Arvind M. Kayastha

4.4k total citations
151 papers, 3.4k citations indexed

About

Arvind M. Kayastha is a scholar working on Molecular Biology, Biotechnology and Plant Science. According to data from OpenAlex, Arvind M. Kayastha has authored 151 papers receiving a total of 3.4k indexed citations (citations by other indexed papers that have themselves been cited), including 88 papers in Molecular Biology, 60 papers in Biotechnology and 34 papers in Plant Science. Recurrent topics in Arvind M. Kayastha's work include Enzyme Production and Characterization (58 papers), Enzyme Catalysis and Immobilization (40 papers) and Phytase and its Applications (19 papers). Arvind M. Kayastha is often cited by papers focused on Enzyme Production and Characterization (58 papers), Enzyme Catalysis and Immobilization (40 papers) and Phytase and its Applications (19 papers). Arvind M. Kayastha collaborates with scholars based in India, United States and Germany. Arvind M. Kayastha's co-authors include Alka Dwevedi, Punit Srivastava, Arpana Kumari, Nilanjana Das, Sandeep Kumar, Ranjana Das, Mahe Talat, O. N. Srivastava, Vinay Kumar Singh and Anchal Srivastava and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and PLoS ONE.

In The Last Decade

Arvind M. Kayastha

146 papers receiving 3.3k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Arvind M. Kayastha India 34 2.0k 993 647 570 552 151 3.4k
Fahrul Huyop Malaysia 25 1.7k 0.9× 566 0.6× 524 0.8× 804 1.4× 537 1.0× 189 3.3k
Oliver Spadiut Austria 35 2.9k 1.5× 774 0.8× 766 1.2× 837 1.5× 207 0.4× 190 4.2k
Reinhard Wimmer Denmark 35 1.9k 0.9× 341 0.3× 549 0.8× 364 0.6× 125 0.2× 148 4.0k
Xueqin Lv China 36 2.7k 1.4× 496 0.5× 419 0.6× 718 1.3× 280 0.5× 187 4.0k
Claire Vieille United States 32 3.6k 1.8× 1.5k 1.5× 725 1.1× 1.6k 2.8× 126 0.2× 62 5.0k
Seunho Jung South Korea 33 865 0.4× 184 0.2× 642 1.0× 691 1.2× 396 0.7× 208 3.6k
Ayelet Fishman Israel 35 1.6k 0.8× 369 0.4× 370 0.6× 350 0.6× 167 0.3× 91 3.6k
Philippe Soucaille France 48 4.0k 2.0× 467 0.5× 258 0.4× 2.8k 4.9× 531 1.0× 111 6.0k
Yan Feng China 40 3.5k 1.7× 779 0.8× 345 0.5× 1.1k 1.9× 223 0.4× 197 5.6k
Shoichi Shimizu Japan 44 4.2k 2.1× 632 0.6× 317 0.5× 1.1k 1.9× 244 0.4× 260 6.0k

Countries citing papers authored by Arvind M. Kayastha

Since Specialization
Citations

This map shows the geographic impact of Arvind M. Kayastha'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 Arvind M. Kayastha with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Arvind M. Kayastha more than expected).

Fields of papers citing papers by Arvind M. Kayastha

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Arvind M. Kayastha. 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 Arvind M. Kayastha. The network helps show where Arvind M. Kayastha may publish in the future.

