K. Ravi Acharya

15.2k total citations · 3 hit papers
272 papers, 12.0k citations indexed

About

K. Ravi Acharya is a scholar working on Molecular Biology, Immunology and Materials Chemistry. According to data from OpenAlex, K. Ravi Acharya has authored 272 papers receiving a total of 12.0k indexed citations (citations by other indexed papers that have themselves been cited), including 172 papers in Molecular Biology, 61 papers in Immunology and 44 papers in Materials Chemistry. Recurrent topics in K. Ravi Acharya's work include Enzyme Structure and Function (41 papers), Glycosylation and Glycoproteins Research (37 papers) and Toxin Mechanisms and Immunotoxins (28 papers). K. Ravi Acharya is often cited by papers focused on Enzyme Structure and Function (41 papers), Glycosylation and Glycoproteins Research (37 papers) and Toxin Mechanisms and Immunotoxins (28 papers). K. Ravi Acharya collaborates with scholars based in United Kingdom, United States and South Africa. K. Ravi Acharya's co-authors include Edward D. Sturrock, Sylva L. U. Schwager, R. Natesh, Keith Brew, Steven J. Ackerman, David I. Stuart, D.D. Leonidas, Kenneth P. Holbourn, Shalini Iyer and Anastassios C. Papageorgiou and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

K. Ravi Acharya

263 papers receiving 11.7k citations

Hit Papers

3 papers align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Crystal structure of the human angiotensin-converting enzyme–lisinopril complex

2003 712 citations R. Natesh, Sylva L. U. Schwager et al. profile →
ANG mutations segregate with familial and 'sporadic' amyotrophic lateral sclerosis

2006 518 citations K. Ravi Acharya et al. profile →
Eosinophil Granule Proteins: Form and Function

2014 371 citations K. Ravi Acharya, Steven J. Ackerman Journal of Biological Chemistry profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
K. Ravi Acharya United Kingdom	58	7.1k	1.9k	1.2k	1.2k	1.1k	272	12.0k
Fuyuhiko Inagaki Japan	64	7.3k 1.0×	2.3k 1.2×	636 0.5×	854 0.7×	2.1k 2.0×	329	14.6k
Yasushi Ishihama Japan	61	13.7k 1.9×	1.3k 0.7×	437 0.4×	893 0.7×	448 0.4×	253	21.5k
Walter Chazin United States	74	12.0k 1.7×	2.0k 1.0×	178 0.1×	1.1k 0.9×	406 0.4×	292	16.2k
Luke Whitesell United States	59	10.3k 1.5×	4.2k 2.2×	319 0.3×	780 0.6×	453 0.4×	147	15.8k
Len Neckers United States	85	19.4k 2.7×	4.0k 2.1×	368 0.3×	1.5k 1.2×	644 0.6×	248	24.9k
Joël Vandekerckhove Belgium	80	13.6k 1.9×	2.3k 1.2×	301 0.2×	717 0.6×	322 0.3×	307	21.5k
Jane B. Trepel United States	74	11.8k 1.7×	2.2k 1.2×	664 0.5×	536 0.4×	439 0.4×	290	17.6k
Marja Jäättelä Denmark	80	15.2k 2.1×	3.0k 1.6×	418 0.3×	785 0.6×	472 0.4×	182	23.8k
Martino Bolognesi Italy	60	9.4k 1.3×	771 0.4×	194 0.2×	1.4k 1.2×	620 0.6×	430	14.9k
Bernhard Lohkamp Sweden	15	16.0k 2.3×	1.8k 1.0×	174 0.1×	4.0k 3.3×	1.1k 1.0×	26	22.3k

Countries citing papers authored by K. Ravi Acharya

Since Specialization

Citations

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

Fields of papers citing papers by K. Ravi Acharya

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of K. Ravi Acharya

This figure shows the co-authorship network connecting the top 25 collaborators of K. Ravi Acharya. A scholar is included among the top collaborators of K. Ravi Acharya 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 K. Ravi Acharya. K. Ravi Acharya 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

Cozier, Gyles E., et al.. (2025). Molecular basis of human angiotensin‐1 converting enzyme inhibition by a series of diprolyl‐derived compounds. FEBS Journal. 292(5). 1141–1158.

