Gotam K. Jarori

874 total citations
46 papers, 690 citations indexed

About

Gotam K. Jarori is a scholar working on Molecular Biology, Materials Chemistry and Public Health, Environmental and Occupational Health. According to data from OpenAlex, Gotam K. Jarori has authored 46 papers receiving a total of 690 indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 13 papers in Materials Chemistry and 9 papers in Public Health, Environmental and Occupational Health. Recurrent topics in Gotam K. Jarori's work include Enzyme Structure and Function (12 papers), Malaria Research and Control (9 papers) and Protein Structure and Dynamics (8 papers). Gotam K. Jarori is often cited by papers focused on Enzyme Structure and Function (12 papers), Malaria Research and Control (9 papers) and Protein Structure and Dynamics (8 papers). Gotam K. Jarori collaborates with scholars based in India, United States and Portugal. Gotam K. Jarori's co-authors include Ipsita Pal‐Bhowmick, D. N. Rao, Shobhona Sharma, Isabelle Coppens, Nagarajan Murali, Bruce D. Ray, Monika Mehta, V. Jo Davisson, Nirbhay Kumar and Umakant W. Kenkare and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Biochemistry.

In The Last Decade

Gotam K. Jarori

45 papers receiving 676 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gotam K. Jarori India 15 402 138 105 86 77 46 690
Shahir S. Rizk United States 11 651 1.6× 321 2.3× 105 1.0× 39 0.5× 66 0.9× 13 1.1k
Juha Vahokoski Norway 12 305 0.8× 197 1.4× 57 0.5× 88 1.0× 34 0.4× 20 607
Rie Nakajima Japan 17 390 1.0× 84 0.6× 140 1.3× 39 0.5× 72 0.9× 34 943
B.G. Guimarães Brazil 21 864 2.1× 85 0.6× 143 1.4× 33 0.4× 59 0.8× 65 1.3k
Amr M. Karim Egypt 18 478 1.2× 107 0.8× 39 0.4× 179 2.1× 28 0.4× 35 1.1k
G. Paul Curley Ireland 16 279 0.7× 107 0.8× 41 0.4× 115 1.3× 103 1.3× 17 609
J. Richardson United Kingdom 18 567 1.4× 138 1.0× 22 0.2× 68 0.8× 25 0.3× 38 999
Andrés Palencia France 20 899 2.2× 63 0.5× 139 1.3× 124 1.4× 56 0.7× 39 1.2k
Catherine J. Merrick United Kingdom 18 973 2.4× 318 2.3× 44 0.4× 63 0.7× 115 1.5× 33 1.4k
Lu-Yun Lian United Kingdom 20 1.2k 3.0× 157 1.1× 136 1.3× 17 0.2× 106 1.4× 25 1.6k

