Santosh Panjikar

6.0k total citations
151 papers, 4.6k citations indexed

About

Santosh Panjikar is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Santosh Panjikar has authored 151 papers receiving a total of 4.6k indexed citations (citations by other indexed papers that have themselves been cited), including 109 papers in Molecular Biology, 66 papers in Materials Chemistry and 22 papers in Genetics. Recurrent topics in Santosh Panjikar's work include Enzyme Structure and Function (61 papers), Biochemical and Molecular Research (27 papers) and Protein Structure and Dynamics (24 papers). Santosh Panjikar is often cited by papers focused on Enzyme Structure and Function (61 papers), Biochemical and Molecular Research (27 papers) and Protein Structure and Dynamics (24 papers). Santosh Panjikar collaborates with scholars based in Australia, Germany and China. Santosh Panjikar's co-authors include Paul A. Tucker, Joachim Stöckigt, M.S. Weiss, Victor S. Lamzin, Venkataraman Parthasarathy, Elke A. Loris, Juergen Koepke, Xueyan Ma, Nathan Cowieson and Leif Barleben and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Santosh Panjikar

145 papers receiving 4.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Santosh Panjikar Australia	34	2.8k	1.0k	649	510	421	151	4.6k
Glaucius Oliva Brazil	40	3.0k 1.1×	674 0.7×	1.6k 2.4×	449 0.9×	482 1.1×	205	6.6k
Walter Filgueira de Azevedo Brazil	44	4.5k 1.6×	1.0k 1.0×	1.3k 2.0×	515 1.0×	506 1.2×	199	7.1k
Wulf Blankenfeldt Germany	38	3.1k 1.1×	406 0.4×	599 0.9×	470 0.9×	755 1.8×	147	4.9k
J.P. Turkenburg United Kingdom	43	5.2k 1.8×	863 0.8×	1.0k 1.6×	380 0.7×	238 0.6×	121	7.1k
William N. Hunter United Kingdom	49	5.5k 2.0×	981 1.0×	1.1k 1.8×	521 1.0×	510 1.2×	210	7.6k
J.A. Hermoso Spain	45	4.1k 1.5×	684 0.7×	928 1.4×	758 1.5×	313 0.7×	192	6.5k
David L. Ollis Australia	47	5.4k 1.9×	1.2k 1.2×	570 0.9×	938 1.8×	577 1.4×	140	7.9k
Tzu‐Ping Ko Taiwan	46	4.4k 1.6×	971 1.0×	596 0.9×	655 1.3×	821 2.0×	217	7.3k
Alexander W. Schüttelkopf United Kingdom	25	4.1k 1.5×	672 0.7×	1.3k 2.1×	281 0.6×	438 1.0×	32	6.3k
Vishal Verma United States	13	2.5k 0.9×	438 0.4×	1.2k 1.8×	299 0.6×	370 0.9×	28	4.4k

Countries citing papers authored by Santosh Panjikar

Since Specialization

Citations

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

Fields of papers citing papers by Santosh Panjikar

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Santosh Panjikar. 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 Santosh Panjikar. The network helps show where Santosh Panjikar may publish in the future.

Co-authorship network of co-authors of Santosh Panjikar

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Yadav, Arti, Santosh Panjikar, & R.K. Singh Raman. (2025). Graphene-Based Impregnation into Polymeric Coating for Corrosion Resistance. Nanomaterials. 15(7). 486–486. 6 indexed citations

Panjikar, Santosh, et al.. (2025). Immobilisation of bovine serum albumin on graphene oxide through covalent and noncovalent interactions. Colloids and Surfaces B Biointerfaces. 258. 115203–115203.