Acharya, K. Ravi, et al.. (2024). Advances in the structural basis for angiotensin-1 converting enzyme (ACE) inhibitors. Bioscience Reports. 44(8). 18 indexed citations

Acharya, K. Ravi, et al.. (2023). A Comprehensive Structural Analysis of Clostridium botulinum Neurotoxin A Cell-Binding Domain from Different Subtypes. Toxins. 15(2). 92–92. 7 indexed citations

Acharya, K. Ravi, et al.. (2023). Engineering Plastic Eating Enzymes Using Structural Biology. Biomolecules. 13(9). 1407–1407. 14 indexed citations

Isaac, R. Elwyn, et al.. (2023). A Molecular Analysis of the Aminopeptidase P-Related Domain of PID-5 from Caenorhabditis elegans. Biomolecules. 13(7). 1132–1132. 1 indexed citations

Żukowska, Joanna, Stephen J. Moss, Vasanta Subramanian, & K. Ravi Acharya. (2023). Molecular basis of selective amyloid‐β degrading enzymes in Alzheimer's disease. FEBS Journal. 291(14). 2999–3029. 14 indexed citations

Liu, Sai, et al.. (2023). Crystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue from Enterococcus faecium: Potential Insights into Substrate Recognition. International Journal of Molecular Sciences. 24(16). 12721–12721.

Cozier, Gyles E., et al.. (2022). Structural basis for the inhibition of human angiotensin‐1 converting enzyme by fosinoprilat. FEBS Journal. 289(21). 6659–6671. 3 indexed citations

Liu, Sai, et al.. (2022). Structural Features of Clostridium botulinum Neurotoxin Subtype A2 Cell Binding Domain. Toxins. 14(5). 356–356. 7 indexed citations

10.

Holloway, Daniel E., et al.. (2019). The catalytic activity and secretion of zebrafish RNases are essential for their in vivo function in motor neurons and vasculature. Scientific Reports. 9(1). 1107–1107. 9 indexed citations

11.

Davies, Jonathan, et al.. (2018). High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA. PeerJ. 6. e4552–e4552. 10 indexed citations

12.

Cozier, Gyles E., et al.. (2017). The Design and Development of a Potent and Selective Novel Diprolyl Derivative That Binds to the N-Domain of Angiotensin-I Converting Enzyme. Journal of Medicinal Chemistry. 61(1). 344–359. 24 indexed citations

13.

Bradshaw, W.J., April K. Roberts, Clifford C. Shone, & K. Ravi Acharya. (2017). The structure of the S-layer of Clostridium difficile. Journal of Cell Communication and Signaling. 12(1). 319–331. 37 indexed citations

14.

Michaud, Annie, K. Ravi Acharya, Geoffrey Masuyer, et al.. (2013). Absence of cell surface expression of human ACE leads to perinatal death. Human Molecular Genetics. 23(6). 1479–1491. 14 indexed citations

15.

Iyer, Shalini, Robert Visse, Hideaki Nagase, & K. Ravi Acharya. (2006). Crystal Structure of an Active Form of Human MMP-1. Journal of Molecular Biology. 362(1). 78–88. 88 indexed citations

16.

Corradi, Hazel, Anne V. Corrigall, Ester Boix, et al.. (2006). Crystal Structure of Protoporphyrinogen Oxidase from Myxococcus xanthus and Its Complex with the Inhibitor Acifluorfen. Journal of Biological Chemistry. 281(50). 38625–38633. 57 indexed citations

17.

Natesh, R., Sylva L. U. Schwager, Hazel R. Evans, Edward D. Sturrock, & K. Ravi Acharya. (2004). Structural Details on the Binding of Antihypertensive Drugs Captopril and Enalaprilat to Human Testicular Angiotensin I-Converting Enzyme ^,. Biochemistry. 43(27). 8718–8724. 234 indexed citations

18.

Acharya, K. Ravi, Edward D. Sturrock, James Riordan, & Mario R. Ehlers. (2003). Ace revisited: A new target for structure-based drug design. Nature Reviews Drug Discovery. 2(11). 891–902. 259 indexed citations

19.

Russo, Aniello, et al.. (2001). Small Molecule Inhibitors of RNase A and Related Enzymes. Methods in enzymology on CD-ROM/Methods in enzymology. 341. 629–648. 44 indexed citations

20.

Leonidas, D.D., et al.. (1995). Crystal structure of human Charcot–Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure. 3(12). 1379–1393. 117 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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