Vasundara Srinivasan

1.9k total citations
21 papers, 1.1k citations indexed

About

Vasundara Srinivasan is a scholar working on Molecular Biology, Nutrition and Dietetics and Oncology. According to data from OpenAlex, Vasundara Srinivasan has authored 21 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 8 papers in Nutrition and Dietetics and 4 papers in Oncology. Recurrent topics in Vasundara Srinivasan's work include Trace Elements in Health (8 papers), Drug Transport and Resistance Mechanisms (4 papers) and Iron Metabolism and Disorders (4 papers). Vasundara Srinivasan is often cited by papers focused on Trace Elements in Health (8 papers), Drug Transport and Resistance Mechanisms (4 papers) and Iron Metabolism and Disorders (4 papers). Vasundara Srinivasan collaborates with scholars based in Germany, Belgium and United States. Vasundara Srinivasan's co-authors include Roland Lill, Antonio J. Pierik, Ulrich Mühlenhoff, Jan Steyaert, Daili J. A. Netz, Judita Mascarenhas, John N. Barlow, David Oyen, Els Pardon and Martin Stümpfig and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and The EMBO Journal.

In The Last Decade

Vasundara Srinivasan

21 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Vasundara Srinivasan Germany 16 726 229 218 144 122 21 1.1k
Manuele Martinelli Italy 17 844 1.2× 386 1.7× 52 0.2× 115 0.8× 107 0.9× 25 1.8k
Balu Kamaraj India 21 617 0.8× 90 0.4× 120 0.6× 89 0.6× 51 0.4× 45 1.1k
G. E. Morozevich Russia 16 470 0.6× 124 0.5× 167 0.8× 151 1.0× 25 0.2× 56 1.6k
Kourosh Honarmand Ebrahimi United Kingdom 19 508 0.7× 239 1.0× 92 0.4× 69 0.5× 78 0.6× 42 972
Jérôme Dupuy France 16 593 0.8× 201 0.9× 56 0.3× 45 0.3× 117 1.0× 23 1.3k
Andreas Becker United States 20 1.1k 1.5× 27 0.1× 119 0.5× 367 2.5× 153 1.3× 23 1.6k
Kevin G. Hoff United States 19 1.4k 1.9× 324 1.4× 702 3.2× 103 0.7× 253 2.1× 22 2.1k
Ludovic Pecqueur France 19 571 0.8× 72 0.3× 282 1.3× 33 0.2× 97 0.8× 31 970
Markus Eser United States 10 655 0.9× 81 0.4× 18 0.1× 161 1.1× 138 1.1× 17 955
Kostas Tokatlidis Greece 33 2.7k 3.8× 180 0.8× 116 0.5× 62 0.4× 163 1.3× 69 3.2k

Countries citing papers authored by Vasundara Srinivasan

Since Specialization
Citations

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

Fields of papers citing papers by Vasundara Srinivasan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Vasundara Srinivasan

