T
Tamanna Anwar
Researcher at Jawaharlal Nehru University
Publications - 14
Citations - 205
Tamanna Anwar is an academic researcher from Jawaharlal Nehru University. The author has contributed to research in topics: Influenza A virus subtype H5N1 & Virus. The author has an hindex of 6, co-authored 14 publications receiving 178 citations. Previous affiliations of Tamanna Anwar include Aligarh Muslim University.
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Journal ArticleDOI
Biophysical and molecular docking insight into the interaction of cytosine β-D Arabinofuranoside with Human serum albumin
Parvez Alam,Sumit Kumar Chaturvedi,Tamanna Anwar,Mohammad Khursheed Siddiqi,Mohd Rehan Ajmal,Gamal Badr,Mohamed H. Mahmoud,Rizwan Hasan Khan +7 more
TL;DR: This study will be helpful to understand the binding mechanism of cytosine β-D arabinofuranoside with HSA and associated alterations and help understand the topology of protein in absence and presence of drug.
Journal Article
In silico analysis of genes nucleoprotein, neuraminidase and hemagglutinin: a comparative study on different strains of influenza A (Bird flu) virus sub-type H5N1.
TL;DR: The in silico analysis predicted that HA of influenza A virus is highly sensitive to mutations and hence it is significant for its pathogenic nature.
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Analysis of the Protein phosphotome of Entamoeba histolytica reveals an intricate phosphorylation network.
TL;DR: A comprehensive phosphotome analysis of E. histolytica shows spectacular low similarity to human phosphatases, making them potent candidates for drug target.
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Non-enzymatic glycation enhances human serum albumin binding capacity to sodium fluorescein at room temperature: A spectroscopic analysis
TL;DR: The interactions were found to be spontaneous, irrespective of temperature or glycation, and SF shows best binding to FA binding site III of HSA, which also overlaps with drug binding site II of subdomain IIIA.
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Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB.
TL;DR: Phosphatases were widely distributed throughout the cell suggesting physiological adaptation of the parasite to regulate its host and the need for new effective and safer antiprotozoal agents.