Sanjeev K. Chandrayan

1.1k total citations
27 papers, 891 citations indexed

About

Sanjeev K. Chandrayan is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Biomedical Engineering. According to data from OpenAlex, Sanjeev K. Chandrayan has authored 27 papers receiving a total of 891 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 7 papers in Renewable Energy, Sustainability and the Environment and 7 papers in Biomedical Engineering. Recurrent topics in Sanjeev K. Chandrayan's work include Enzyme Catalysis and Immobilization (9 papers), Metalloenzymes and iron-sulfur proteins (7 papers) and Biofuel production and bioconversion (6 papers). Sanjeev K. Chandrayan is often cited by papers focused on Enzyme Catalysis and Immobilization (9 papers), Metalloenzymes and iron-sulfur proteins (7 papers) and Biofuel production and bioconversion (6 papers). Sanjeev K. Chandrayan collaborates with scholars based in India, United States and Mexico. Sanjeev K. Chandrayan's co-authors include Michael W. W. Adams, Chun You, Joseph A. Rollin, Suwan Myung, Julia S. Martín del Campo, Y.-H. Percival Zhang, Fangfang Sun, Patrick M. McTernan, Changhao Wu and Purnananda Guptasarma and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Sanjeev K. Chandrayan

27 papers receiving 873 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Sanjeev K. Chandrayan India	15	587	237	165	125	104	27	891
Jason Nichols United States	11	413 0.7×	162 0.7×	155 0.9×	53 0.4×	79 0.8×	14	625
Paul H. Opgenorth United States	7	811 1.4×	357 1.5×	316 1.9×	81 0.6×	65 0.6×	9	1.3k
Takashi Saiki Japan	12	324 0.6×	141 0.6×	113 0.7×	110 0.9×	51 0.5×	41	660
Liang‐Jung Chien Taiwan	14	414 0.7×	250 1.1×	248 1.5×	52 0.4×	63 0.6×	23	786
M I Donnelly United States	15	793 1.4×	257 1.1×	69 0.4×	187 1.5×	70 0.7×	20	1.1k
Ellen Panisko United States	18	608 1.0×	468 2.0×	65 0.4×	74 0.6×	92 0.9×	29	1.2k
Yuki Honda Japan	15	186 0.3×	99 0.4×	247 1.5×	139 1.1×	57 0.5×	27	549
Robert Conrado United States	7	609 1.0×	189 0.8×	43 0.3×	64 0.5×	47 0.5×	8	716
Tae Hoon Yang Germany	14	1.1k 1.9×	612 2.6×	44 0.3×	58 0.5×	30 0.3×	19	1.4k
Johannes Schiffels Germany	13	383 0.7×	138 0.6×	57 0.3×	77 0.6×	44 0.4×	24	599

Countries citing papers authored by Sanjeev K. Chandrayan

Since Specialization

Citations

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

Fields of papers citing papers by Sanjeev K. Chandrayan

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Sanjeev K. Chandrayan. 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 Sanjeev K. Chandrayan. The network helps show where Sanjeev K. Chandrayan may publish in the future.

Co-authorship network of co-authors of Sanjeev K. Chandrayan

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

All Works

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20 of 20 papers shown

Donkor, Emmanuel, et al.. (2018). Novel Bioengineered Cassava Expressing an Archaeal Starch Degradation System and a Bacterial ADP-Glucose Pyrophosphorylase for Starch Self-Digestibility and Yield Increase. Frontiers in Plant Science. 9. 192–192. 11 indexed citations

Odaneth, Annamma A., et al.. (2017). Heterologous expression and biochemical studies of a thermostable glucose tolerant β-glucosidase from Methylococcus capsulatus ( bath strain ). International Journal of Biological Macromolecules. 102. 805–812. 14 indexed citations

Odaneth, Annamma A., et al.. (2017). SGNH hydrolase-type esterase domain containing Cbes-AcXE2: a novel and thermostable acetyl xylan esterase from Caldicellulosiruptor bescii. Extremophiles. 21(4). 687–697. 13 indexed citations

Odaneth, Annamma A., et al.. (2016). Expression, purification and biochemical characterization of a family 6 carboxylesterase from Methylococcus capsulatus (bath). Protein Expression and Purification. 122. 31–37. 2 indexed citations

Rollin, Joseph A., Julia S. Martín del Campo, Suwan Myung, et al.. (2015). High-yield hydrogen production from biomass by in vitro metabolic engineering: Mixed sugars coutilization and kinetic modeling. Proceedings of the National Academy of Sciences. 112(16). 4964–4969. 174 indexed citations

