1098/rsos.160112DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5098961PMC
October 2016
28 Reads

A Novel Spirooxindole Derivative Inhibits the Growth of Leishmania donovani Parasites both In Vitro and In Vivo by Targeting Type IB Topoisomerase.

Antimicrob Agents Chemother 2016 10 23;60(10):6281-93. Epub 2016 Sep 23.

Infectious Diseases and Immunology Division, CSIR-Indian Institute of Chemical Biology, Jadavpur, Kolkata, India

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http://dx.doi.org/10.1128/AAC.00352-16DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5038232PMC
October 2016
30 Reads
3 Citations
4.480 Impact Factor

Silver-catalysed azide-alkyne cycloaddition (AgAAC): assessing the mechanism by density functional theory calculations.

R Soc Open Sci 2016 Sep 14;3(9):160090. Epub 2016 Sep 14.

Structural Biology and Bioinformatics Division , CSIR-Indian Institute of Chemical Biology; 4 , Raja S.C. Mullick Road, Kolkata , India.

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http://dx.doi.org/10.1098/rsos.160090DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5043300PMC
September 2016
14 Reads

Binding interaction of a gamma-aminobutyric acid derivative with serum albumin: an insight by fluorescence and molecular modeling analysis.

Springerplus 2016 19;5(1):1121. Epub 2016 Jul 19.

Structural Biology and Bioinformatics Division, Council of Scientific and Industrial Research (CSIR)-Indian Institute of Chemical Biology (IICB), Kolkata, West Bengal India.

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http://dx.doi.org/10.1186/s40064-016-2752-xDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949196PMC
August 2016
38 Reads

Conformational selection underpins recognition of multiple DNA sequences by proteins and consequent functional actions.

Phys Chem Chem Phys 2016 Aug 18;18(31):21618-28. Epub 2016 Jul 18.

Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology, 4, Raja S. C. Mullick Road, Kolkata 700 032, India.

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http://dx.doi.org/10.1039/c6cp03278hDOI Listing
August 2016
51 Reads
4.493 Impact Factor

Molecular Details of Acetate Binding to a New Diamine Receptor by NMR and FT-IR Analyses.

J Phys Chem A 2016 Apr 8;120(15):2330-41. Epub 2016 Apr 8.

Organic & Medicinal Chemistry Division and ‡Structural Biology & Bioinformatics Division, CSIR-Indian Institute of Chemical Biology , 4, Raja S.C. Mullick Road, Kolkata 700032, India.

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http://dx.doi.org/10.1021/acs.jpca.6b01078DOI Listing
April 2016
25 Reads
2.693 Impact Factor

STATISTICAL INSIGHT INTO THE BINDING REGIONS IN DISORDERED HUMAN PROTEOME

The human proteome contains a significant number of intrinsically disordered proteins (IDPs). They show unusual structural features that enable them to participate in diverse cellular functions and play significant roles in cell signaling and reorganization processes. In addition, the actions of IDPs, their functional cooperativity, conformational alterations and folding often accompany binding to a target macromolecule. Applying bioinformatics approaches and with the aid of statistical methodologies, we investigated the statistical parameters of binding regions (BRs) found in disordered human proteome. In this report, we detailed the bioinformatics analysis of binding regions found in the IDPs. Statistical models for the occurrence of BRs, their length distribution and percent occupancy in the parent proteins are shown. The frequency of BRs followed a Poisson distribution pattern with increasing expectancy with the degree of disorderedness. The length of the individual BRs also followed Poisson distribution with a mean of 6 residues, whereas, percentage of residues in BR showed a normal distribution pattern. We also explored the physicochemical properties such as the grand average of hydropathy (GRAVY) and the theoretical isoelectric points (pIs). The theoretical pIs of the BRs followed a bimodal distribution as in the parent proteins. However, the mean acidic/basic pIs were significantly lower/higher than that of the proteins, respectively. We further showed that the amino acid composition of BRs was enriched in hydrophobic residues such as Ala, Val, Ile, Leu and Phe compared to the average sequence content of the proteins. Sequences in a BR showed conformational adaptability mostly towards flexible coil structure and followed by helix, however, the ordered secondary structural conformation was significantly lower in BRs than the proteins. Combining and comparing these statistical information of BRs with other methods may be useful for high-throughput functional annotation of proteins, drug target identification and drug discovery linking protein disorder.

https://doaj.org/article/bec0fdc262df461b87689bacecbcbd4d

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January 2016
9 Reads

ORIGIN OF PROTEIN AGGREGATION: IDENTIFICATION OF SOME CHARACTERISTIC TRAITS IN STRUCTURED AND INTRINSICALLY DISORDERED PROTEINS

