A. Srinivasan
About
A. Srinivasan is a scholar working on Molecular Biology, Genetics and Nutrition and Dietetics.
According to data from OpenAlex, A. Srinivasan has authored 39 papers receiving a total of 947 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 14 papers in Genetics and 7 papers in Nutrition and Dietetics. Recurrent topics in A. Srinivasan's work include Venomous Animal Envenomation and Studies (13 papers), Enzyme Structure and Function (6 papers) and Healthcare and Venom Research (5 papers). A. Srinivasan is often cited by papers focused on Venomous Animal Envenomation and Studies (13 papers), Enzyme Structure and Function (6 papers) and Healthcare and Venom Research (5 papers). A. Srinivasan collaborates with scholars based in India, Germany and Japan. A. Srinivasan's co-authors include T.P. Singh, Punit Kaur, M. Paramasivam, J. Jasti, Sujata Sharma, Ch. Betzel, Vikas Chandra, N. Singh, Savita Yadav and Samudrala Gourinath and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and Journal of Molecular Biology.
In The Last Decade
A. Srinivasan
38 papers receiving 931 citations
Peers
A. Srinivasan
G. Cohen Israel
Monica Lindh Sweden
Kurt W. Miller United States
Rachel M. Adams United States
James D. Love United States
Zongchao Jia Canada
Umashankar Vetrivel India
W. W. Fish United States
Heather W. Pinkett United States
Yu‐Ching Lee Taiwan
Citations per year, relative to A. Srinivasan A. Srinivasan (= 1×)
peers
G. Cohen
Countries citing papers authored by A. Srinivasan
Since
Specialization
Citations
This map shows the geographic impact of A. Srinivasan's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by A. Srinivasan with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites A. Srinivasan more than expected).
Fields of papers citing papers by A. Srinivasan
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by A. Srinivasan. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by A. Srinivasan. The network helps show where A. Srinivasan may publish in the future.
Co-authorship network of co-authors of A. Srinivasan
This figure shows the co-authorship network connecting the top 25 collaborators of A. Srinivasan. A scholar is included among the top collaborators of A. Srinivasan based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with A. Srinivasan. A. Srinivasan is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Aslam, Muhammad, Shashank Pandey, Samiksha Nayak, et al.. (2014). Differential proteomic profile of spermatogenic and Sertoli cells from peri-pubertal testes of three different bovine breeds. Frontiers in Cell and Developmental Biology. 2. 24–24.
2.
Tomar, Anil Kumar, et al.. (2011). Purification and Partial Characterization of Low Molecular Weight Vicilin-Like Glycoprotein from the Seeds of Citrullus lanatus. The Protein Journal. 30(8). 575–580.
3.
Sharma, Sujata, et al.. (2011). RASOnD - A comprehensive resource and search tool for RAS superfamily oncogenes from various species. BMC Genomics. 12(1). 341–341.
4.
Singh, Avinash, N. Singh, Sujata Sharma, et al.. (2009). Inhibition of Lactoperoxidase by Its Own Catalytic Product: Crystal Structure of the Hypothiocyanate-Inhibited Bovine Lactoperoxidase at 2.3-Å Resolution. Biophysical Journal. 96(2). 646–654.
5.
Sinha, M., Sujata Sharma, N. Singh, et al.. (2008). Isolation, purification, crystallization and preliminary crystallographic studies of sagitoxin, an oligomeric cardiotoxin from the venom ofNaja naja saggitifera. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64(6). 545–547.
6.
Srivastava, Devendra B., A.S. Ethayathulla, Janesh Kumar, et al.. (2006). Crystal structure of a secretory signalling glycoprotein from sheep at 2.0 Å resolution. Journal of Structural Biology. 156(3). 505–516.
7.
Ethayathulla, A.S., T. Jabeen, N. Singh, et al.. (2006). Crystal structure of a highly acidic neurotoxin from scorpion Buthus tamulus at 2.2 Ǻ resolution reveals novel structural features. Journal of Structural Biology. 155(1). 52–62.
