Kutti R. Vinothkumar

3.1k total citations · 1 hit paper
40 papers, 2.2k citations indexed

About

Kutti R. Vinothkumar is a scholar working on Molecular Biology, Materials Chemistry and Structural Biology. According to data from OpenAlex, Kutti R. Vinothkumar has authored 40 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 7 papers in Materials Chemistry and 6 papers in Structural Biology. Recurrent topics in Kutti R. Vinothkumar's work include Photosynthetic Processes and Mechanisms (7 papers), Protein Structure and Dynamics (6 papers) and Mitochondrial Function and Pathology (6 papers). Kutti R. Vinothkumar is often cited by papers focused on Photosynthetic Processes and Mechanisms (7 papers), Protein Structure and Dynamics (6 papers) and Mitochondrial Function and Pathology (6 papers). Kutti R. Vinothkumar collaborates with scholars based in United Kingdom, India and United States. Kutti R. Vinothkumar's co-authors include Judy Hirst, Jiapeng Zhu, Richard A. Henderson, Werner Kühlbrandt, Özkan Yıldız, Panchali Goswami, James N. Blaza, Matthew Freeman, Steven H. L. Verhelst and Greg McMullan and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Kutti R. Vinothkumar

40 papers receiving 2.2k citations

Hit Papers

Structure of mammalian respiratory complex I 2016 2026 2019 2022 2016 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kutti R. Vinothkumar United Kingdom 20 1.6k 257 218 197 156 40 2.2k
M.G. Iadanza United Kingdom 18 1.4k 0.8× 222 0.9× 143 0.7× 466 2.4× 157 1.0× 21 2.1k
Prashant Rao United States 25 1.8k 1.1× 365 1.4× 79 0.4× 301 1.5× 166 1.1× 41 2.3k
Alexey Amunts Sweden 30 3.4k 2.1× 210 0.8× 48 0.2× 231 1.2× 178 1.1× 57 3.7k
Soojay Banerjee United States 21 2.5k 1.5× 681 2.6× 84 0.4× 461 2.3× 121 0.8× 24 3.7k
Ashwin Chari Germany 28 2.3k 1.4× 403 1.6× 73 0.3× 319 1.6× 92 0.6× 44 2.9k
Kaoru Mitsuoka Japan 25 2.4k 1.4× 303 1.2× 112 0.5× 332 1.7× 182 1.2× 61 3.2k
Joanna Kirkpatrick Germany 21 1.2k 0.7× 145 0.6× 169 0.8× 53 0.3× 121 0.8× 50 1.8k
Teruhisa Hirai Japan 23 2.5k 1.5× 199 0.8× 182 0.8× 429 2.2× 272 1.7× 52 3.6k
Terrence Frey United States 20 1.8k 1.1× 163 0.6× 72 0.3× 182 0.9× 28 0.2× 41 2.5k
Christoph von Ballmoos Switzerland 30 2.0k 1.2× 67 0.3× 94 0.4× 172 0.9× 206 1.3× 69 2.6k

Countries citing papers authored by Kutti R. Vinothkumar

Since Specialization
Citations

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

Fields of papers citing papers by Kutti R. Vinothkumar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Kutti R. Vinothkumar. 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 Kutti R. Vinothkumar. The network helps show where Kutti R. Vinothkumar may publish in the future.