Proteins containing amyloidogenic regions are prone to form aggregates and undergo amyloidosis. Literature shows that both the structured and disordered proteins might be amyloidogenic. However, the amyloidogenic proteins differ from their non-amyloidogenic counterpart in various physicochemical properties and, therefore, based on these properties they can be categorized. Our analysis also indicated that the sequence composition and the physicochemical properties such as isoelectric point (pI), hydrophobicity, aliphatic index (AI) and instability index (II) of amyloidogenic and non-amylidogenic proteins differed in large extent. However, unique to our finding is that such differences appeared to be exclusive for intrinsically disordered proteins. Structured amyloidogenic proteins were found to be more similar to their non-amyloidogenic counterparts except for their sequence composition and the distribution of their isoelectric points. In this report, we have shown from the sequence analysis that the distinction between amyloidogenic and non-amyloidogenic proteins is much wider in case of disordered proteins than the structured proteins. Our finding also suggests why structured proteins that are amyloidogenic require drastic change in the solution condition to undergo amyloid formation. The results have implication in developing better algorithms for the detection and differentiation of amyloidogenic proteins.

https://doaj.org/article/4c8b85448fbc47c6b1788067d93ebf5c

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January 2016
9 Reads

Binding interaction of a novel fluorophore with serum albumins: steady state fluorescence perturbation and molecular modeling analysis.

Springerplus 2015 24;4:548. Epub 2015 Sep 24.

Structural Biology and Bioinformatics Division, Council of Scientific and Industrial Research (CSIR)-Indian Institute of Chemical Biology (IICB), Kolkata, West Bengal India.

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http://link.springer.com/content/pdf/10.1186%2Fs40064-015-13
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http://www.springerplus.com/content/4/1/548
Publisher Site
http://dx.doi.org/10.1186/s40064-015-1333-8DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4582037PMC
October 2015
15 Reads
1 Citation

Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.

PLoS One 2014 3;9(3):e89781. Epub 2014 Mar 3.

Structural Biology and Bioinformatics Division, Council of Scientific and Industrial Research (CSIR)-Indian Institute of Chemical Biology (IICB), Kolkata, India.

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0089781PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3940659PMC
January 2015
16 Reads
6 Citations
3.234 Impact Factor

Cα-H carries information of a hydrogen bond involving the geminal hydroxyl group: a case study with a hydrogen-bonded complex of 1,1,1,3,3,3-hexafluoro-2-propanol and tertiary amines.

J Phys Chem A 2014 Feb 30;118(6):1024-30. Epub 2014 Jan 30.

Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology , 4, Raja S.C. Mullick Road, Kolkata 700032, India.

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http://dx.doi.org/10.1021/jp411488aDOI Listing
February 2014
13 Reads
3 Citations
2.693 Impact Factor

pKa determination of D-ribose by Raman spectroscopy.

J Phys Chem B 2014 Jan 17;118(4):909-14. Epub 2014 Jan 17.

Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Council of Scientific and Industrial Research , 4, Raja S.C. Mullick Road, Kolkata 700032, India.

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http://dx.doi.org/10.1021/jp4092392DOI Listing
January 2014
43 Reads
1 Citation

2,2'-diphenyl-3,3'-diindolylmethane: a potent compound induces apoptosis in breast cancer cells by inhibiting EGFR pathway.

PLoS One 2013 28;8(3):e59798. Epub 2013 Mar 28.

Division of Cancer Biology and Inflammatory Disorder, Council of Scientific and Industrial Research (CSIR)-Indian Institute of Chemical Biology (IICB), Kolkata, West Bengal, India.

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0059798PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3610887PMC
January 2014
13 Reads
9 Citations
3.234 Impact Factor

pKa Determination of d-Ribose by Raman Spectroscopy

The Journal of Physical Chemistry B

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January 2014
9 Reads

Melatonin inhibits matrix metalloproteinase-9 activity by binding to its active site.

J Pineal Res 2013 May 17;54(4):398-405. Epub 2013 Jan 17.

Drug Development Diagnostics and Biotechnology Division, Department of Physiology, Indian Institute of Chemical Biology, Kolkata, India.

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http://dx.doi.org/10.1111/jpi.12034DOI Listing
May 2013
39 Reads
13 Citations
9.600 Impact Factor

Potent anticancer activity of cystine-based dipeptides and their interaction with serum albumins.

Chem Cent J 2013 May 24;7(1):91. Epub 2013 May 24.

Department of Chemistry, CSIR-Indian Institute of Chemical Biology, 4, Raja S,C, Mullick Road, Kolkata 700032, India.