8.
Singh, N., T. Jabeen, Sujata Sharma, et al.. (2006). Specific binding of non-steroidal anti-inflammatory drugs (NSAIDs) to phospholipase A2: structure of the complex formed between phospholipase A2and diclofenac at 2.7 Å resolution. Acta Crystallographica Section D Biological Crystallography. 62(4). 410–416.
9.
Singh, Garima, J. Jasti, Saravanan Kolandaivelu, et al.. (2005). Crystal structure of the complex formed between a group I Phospholipase A2 and a naturally occurring fatty acid at 2.7 Å resolution. Protein Science. 14(2). 395–400.
10.
Jabeen, T., Sujata Sharma, N. Singh, et al.. (2005). Structure of the zinc-induced heterodimer of two calcium-free isoforms of phospholipase A2fromNaja naja sagittiferaat 2.7 Å resolution. Acta Crystallographica Section D Biological Crystallography. 61(3). 302–308.
11.
Singh, Garima, Samudrala Gourinath, Saravanan Kolandaivelu, et al.. (2004). Sequence-induced trimerization of phospholipase A2: structure of a trimeric isoform of PLA2from common krait (Bungarus caeruleus) at 2.5 Å resolution. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(1). 8–13.
12.
Jasti, J., M. Paramasivam, A. Srinivasan, & T.P. Singh. (2003). Crystal Structure of Echicetin from Echis carinatus (Indian Saw-scaled Viper) at 2.4Å Resolution. Journal of Molecular Biology. 335(1). 167–176.
13.
Paramasivam, M., et al.. (2002). Expression, purification, and characterization of equine lactoferrin in Pichia pastoris. Protein Expression and Purification. 26(1). 28–34.
14.
Chandra, Vikas, J. Jasti, Punit Kaur, et al.. (2002). Design of specific peptide inhibitors of phospholipase A2: structure of a complex formed between Russell's viper phospholipase A2and a designed peptide Leu-Ala-Ile-Tyr-Ser (LAIYS). Acta Crystallographica Section D Biological Crystallography. 58(10). 1813–1819.
15.
Chandra, Vikas, J. Jasti, Punit Kaur, et al.. (2002). First Structural Evidence of a Specific Inhibition of Phospholipase A2 by α-Tocopherol (Vitamin E) and its Implications in Inflammation: Crystal Structure of the Complex Formed Between Phospholipase A2 and α-Tocopherol at 1.8Å Resolution. Journal of Molecular Biology. 320(2). 215–222.
16.
Kumar, Pravindra, et al.. (2001). A novel 40 kDa protein from goat mammary secretions: purification, crystallization and preliminary X-ray diffraction studies. Acta Crystallographica Section D Biological Crystallography. 57(9). 1332–1333.
17.
Khan, Javed, Pravindra Kumar, A. Srinivasan, & T.P. Singh. (2001). Protein Intermediate Trapped by the Simultaneous Crystallization Process. Journal of Biological Chemistry. 276(39). 36817–36823.
18.
Singh, Garima, Samudrala Gourinath, Sujata Sharma, et al.. (2001). Sequence and crystal structure determination of a basic phospholipase A2 from common krait ( Bungarus caeruleus ) at 2.4 Å resolution: identification and characterization of its pharmacological sites 1 1Edited by R. Huber. Journal of Molecular Biology. 307(4). 1049–1059.
19.
Khan, Javed, Pravindra Kumar, M. Paramasivam, et al.. (2001). Camel Lactoferrin, a Transferrin-cum-Lactoferrin: Crystal Structure of Camel Apolactoferrin at 2.6Å Resolution and Structural Basis of its Dual Role. Journal of Molecular Biology. 309(3). 751–761.
20.
Sharma, Ashwani Kumar, M. Paramasivam, A. Srinivasan, Miklesh Prasad Yadav, & T.P. Singh. (1999). Three-dimensional structure of mare diferric lactoferrin at 2.6 Å resolution. Journal of Molecular Biology. 289(2). 303–317.
Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.
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