Publications by authors named "P Nair Leena"

5 Publications

  • Page 1 of 1

Life profile of Vaikath Parameswaran Moothath, a polymath.

J Ayurveda Integr Med 2019 Jan - Mar;10(1):69-71. Epub 2019 Mar 4.

Department of Maulika Siddhanta (Basic Principles of Ayurveda), Amrita School of Ayurveda, Amrita Vishwa Vidyapeetham, Amritapuri, India. Electronic address:

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http://dx.doi.org/10.1016/j.jaim.2019.01.001DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6470301PMC
March 2019

Biological Activity of Steroids from the Marine Gastropods Collected from South West Coast of India.

Avicenna J Med Biotechnol 2018 Jul-Sep;10(3):158-162

Department of Chemical Oceanography, Faculty of Marine Sciences, Cochin University of Science and Technology, Cochin-682016, India.

Background: The purpose of this study was to investigate the sterol profiling and predict the pharmacological potential of marine gastropod , collected from mangrove ecosystem in the South west coast of India.

Methods: Sterol fractions were separated from the crude lipids using 15% ethyl acetate. Ethyl acetate fractions were dried under ultrahigh purity N and analyzed using GC-MS. The biological activity was predicted using the software CLC-Pred; predictions of cytotoxicity for tumor and non-tumor cell lines and PASS.

Results: This study proved the existence of four sterols, of which cholesterol was abundant. It was found that most of the steroids profiled from displayed activity against reproductive system as well as skin related diseases.

Conclusion: The predicted anti infertility and skin related activity of the steroids identified from the marine gastropod is useful to attract industrial interest towards this species which will be helpful in rising new combinations with added therapeutic and nutritional worth.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6064002PMC
August 2018

Heavy metal concentrations in some gastropods and bivalves collected from the fishing zone of South India.

Mar Pollut Bull 2017 May 21;118(1-2):452-458. Epub 2017 Mar 21.

Department of Chemical Oceanography, School of Marine Sciences, Cochin University of Science and Technology, Cochin 682016, India. Electronic address:

The present study investigates heavy metal concentrations in gastropods and bivalves collected from major fishing centers in South India. Three gastropods, Bursa spinosa, Tibia curta, and Murex trapa, and two bivalves, Perna viridis and Villoritta cyprinoids, were collected for the analysis of heavy metals. The metals in the present study followed the order Mg>Ca>Zn>Fe>Cu>Mn>Cr>Pb>Ni>Co>Cd. Trace metal concentrations in the soft tissue of the molluscs varied as follows: for Cd: 0.04-5.33, Co: 0.09-0.87, Cr: 2.18-7.59, Cu: 9.54-37.02, Mn: 1.30-8.50, Ni: 0.94-3.21, Pb: 1.16-2.64 and Zn: 68.16-113.64mgkg. Metal concentrations in all the species were below the limits proposed by the World Health Organization, except for Pb and Cd. This baseline study suggests that the levels of toxic metals in M. trapa, T. curta, and B. spinosa should be continuously monitored to assess the fate and effects of these metals in this fragile ecosystem.
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http://dx.doi.org/10.1016/j.marpolbul.2017.03.029DOI Listing
May 2017

Three-dimensional solution structures of the chromodomains of cpSRP43.

J Biol Chem 2005 Dec 23;280(50):41465-71. Epub 2005 Sep 23.

Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, USA.

Chloroplasts contain a unique signal recognition particle (cpSRP). Unlike the cytoplasmic forms, the cpSRP lacks RNA but contains a conserved 54-kDa GTPase and a novel 43-kDa subunit (cpSRP43). Recently, three functionally distinct chromodomains (CDs) have been identified in cpSRP43. In the present study, we report the three-dimensional solution structures of the three CDs (CD1, CD2, and CD3) using a variety of triple resonance NMR experiments. The structure of CD1 consists of a triple-stranded beta-sheet segment. The C-terminal helical segment typically found in the nuclear chromodomains is absent in CD1. The secondary structural elements in CD2 and CD3 include a triple-stranded antiparallel beta-sheet and a C-terminal helix. Interestingly, the orientation of the C-terminal helix is significantly different in the structures of CD2 and CD3. Critical comparison of the structures of the chromodomains of cpSRP43 with those found in nuclear chromodomain proteins revealed that the diverse protein-protein interactions mediated by the CDs appear to stem from the differences that exist in the surface charge potentials of each CD. Results of isothermal titration calorimetry experiments confirmed that only CD2 is involved in binding to cpSRP54. The negatively charged C-terminal helix in CD2 possibly plays a crucial role in the cpSRP54-cpSRP43 interaction.
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http://dx.doi.org/10.1074/jbc.M507077200DOI Listing
December 2005

Oligomerization of acidic fibroblast growth factor is not a prerequisite for its cell proliferation activity.

Protein Sci 2002 May;11(5):1050-61

Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan.

Oligomerization of fibroblast growth factors (FGFs) induced on binding to heparin or heparan sulfate proteoglycan is considered to be crucial for receptor activation and initiation of biological responses. To gain insight into the mechanism of activation of the receptor by FGFs, in the present study we investigate the effect(s) of interaction of a heparin analog, sucrose octasulfate (SOS), on the structure, stability, and biological activities of a recombinant acidic FGF from Notophthalmus viridescens (nFGF-1). SOS is found to bind to nFGF-1 and significantly increase the thermodynamic stability of the protein. Using a variety of techniques such as size-exclusion chromatography, sedimentation velocity, and multidimensional nuclear magnetic resonance (NMR) spectroscopy, it is shown that binding of SOS to nFGF-1 retains the protein in its monomeric state. In its monomeric state (complexed to SOS), n-FGF-1 shows significant cell proliferation activity. (15)N and (1)H chemical shift perturbation and the intermolecular nuclear Overhauser effects (NOEs) between SOS and nFGF-1 reveal that the ligand binds to the dense, positively charged cluster located in the groove enclosed by beta-strands 10 and 11. In addition, molecular modeling based on the NOEs observed for the SOS-nFGF-1 complex, indicates that SOS and heparin share a common binding site on the protein. In conclusion, the results of the present study clearly show that heparin-induced oligomerization of nFGF-1 is not mandatory for its cell proliferation activity.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2373565PMC
http://dx.doi.org/10.1110/ps.2270102DOI Listing
May 2002
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