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http://dx.doi.org/10.1186/1752-153X-7-91DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3680302PMC
May 2013
26 Reads
3 Citations
2.190 Impact Factor

CHAPERONE ACTION OF CYCLOPHILIN ON LYSOZYME AND ITS AGGREGATE

Various protein aggregates are formed in cellular systems when partially misfolded/folded states of proteins are trapped in a certain conformation. It eventually leads to the formation of larger and more stable aggregates. In the aggregated state proteins are functionally inactive and they are often enriched with antiparallel β-strands as compared to the native state. It has been established that a closely neaten molecular chaperone activity helps many proteins to preserve their cellular function by maintaining the protein conformation in their functional states. Thus the action of chaperone helps the cell to sustain various stresses that otherwise cause an extensive protein denaturation and aggregation. Recently, our laboratory demonstrated that AdK which has an inherent tendency to form inactive soluble aggregates could be disaggregated by cyclophilin derived from L. donovani (LdCyp) in an isomerase-independent fashion and resulted reactivation. Investigation is continuing to evaluate its action on amyloid aggregates formed by lysozyme. In addition the self and co-aggregation process of cyclophilin has been studied by fluorescence and TEM measurements. To our surprise, we observed the formation of elongated and fine fibrils when lysozyme was co-incubated with cyclophilin. Cyclophiln itself did not form any detectable aggregates under similar condition; however, it showed potential to disaggregate amorphous aggregate of lysozyme. Computational analysis was further performed to describe the aggregation and disaggregation of the proteins and their amyloidogenic behavior.

https://doaj.org/article/b8f255f33b594cc2aade0dc33ce50738

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January 2013
9 Reads

Novel anti-inflammatory activity of epoxyazadiradione against macrophage migration inhibitory factor: inhibition of tautomerase and proinflammatory activities of macrophage migration inhibitory factor.

J Biol Chem 2012 Jul 29;287(29):24844-61. Epub 2012 May 29.

Division of Infectious Diseases and Immunology, Council of Scientific and Industrial Research (CSIR)-Indian Institute of Chemical Biology, 4 Raja S. C. Mullick Road, Jadavpur, Kolkata 700032, West Bengal, India.

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http://dx.doi.org/10.1074/jbc.M112.341321DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3397911PMC
July 2012
36 Reads
16 Citations
4.573 Impact Factor

Nickel(II)-Schiff base complex recognizing domain II of bovine and human serum albumin: spectroscopic and docking studies.

Spectrochim Acta A Mol Biomol Spectrosc 2012 Jun 25;92:164-74. Epub 2012 Feb 25.

Chemical Sciences Division, Saha Institute of Nuclear Physics, Kolkata, India.

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http://dx.doi.org/10.1016/j.saa.2012.02.060DOI Listing
June 2012
13 Reads
5 Citations
2.353 Impact Factor

Interaction of Merocyanine 540 with serum albumins: photophysical and binding studies.

J Photochem Photobiol B 2012 Mar 29;108:23-33. Epub 2011 Dec 29.

Chemical Sciences Division, Saha Institute of Nuclear Physics, Kolkata, India.

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http://dx.doi.org/10.1016/j.jphotobiol.2011.12.005DOI Listing
March 2012
14 Reads
3 Citations
2.960 Impact Factor

Synthesis and bio-evaluation of human macrophage migration inhibitory factor inhibitor to develop anti-inflammatory agent.

Bioorg Med Chem 2011 Dec 24;19(24):7365-73. Epub 2011 Oct 24.

Department of Infectious Diseases and Immunology, Indian Institute of Chemical Biology, 4 Raja S C Mullick Road, Jadavpur, Kolkata 700 032, West Bengal, India.

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http://dx.doi.org/10.1016/j.bmc.2011.10.056DOI Listing
December 2011
39 Reads
6 Citations
2.793 Impact Factor

Top co-authors

Nakul C Maiti
Nakul C Maiti

Case Western Reserve University

13
Biswadip Banerji
Biswadip Banerji

CSIR-Indian Institute of Chemical Biology

7
Nakul Chandra Maiti
Nakul Chandra Maiti

Council of Scientific and Industrial Research (CSIR)-Indian Institute of Chemical Biology (IICB)

7
Sumit Kumar Pramanik
Sumit Kumar Pramanik

CSIR-Indian Institute of Chemical Biology

5
Samita Basu
Samita Basu

Saha Institute of Nuclear Physics

4
Biswarup Satpati
Biswarup Satpati

Indian Institute of Technology Ropar

3
Dulal Senapati
Dulal Senapati

Jackson State University

3
Anupam Roy
Anupam Roy

Institute of Physics

3
Moumita Chatterjee
Moumita Chatterjee

University of Delaware

3

Following

Snehasikta Swarnakar
Snehasikta Swarnakar

Indian Institute of Chemical Biology