This figure shows the co-authorship network connecting the top 25 collaborators of Vasundara Srinivasan. A scholar is included among the top collaborators of Vasundara 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 Vasundara Srinivasan. Vasundara Srinivasan 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.
Fu, Zhenglin, Thomas Güttler, S. Trakhanov, et al.. (2024). A checkpoint function for Nup98 in nuclear pore formation suggested by novel inhibitory nanobodies. The EMBO Journal. 43(11). 2198–2232. 4 indexed citations
2.
Ewert, Wiebke, Sebastian Günther, Sven Falke, et al.. (2022). Hydrazones and Thiosemicarbazones Targeting Protein-Protein-Interactions of SARS-CoV-2 Papain-like Protease. Frontiers in Chemistry. 10. 832431–832431. 13 indexed citations
3.
Srinivasan, Vasundara, et al.. (2021). Conformational changes in the yeast mitochondrial ABC transporter Atm1 during the transport cycle. Science Advances. 7(52). eabk2392–eabk2392. 10 indexed citations
4.
Schmermund, Luca, et al.. (2019). Directed Evolution of an Fe II -Dependent Halogenase for Asymmetric C(sp 3 )–H Chlorination. ACS Catalysis. 10(2). 1272–1277. 47 indexed citations
5.
Albert, Lea, et al.. (2017). Controlled inhibition of methyltransferases using photoswitchable peptidomimetics: towards an epigenetic regulation of leukemia. Chemical Science. 8(6). 4612–4618. 42 indexed citations
6.
Lill, Roland, Rafał Dutkiewicz, Sven‐Andreas Freibert, et al.. (2015). The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron–sulfur proteins. European Journal of Cell Biology. 94(7-9). 280–291. 143 indexed citations
7.
Schaedler, Theresia A., C.A. Shintre, Elisabeth P. Carpenter, et al.. (2015). Structures and functions of mitochondrial ABC transporters. Biochemical Society Transactions. 43(5). 943–951. 55 indexed citations
8.
Steinchen, Wieland, Jan S. Schuhmacher, Florian Altegoer, et al.. (2015). Catalytic mechanism and allosteric regulation of an oligomeric (p)ppGpp synthetase by an alarmone. Proceedings of the National Academy of Sciences. 112(43). 13348–13353. 87 indexed citations
9.
10.
Lill, Roland, Vasundara Srinivasan, & Ulrich Mühlenhoff. (2014). The role of mitochondria in cytosolic-nuclear iron–sulfur protein biogenesis and in cellular iron regulation. Current Opinion in Microbiology. 22. 111–119. 102 indexed citations
11.
Srinivasan, Vasundara, Antonio J. Pierik, & Roland Lill. (2014). Crystal Structures of Nucleotide-Free and Glutathione-Bound Mitochondrial ABC Transporter Atm1. Science. 343(6175). 1137–1140. 172 indexed citations
12.
Oyen, David, Rainer Wechselberger, Vasundara Srinivasan, Jan Steyaert, & John N. Barlow. (2013). Mechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihydrofolate reductase of Escherichia coli. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834(10). 2147–2157. 28 indexed citations
13.
Chevigné, Andy, Els Pardon, Vasundara Srinivasan, et al.. (2013). Allosteric inhibition of VIM metallo-β-lactamases by a camelid nanobody. Biochemical Journal. 450(3). 477–486. 26 indexed citations
14.
Srinivasan, Vasundara, Els Pardon, Florine Dupeux, et al.. (2011). Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic β2-microglobulin variant. Proceedings of the National Academy of Sciences. 108(4). 1314–1319. 97 indexed citations
15.
Oyen, David, Vasundara Srinivasan, Jan Steyaert, & John N. Barlow. (2011). Constraining Enzyme Conformational Change by an Antibody Leads to Hyperbolic Inhibition. Journal of Molecular Biology. 407(1). 138–148. 30 indexed citations
16.
Clercq, Sarah De, Veerle De Corte, Sameh H. Soror, et al.. (2010). A llama-derived gelsolin single-domain antibody blocks gelsolin–G-actin interaction. Cellular and Molecular Life Sciences. 67(9). 1519–1535. 49 indexed citations
17.
Cherezov, Vadim, Doletha M. E. Szebenyi, J. Gerard Wall, et al.. (2008). Insights into the Mode of Action of a Putative Zinc Transporter CzrB in Thermus thermophilus. Structure. 16(9). 1378–1388. 73 indexed citations
18.
Srinivasan, Vasundara, Daili J. A. Netz, Holger Webert, et al.. (2007). Structure of the Yeast WD40 Domain Protein Cia1, a Component Acting Late in Iron-Sulfur Protein Biogenesis. Structure. 15(10). 1246–1257. 60 indexed citations
19.
Srinivasan, Vasundara, Chitra Rajendran, Filipa L. Sousa, et al.. (2004). Structure at 1.3Å Resolution of Rhodothermus marinus caa3 Cytochrome c Domain. Journal of Molecular Biology. 345(5). 1047–1057. 15 indexed citations
20.
Srinivasan, Vasundara, Kesen Ma, Michael W. W. Adams, et al.. (2002). Towards the crystal structure of glycerol dehydrogenase fromThermotoga maritima. Acta Crystallographica Section D Biological Crystallography. 58(5). 867–869. 5 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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