R. Natesh

1.8k total citations · 1 hit paper
21 papers, 1.5k citations indexed

About

R. Natesh is a scholar working on Molecular Biology, Oncology and Materials Chemistry. According to data from OpenAlex, R. Natesh has authored 21 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 5 papers in Oncology and 5 papers in Materials Chemistry. Recurrent topics in R. Natesh's work include Glycosylation and Glycoproteins Research (3 papers), Peptidase Inhibition and Analysis (3 papers) and Renin-Angiotensin System Studies (3 papers). R. Natesh is often cited by papers focused on Glycosylation and Glycoproteins Research (3 papers), Peptidase Inhibition and Analysis (3 papers) and Renin-Angiotensin System Studies (3 papers). R. Natesh collaborates with scholars based in United Kingdom, India and United States. R. Natesh's co-authors include K. Ravi Acharya, Edward D. Sturrock, Sylva L. U. Schwager, Hazel R. Evans, Jason van Rooyen, G. Jawahar Swaminathan, Ester Boix, Yingnan Zhang, Keith Brew and M. A. Viswamitra and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

R. Natesh

20 papers receiving 1.4k citations

Hit 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. Nature profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
R. Natesh United Kingdom	12	1.1k	266	242	220	211	21	1.5k
Sylva L. U. Schwager South Africa	24	1.6k 1.5×	465 1.7×	337 1.4×	572 2.6×	193 0.9×	45	2.3k
Xu Shen China	31	1.6k 1.4×	207 0.8×	58 0.2×	30 0.1×	392 1.9×	66	2.3k
Saori Takahashi Japan	22	814 0.7×	28 0.1×	39 0.2×	234 1.1×	111 0.5×	95	1.6k
Jin‐Cherng Lien Taiwan	27	959 0.9×	34 0.1×	63 0.3×	59 0.3×	529 2.5×	113	2.1k
Wibke E. Diederich Germany	22	842 0.8×	184 0.7×	26 0.1×	58 0.3×	247 1.2×	55	1.6k
Yamei Yu China	27	842 0.8×	48 0.2×	31 0.1×	42 0.2×	377 1.8×	81	2.0k
Sarah Naomi Bolz Germany	8	757 0.7×	300 1.1×	30 0.1×	20 0.1×	249 1.2×	12	1.4k
Peter C. Gareiss United States	17	1.7k 1.6×	117 0.4×	20 0.1×	47 0.2×	328 1.6×	26	2.2k
Bibha Choudhary India	27	1.7k 1.6×	65 0.2×	33 0.1×	16 0.1×	381 1.8×	92	2.6k
Richard J. Sciotti United States	25	537 0.5×	95 0.4×	44 0.2×	12 0.1×	623 3.0×	48	1.6k

Countries citing papers authored by R. Natesh

Since Specialization

Citations

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

Fields of papers citing papers by R. Natesh

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of R. Natesh

This figure shows the co-authorship network connecting the top 25 collaborators of R. Natesh. A scholar is included among the top collaborators of R. Natesh 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 R. Natesh. R. Natesh 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

Natesh, R., et al.. (2024). Efficient ROS Scavenging Improves the Growth and Yield in Black Gram (Vigna mungo (L.) Hepper) after Seed Priming and Treatment using Biosynthesized Silver Nanoparticles with Pongamia pinnata (L.) Pierre Leaf Extract. Journal of Plant Growth Regulation. 43(7). 2422–2438. 5 indexed citations

Natesh, R., et al.. (2024). HrpY protein of Ralstonia solanacearum exhibits spontaneous formation of pilus like assembly: analysis of its stability. Journal of Biomolecular Structure and Dynamics. 43(9). 4591–4602.