Countries citing papers authored by Gotam K. Jarori

Since Specialization
Citations

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

Fields of papers citing papers by Gotam K. Jarori

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Gotam K. Jarori

This figure shows the co-authorship network connecting the top 25 collaborators of Gotam K. Jarori. A scholar is included among the top collaborators of Gotam K. Jarori 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 Gotam K. Jarori. Gotam K. Jarori 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.
Sahal, Dinkar, et al.. (2018). Strain-transcending neutralization of malaria parasite by antibodies against Plasmodium falciparum enolase. Malaria Journal. 17(1). 304–304. 15 indexed citations
2.
Jarori, Gotam K., et al.. (2015). Cloning, expression, purification and characterization of Plasmodium spp. glyceraldehyde-3-phosphate dehydrogenase. Protein Expression and Purification. 117. 17–25. 10 indexed citations
3.
Mukherjee, Debanjan, Pushpa Mishra, Mamata Joshi, et al.. (2015). EWGWS insert in Plasmodium falciparum ookinete surface enolase is involved in binding of PWWP containing peptides: Implications to mosquito midgut invasion by the parasite. Insect Biochemistry and Molecular Biology. 68. 13–22. 4 indexed citations
4.
DasSarma, Priya, et al.. (2015). Immunogenicity and protective potential of a Plasmodium spp. enolase peptide displayed on archaeal gas vesicle nanoparticles. Malaria Journal. 14(1). 406–406. 20 indexed citations
5.
Jarori, Gotam K., et al.. (2013). Food Vacuole Associated Enolase in Plasmodium Undergoes Multiple Post-Translational Modifications: Evidence for Atypical Ubiquitination. PLoS ONE. 8(8). e72687–e72687. 11 indexed citations
6.
Mout, Rubul, et al.. (2012). Anti-malarial activity of geldanamycin derivatives in mice infected with Plasmodium yoelii. Malaria Journal. 11(1). 54–54. 22 indexed citations
7.
Das, Sujaan, et al.. (2011). Plasmodium falciparum enolase complements yeast enolase functions and associates with the parasite food vacuole. Molecular and Biochemical Parasitology. 179(1). 8–17. 13 indexed citations
8.
Pal‐Bhowmick, Ipsita, et al.. (2009). Effect of deletion of a plant like pentapeptide insert on kinetic, structural and immunological properties of enolase from Plasmodium falciparum. Archives of Biochemistry and Biophysics. 485(2). 128–138. 21 indexed citations
9.
Mehta, Monika, et al.. (2009). Plant-like phosphofructokinase from Plasmodium falciparum belongs to a novel class of ATP-dependent enzymes. International Journal for Parasitology. 39(13). 1441–1453. 14 indexed citations
10.
Pal‐Bhowmick, Ipsita, Sadagopan Krishnan, & Gotam K. Jarori. (2007). Differential susceptibility of Plasmodium falciparum versus yeast and mammalian enolases to dissociation into active monomers. FEBS Journal. 274(8). 1932–1945. 16 indexed citations
11.
Pal‐Bhowmick, Ipsita, et al.. (2007). Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions. Malaria Journal. 6(1). 45–45. 58 indexed citations
12.
Xie, Yong, Dongmao Zhang, Gotam K. Jarori, V. Jo Davisson, & Dor Ben‐Amotz. (2004). The Raman detection of peptide tyrosine phosphorylation. Analytical Biochemistry. 332(1). 116–121. 49 indexed citations
13.
Maity, Haripada, Yan Lin, & Gotam K. Jarori. (2002). Structure of Triphosphoryl Nucleotide Bound at the Active Site of Yeast Hexokinase: 1H-Nuclear Magnetic Resonance Study. Journal of Protein Chemistry. 21(4). 265–277. 1 indexed citations
14.
Maity, Haripada & Gotam K. Jarori. (2002). Fluorescence quenching of dimeric and monomeric forms of yeast hexokinase (PII): effect of substrate binding steady-state and time-resolved fluorescence studies.. PubMed. 34(1). 43–60. 1 indexed citations
15.
Ray, Bruce D., Gotam K. Jarori, & D. N. Rao. (1999). Paramagnetic Effects on Nuclear Relaxation in Enzyme-Bound Co(II)–Adenine Nucleotide Complexes: Relative Contributions of Dipolar and Scalar Interactions. Journal of Magnetic Resonance. 136(1). 130–133.
16.
Murali, Nagarajan, Gotam K. Jarori, & D. N. Rao. (1994). Two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY) studies of nucleotide conformations in arginine kinase complexes. Biochemistry. 33(47). 14227–14236. 15 indexed citations
17.
18.
Jarori, Gotam K., et al.. (1991). Nature of primary product(s) of D‐glucose 6‐phosphate dehydrogenase reaction 13C and 31P NMR study. FEBS Letters. 278(2). 247–251. 10 indexed citations
19.
Jarori, Gotam K., et al.. (1990). Mapping of glucose and glucose‐6‐phosphate binding sites on bovine brain hexokinase. European Journal of Biochemistry. 188(1). 9–14. 8 indexed citations
20.
Mehta, Alka, Gotam K. Jarori, & Umakant W. Kenkare. (1988). Brain hexokinase has no preexisting allosteric site for glucose 6-phosphate.. Journal of Biological Chemistry. 263(30). 15492–15497. 15 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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