Co-authorship network of co-authors of Arvind M. Kayastha

This figure shows the co-authorship network connecting the top 25 collaborators of Arvind M. Kayastha. A scholar is included among the top collaborators of Arvind M. Kayastha 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 Arvind M. Kayastha. Arvind M. Kayastha is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Singh, Sakshi, et al.. (2025). An exploration of lipid remodeling by microalga Chlamydomonas reinhardtii in autotrophic and mixotrophic cultivation for bioenergy prospects. Biomass and Bioenergy. 200. 108015–108015. 2 indexed citations
2.
3.
Kayastha, Arvind M., et al.. (2024). Exploring the catalytic potential of watermelon urease: Purification, biochemical characterization, and heavy metal precipitation. International Journal of Biological Macromolecules. 282(Pt 1). 136798–136798. 4 indexed citations
4.
Kumar, Avinash, et al.. (2024). Deciphering unfolding pathways: Chemical, heat, and acid induced investigations using fenugreek (Trigonella foenum-graecum) α-amylase. Journal of Molecular Structure. 1315. 138857–138857. 1 indexed citations
5.
Kumar, Avinash, Vinay Kumar Singh, & Arvind M. Kayastha. (2024). Studies on α-amylase inhibition by acarbose and quercetin using fluorescence, circular dichroism, docking, and dynamics simulations. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy. 314. 124160–124160. 10 indexed citations
6.
Dkhar, Daphika S., et al.. (2024). Watermelon Derived Urease Immobilized Gold Nanoparticles-Graphene Oxide Transducer for Direct Detection of Urea in Milk Samples. ACS Applied Bio Materials. 7(10). 6357–6370. 11 indexed citations
7.
Singh, Vinay Kumar, et al.. (2023). In Silico Structural and Functional Insight into the Binding Interactions of the Modeled Structure of Watermelon Urease with Urea. ACS Omega. 9(2). 2272–2285. 9 indexed citations
8.
Kumar, Suveen, Shiju Abraham, Tejendra K. Gupta, et al.. (2016). Excellent storage stability and sensitive detection of neurotoxin quinolinic acid. Biosensors and Bioelectronics. 90. 224–229. 13 indexed citations
9.
Singh, Asha Lata, et al.. (2015). Decolorization and degradation of textile effluent with the help of Enterobacter asburiae. Indian Journal of Biotechnology. 14(1). 101–106. 16 indexed citations
10.
Srivastava, Garima, Sonam Roy, & Arvind M. Kayastha. (2014). Immobilisation of Fenugreek β-amylase on chitosan/PVP blend and chitosan coated PVC beads: A comparative study. Food Chemistry. 172. 844–851. 20 indexed citations
11.
Kumar, Sandeep & Arvind M. Kayastha. (2013). Acetohydroxamic Acid - A Competitive Inhibitor of Urease from Soybean “Glycine max”. Journal of Proteins and Proteomics. 1(1). 11 indexed citations
12.
Kumari, Arpana, Tobias Rosenkranz, Jörg Fitter, & Arvind M. Kayastha. (2011). Structural Stability of Soybean (Glycine max) α-Amylase: Properties of the Unfolding Transition Studied with Fluorescence and CD Spectroscopy. Protein and Peptide Letters. 18(3). 253–260. 7 indexed citations
13.
Kumari, Arpana, Vinay Kumar Singh, Jörg Fitter, Tino Polen, & Arvind M. Kayastha. (2010). α-Amylase from germinating soybean (Glycine max) seeds – Purification, characterization and sequential similarity of conserved and catalytic amino acid residues. Phytochemistry. 71(14-15). 1657–1666. 42 indexed citations
14.
Singh, Shweta, Shweta Singh, Arvind M. Kayastha, et al.. (2004). Response of Garden Pea to Nickel Toxicity. Journal of Plant Nutrition. 27(9). 1543–1560. 7 indexed citations
15.
Biswas, Shyamasri & Arvind M. Kayastha. (2004). Spectroscopic Characterization Of Phaseolus Vulgaris Leucoagglutinin. Protein and Peptide Letters. 11(1). 1–7. 12 indexed citations
16.
Mathew, Arun Tom, et al.. (2004). Solid state potentiometric sensor for the estimation of tributyrin and urea. Sensors and Actuators B Chemical. 107(1). 418–423. 38 indexed citations
17.
Biswas, Shyamasri, Arvind M. Kayastha, & Robert Seckler. (2003). Purification and characterization of a thermostable β-Galactosidase from kidney beans (Phaseolus vulgaris L.) cv. PDR14. Journal of Plant Physiology. 160(4). 327–337. 30 indexed citations
18.
Srivastava, Punit, Arvind M. Kayastha, & Medicherla V. Jagannadham. (2002). Kinetics of Inhibition and Molecular Asymmetry in Pigeonpea ( Cajanus cajan ) Urease. PubMed. 6(1). 1–6. 10 indexed citations
19.
Kayastha, Arvind M., et al.. (2000). The Role of Peroxidase and Polyphenol Oxidase Isozymes in Wheat Resistance to Alternaria triticina. Biologia Plantarum. 43(4). 559–562. 23 indexed citations
20.
Srinivasan, R., Arvind M. Kayastha, & O.P. Malhotra. (1992). Substrate-Induced Stability of Glyceraldehyde 3-Phosphate Dehydrogenase from Mung Beans (Vigna radiata L.). PLANT PHYSIOLOGY. 100(4). 2109–2112. 2 indexed citations

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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