Currie, Michael, Santosh Panjikar, Rosmarie Friemann, et al.. (2024). On the function of TRAP substrate-binding proteins: Conformational variation of the sialic acid binding protein SiaP. Journal of Biological Chemistry. 300(11). 107851–107851. 2 indexed citations

Lee, Mihwa, et al.. (2021). Differential lysine‐mediated allosteric regulation of plant dihydrodipicolinate synthase isoforms. FEBS Journal. 288(16). 4973–4986. 5 indexed citations

Sastry, Murali, et al.. (2021). Graphene and Graphene Oxide as a Support for Biomolecules in the Development of Biosensors. PubMed. Volume 14. 197–220. 105 indexed citations

Costa, Tatiana P. Soares da, Santosh Panjikar, Mark D. Hulett, et al.. (2021). Towards novel herbicide modes of action by inhibiting lysine biosynthesis in plants. eLife. 10. 14 indexed citations

Horne, Christopher R., Hariprasad Venugopal, Santosh Panjikar, et al.. (2021). Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism. Nature Communications. 12(1). 1988–1988. 22 indexed citations

Mills, Stuart J., Jun Aishima, David Aragão, et al.. (2020). Crystal structure of posnjakite formed in the first crystal water-cooling line of the ANSTO Melbourne Australian Synchrotron MX1 Double Crystal Monochromator. Acta Crystallographica Section E Crystallographic Communications. 76(7). 1136–1138. 1 indexed citations

Horne, Christopher R., Thanuja Gangi Setty, S. Ramaswamy, et al.. (2020). The basis for non-canonical ROK family function in the N-acetylmannosamine kinase from the pathogen Staphylococcus aureus. Journal of Biological Chemistry. 295(10). 3301–3315. 13 indexed citations

10.

Panjikar, Santosh, et al.. (2019). Combining random microseed matrix screening and the magic triangle for the efficient structure solution of a potential lysin from bacteriophage P68. Acta Crystallographica Section D Structural Biology. 75(7). 670–681. 3 indexed citations

11.

Traoré, Daouda A. K., Jessica A. Wisniewski, Paul J. Conroy, et al.. (2018). Crystal structure of TcpK in complex with oriT DNA of the antibiotic resistance plasmid pCW3. Nature Communications. 9(1). 3732–3732. 18 indexed citations

12.

Ellisdon, Andrew M., Cyril F. Reboul, Santosh Panjikar, et al.. (2015). Stonefish toxin defines an ancient branch of the perforin-like superfamily. Proceedings of the National Academy of Sciences. 112(50). 15360–15365. 50 indexed citations

13.

Palm, Gottfried J., Anurag Sharma, Moni Kumari, et al.. (2014). Post‐translational modification and extended glycosylation pattern of a plant latex peroxidase of native source characterized by X‐ray crystallography. FEBS Journal. 281(18). 4319–4333. 6 indexed citations

14.

Panjikar, Santosh, et al.. (2013). Importance of Hydrophobic Cavities in Allosteric Regulation of Formylglycinamide Synthetase: Insight from Xenon Trapping and Statistical Coupling Analysis. PLoS ONE. 8(11). e77781–e77781. 17 indexed citations

15.

Jeyakanthan, Jeyaraman, Subbiah Thamotharan, Santosh Panjikar, et al.. (2010). Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) fromAquifex aeolicusVF5. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(2). 184–186. 2 indexed citations

16.

Manolaridis, Ioannis, J.A. Wojdyla, Santosh Panjikar, et al.. (2009). Structure of the C-terminal domain of NSP4 from feline infection peritonitis virus. Acta Crystallographica Section A Foundations of Crystallography. 65(a1). s167–s167. 1 indexed citations

17.

Martínez‐Rodríguez, Sergio, Santosh Panjikar, Karolien Van Belle, et al.. (2008). Nonspecific base recognition mediated by water bridges and hydrophobic stacking in ribonuclease I from Escherichia coli. Protein Science. 17(4). 681–690. 8 indexed citations

18.

Koh, Cha San, Claude Didierjean, Nicolas Navrot, et al.. (2007). Crystal Structures of a Poplar Thioredoxin Peroxidase that Exhibits the Structure of Glutathione Peroxidases: Insights into Redox-driven Conformational Changes. Journal of Molecular Biology. 370(3). 512–529. 83 indexed citations

19.

Ma, Xueyan, Santosh Panjikar, Juergen Koepke, Elke A. Loris, & Joachim Stöckigt. (2006). The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins. The Plant Cell. 18(4). 907–920. 109 indexed citations

20.

Nowak, Elżbieta, et al.. (2006). Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis. Structure. 14(2). 275–285. 34 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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