Myung, Suwan, Joseph A. Rollin, Chun You, et al.. (2014). In vitro metabolic engineering of hydrogen production at theoretical yield from sucrose. Metabolic Engineering. 24. 70–77. 78 indexed citations

Chandrayan, Sanjeev K., Changhao Wu, Patrick M. McTernan, & Michael W. W. Adams. (2014). High yield purification of a tagged cytoplasmic [NiFe]-hydrogenase and a catalytically-active nickel-free intermediate form. Protein Expression and Purification. 107. 90–94. 26 indexed citations

Chandrayan, Sanjeev K., et al.. (2014). Mannosylglycerate and Di- myo -Inositol Phosphate Have Interchangeable Roles during Adaptation of Pyrococcus furiosus to Heat Stress. Applied and Environmental Microbiology. 80(14). 4226–4233. 24 indexed citations

Lewis, Derrick, Sanjeev K. Chandrayan, Andrew J. Loder, et al.. (2014). A mutant (‘lab strain’) of the hyperthermophilic archaeon Pyrococcus furiosus, lacking flagella, has unusual growth physiology. Extremophiles. 19(2). 269–281. 7 indexed citations

10.

Chandrayan, Sanjeev K., Satya Prakash, Shubbir Ahmed, & Purnananda Guptasarma. (2014). Hyperthermophile Protein Behavior: Partially-Structured Conformations of Pyrococcus furiosus Rubredoxin Monomers Generated through Forced Cold-Denaturation and Refolding. PLoS ONE. 9(3). e80014–e80014. 4 indexed citations

11.

McTernan, Patrick M., Sanjeev K. Chandrayan, Cui Wu, et al.. (2014). Engineering the respiratory membrane-bound hydrogenase of the hyperthermophilic archaeon Pyrococcus furiosus and characterization of the catalytically active cytoplasmic subcomplex. Protein Engineering Design and Selection. 28(1). 1–8. 7 indexed citations

12.

Campo, Julia S. Martín del, Joseph A. Rollin, Suwan Myung, et al.. (2013). High‐Yield Production of Dihydrogen from Xylose by Using a Synthetic Enzyme Cascade in a Cell‐Free System. Angewandte Chemie International Edition. 52(17). 4587–4590. 105 indexed citations

13.

Chandrayan, Sanjeev K., Patrick M. McTernan, Robin Hopkins, et al.. (2011). Engineering Hyperthermophilic Archaeon Pyrococcus furiosus to Overproduce Its Cytoplasmic [NiFe]-Hydrogenase. Journal of Biological Chemistry. 287(5). 3257–3264. 42 indexed citations

14.

Hopkins, Robin, et al.. (2011). Homologous Expression of a Subcomplex of Pyrococcus furiosus Hydrogenase that Interacts with Pyruvate Ferredoxin Oxidoreductase. PLoS ONE. 6(10). e26569–e26569. 24 indexed citations

15.

Chandrayan, Sanjeev K. & Purnananda Guptasarma. (2009). Attenuation of ionic interactions profoundly lowers the kinetic thermal stability of Pyrococcus furiosus triosephosphate isomerase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794(6). 905–912. 5 indexed citations

16.

Chandrayan, Sanjeev K. & Purnananda Guptasarma. (2008). Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. Proteins Structure Function and Bioinformatics. 72(2). 539–546. 13 indexed citations

17.

Kumar, Vijay, Sanjeev K. Chandrayan, Shubbir Ahmed, et al.. (2008). Replacement of the active surface of a thermophile protein by that of a homologous mesophile protein through structure-guided ‘protein surface grafting’. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1784(11). 1771–1776. 8 indexed citations

18.

Chandrayan, Sanjeev K., et al.. (2008). Expression, purification, refolding and characterization of a putative lysophospholipase from Pyrococcus furiosus: Retention of structure and lipase/esterase activity in the presence of water-miscible organic solvents at high temperatures. Protein Expression and Purification. 59(2). 327–333. 16 indexed citations

19.

Chandrayan, Sanjeev K., et al.. (2007). Using DNA sequencing electrophoresis compression artifacts as reporters of stable mRNA structures affecting gene expression. Electrophoresis. 28(21). 3862–3867. 3 indexed citations

20.

Das, Utpal, Gururao Hariprasad, A.S. Ethayathulla, et al.. (2007). Inhibition of Protein Aggregation: Supramolecular Assemblies of Arginine Hold the Key. PLoS ONE. 2(11). e1176–e1176. 189 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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