Natesh, R., et al.. (2021). Optimization strategies for expression and purification of soluble N-terminal domain of human centriolar protein SAS-6 in Escherichia coli. Protein Expression and Purification. 183. 105856–105856. 2 indexed citations

Dhar, Suman Kumar, et al.. (2021). Role of unique loops in oligomerization and ATPase function of Plasmodium falciparum gyrase B. Protein Science. 31(2). 323–332. 3 indexed citations

Natesh, R., et al.. (2021). Stability of p53 oligomers: Tetramerization of p53 impinges on its stability. Biochimie. 189. 99–107. 2 indexed citations

Nagaraja, Valakunja, et al.. (2019). Mycobacterial transcript cleavage factor Gre, exhibits chaperone-like activity. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1867(9). 757–764. 3 indexed citations

Natesh, R., Daniel K. Clare, George W. Farr, Arthur L. Horwich, & Helen R. Saibil. (2018). A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin. International Journal of Biological Macromolecules. 118(Pt A). 671–675. 8 indexed citations

Natesh, R., et al.. (2018). Phosphomimetic Mutation Destabilizes the Central Core Domain of Human p53. IUBMB Life. 70(10). 1023–1031. 4 indexed citations

Gu, Steven, Suneela Ramineni, David M. Thal, et al.. (2007). Unique Hydrophobic Extension of the RGS2 Amphipathic Helix Domain Imparts Increased Plasma Membrane Binding and Function Relative to Other RGS R4/B Subfamily Members. Journal of Biological Chemistry. 282(45). 33064–33075. 30 indexed citations

10.

Watermeyer, Jean M., B.T. Sewell, Sylva L. U. Schwager, et al.. (2006). Structure of Testis ACE Glycosylation Mutants and Evidence for Conserved Domain Movement^,. Biochemistry. 45(42). 12654–12663. 49 indexed citations

11.

Balyasnikova, Irina V., Zenda Woodman, Ronald F. Albrecht, et al.. (2005). Localization of an N-Domain Region of Angiotensin-Converting Enzyme Involved in the Regulation of Ectodomain Shedding Using Monoclonal Antibodies. Journal of Proteome Research. 4(2). 258–267. 26 indexed citations

12.

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

13.

Sturrock, Edward D., R. Natesh, Jason van Rooyen, & K. Ravi Acharya. (2004). What’s new in the renin-angiotensin system?. Cellular and Molecular Life Sciences. 61(21). 2677–2686. 81 indexed citations

14.

Natesh, R., Sylva L. U. Schwager, Edward D. Sturrock, & K. Ravi Acharya. (2003). Crystal structure of the human angiotensin-converting enzyme–lisinopril complex. Nature. 421(6922). 551–554. 712 indexed citations breakdown →

15.

Redelinghuys, Pierre, Sylva L. U. Schwager, Mario R. Ehlers, et al.. (2003). Deglycosylation, processing and crystallization of human testis angiotensin-converting enzyme. Biochemical Journal. 371(2). 437–442. 54 indexed citations

16.

Zhang, Yingnan, G. Jawahar Swaminathan, Ashlesha Deshpande, et al.. (2003). Roles of Individual Enzyme−Substrate Interactions by α-1,3-Galactosyltransferase in Catalysis and Specificity^,. Biochemistry. 42(46). 13512–13521. 48 indexed citations

17.

Natesh, R., et al.. (2002). Thermostable xylanase fromThermoascus aurantiacusat ultrahigh resolution (0.89 Å) at 100 K and atomic resolution (1.11 Å) at 293 K refined anisotropically to small-molecule accuracy. Acta Crystallographica Section D Biological Crystallography. 59(1). 105–117. 23 indexed citations

18.

Boix, Ester, G. Jawahar Swaminathan, Yingnan Zhang, et al.. (2001). Structure of UDP Complex of UDP-galactose:β-Galactoside-α-1,3-galactosyltransferase at 1.53-Å Resolution Reveals a Conformational Change in the Catalytically Important C Terminus. Journal of Biological Chemistry. 276(51). 48608–48614. 80 indexed citations

19.

Natesh, R., et al.. (1999). Crystal structure at 1.8 Å resolution and proposed amino acid sequence of a thermostable xylanase from Thermoascus aurantiacus. Journal of Molecular Biology. 288(5). 999–1012. 53 indexed citations

20.

Natesh, R. & G. S. Ansell. (1966). Oxide growth in a AlAl2O3 SAP-type alloy by hot stage transmission electron microscopy. Acta Metallurgica. 14(12). 1735–1756. 2 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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