Co-authorship network of co-authors of Kutti R. Vinothkumar

This figure shows the co-authorship network connecting the top 25 collaborators of Kutti R. Vinothkumar. A scholar is included among the top collaborators of Kutti R. Vinothkumar 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 Kutti R. Vinothkumar. Kutti R. Vinothkumar 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.
Goyal, Parveen, Mariafrancesca Scalise, Rosmarie Friemann, et al.. (2025). Molecular determinants of Neu5Ac binding to a tripartite ATP independent periplasmic (TRAP) transporter. eLife. 13. 1 indexed citations
2.
Vinothkumar, Kutti R., et al.. (2025). An Oryza-specific histone H4 variant predisposes H4 lysine 5 acetylation to modulate salt stress responses. Nature Plants. 11(4). 790–807. 3 indexed citations
3.
Vinothkumar, Kutti R., et al.. (2024). Factors affecting macromolecule orientations in thin films formed in cryo-EM. Acta Crystallographica Section D Structural Biology. 80(7). 535–550. 1 indexed citations
4.
Yeramala, Lahari, et al.. (2023). Regulatory mechanisms of c‐di‐AMP synthase from Mycobacterium smegmatis revealed by a structure: Function analysis. Protein Science. 32(3). e4568–e4568. 3 indexed citations
5.
6.
Fine, Jonathan, Ana Casañal, Gaurav Chopra, et al.. (2020). A 2‐Tyr‐1‐carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase. Angewandte Chemie. 132(39). 17109–17114. 1 indexed citations
7.
Fine, Jonathan, Ana Casañal, Gaurav Chopra, et al.. (2020). A 2‐Tyr‐1‐carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase. Angewandte Chemie International Edition. 59(39). 16961–16966. 11 indexed citations
8.
Vinothkumar, Kutti R., et al.. (2020). Comparison of CryoEM and X-ray structures of dimethylformamidase. Progress in Biophysics and Molecular Biology. 160. 66–78. 3 indexed citations
9.
Cannone, Giuseppe, et al.. (2019). Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway. Nature Communications. 10(1). 4127–4127. 18 indexed citations
10.
Itoh, Yuzuru, et al.. (2019). Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC. Nature Communications. 10(1). 15 indexed citations
11.
Blaza, James N., Kutti R. Vinothkumar, & Judy Hirst. (2018). Structure of the Deactive State of Mammalian Respiratory Complex I. Structure. 26(2). 312–319.e3. 101 indexed citations
12.
Vinothkumar, Kutti R. & Richard A. Henderson. (2016). Single particle electron cryomicroscopy: trends, issues and future perspective. Quarterly Reviews of Biophysics. 49. e13–e13. 137 indexed citations
13.
Vinothkumar, Kutti R.. (2015). Membrane protein structures without crystals, by single particle electron cryomicroscopy. Current Opinion in Structural Biology. 33. 103–114. 43 indexed citations
14.
Vinothkumar, Kutti R., Greg McMullan, & Richard A. Henderson. (2014). Molecular Mechanism of Antibody-Mediated Activation of β-galactosidase. Structure. 22(4). 621–627. 23 indexed citations
15.
Vinothkumar, Kutti R. & Matthew Freeman. (2013). Intramembrane proteolysis by rhomboids: catalytic mechanisms and regulatory principles. Current Opinion in Structural Biology. 23(6). 851–858. 10 indexed citations
16.
Vinothkumar, Kutti R.. (2011). Structure of Rhomboid Protease in a Lipid Environment. Journal of Molecular Biology. 407(2). 232–247. 72 indexed citations
17.
Vinothkumar, Kutti R. & Richard A. Henderson. (2010). Structures of membrane proteins. Quarterly Reviews of Biophysics. 43(1). 65–158. 129 indexed citations
18.
Vinothkumar, Kutti R., Kvido Střı́šovský, Antonina Andreeva, et al.. (2010). The structural basis for catalysis and substrate specificity of a rhomboid protease. The EMBO Journal. 29(22). 3797–3809. 87 indexed citations
19.
Vinothkumar, Kutti R., et al.. (2008). Conformations of NhaA, the Na/H Exchanger from Escherichia coli, in the pH-Activated and Ion-Translocating States. Journal of Molecular Biology. 386(2). 351–365. 61 indexed citations
20.
Yıldız, Özkan, Kutti R. Vinothkumar, Panchali Goswami, & Werner Kühlbrandt. (2006). Structure of the monomeric outer‐membrane porin OmpG in the open and closed conformation. The EMBO Journal. 25(15). 3702–3713. 138 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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