A. Seetharama Acharya

2.1k total citations
86 papers, 1.6k citations indexed

About

A. Seetharama Acharya is a scholar working on Molecular Biology, Cell Biology and Genetics. According to data from OpenAlex, A. Seetharama Acharya has authored 86 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 55 papers in Molecular Biology, 52 papers in Cell Biology and 17 papers in Genetics. Recurrent topics in A. Seetharama Acharya's work include Hemoglobin structure and function (48 papers), Protein Structure and Dynamics (19 papers) and Hemoglobinopathies and Related Disorders (17 papers). A. Seetharama Acharya is often cited by papers focused on Hemoglobin structure and function (48 papers), Protein Structure and Dynamics (19 papers) and Hemoglobinopathies and Related Disorders (17 papers). A. Seetharama Acharya collaborates with scholars based in United States, India and Russia. A. Seetharama Acharya's co-authors include James M. Manning, Belur N. Manjula, Hiroshi Taniuchi, Peter B. Moore, Rajendra P. Roy, Ramnath Seetharam, Thomas Fairwell, R Benesch, Ashok Malavalli and V A Fischetti and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Experimental Medicine.

In The Last Decade

A. Seetharama Acharya

85 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
A. Seetharama Acharya United States 23 934 668 306 225 197 86 1.6k
Giovanna Valentini Italy 22 952 1.0× 137 0.2× 522 1.7× 143 0.6× 233 1.2× 58 1.7k
Alina D. Zamfir Romania 32 1.9k 2.0× 797 1.2× 275 0.9× 56 0.2× 60 0.3× 127 2.8k
Richard L. Cysyk United States 22 977 1.0× 138 0.2× 49 0.2× 33 0.1× 77 0.4× 72 1.5k
Hans JÖRNVALL Sweden 24 828 0.9× 207 0.3× 73 0.2× 44 0.2× 40 0.2× 45 1.4k
G.J. Howlett Australia 20 841 0.9× 162 0.2× 138 0.5× 33 0.1× 25 0.1× 34 1.3k
Kent Lai United States 26 747 0.8× 171 0.3× 148 0.5× 46 0.2× 386 2.0× 64 1.7k
Rajam S. Mani Canada 24 1.7k 1.8× 179 0.3× 52 0.2× 69 0.3× 57 0.3× 69 2.3k
K. Heide Germany 17 590 0.6× 225 0.3× 106 0.3× 141 0.6× 26 0.1× 48 1.2k
Lawrence W. Anderson United States 23 728 0.8× 97 0.1× 35 0.1× 51 0.2× 73 0.4× 57 1.5k
N L Anderson United States 23 1.5k 1.6× 196 0.3× 97 0.3× 49 0.2× 22 0.1× 36 2.1k

Countries citing papers authored by A. Seetharama Acharya

Since Specialization
Citations

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

Fields of papers citing papers by A. Seetharama Acharya

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of A. Seetharama Acharya

This figure shows the co-authorship network connecting the top 25 collaborators of A. Seetharama Acharya. A scholar is included among the top collaborators of A. Seetharama 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 A. Seetharama Acharya. A. Seetharama Acharya 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.
2.
Li, Dongxia, Belur N. Manjula, & A. Seetharama Acharya. (2006). Extension Arm Facilitated PEGylation of Hemoglobin: Correlation of the Properties with the Extent of PEGylation. The Protein Journal. 25(4). 263–274. 39 indexed citations
3.
Acharya, A. Seetharama, et al.. (2002). Product‐conformation‐driven ligation of peptides by V8 protease. Protein Science. 11(6). 1384–1392. 3 indexed citations
4.
Manjula, Belur N., et al.. (2001). Activation of the low oxygen affinity-inducing potential of the Asn108(β)→Lys mutation of Hb-Presbyterian on intramolecular αα-fumaryl cross-bridging. Protein Engineering Design and Selection. 14(5). 359–366. 3 indexed citations
5.
Manjula, Belur N., Ashok Malavalli, Paul K. Smith, et al.. (2000). Cys-93-ββ-Succinimidophenyl Polyethylene Glycol 2000 Hemoglobin A. Journal of Biological Chemistry. 275(8). 5527–5534. 33 indexed citations
6.
Malavalli, Ashok, et al.. (1999). Inhibition of βS-chain dependent polymerization by synergistic complementation of contact site perturbations of α-chain: application of semisynthetic chimeric α-chains. Protein Engineering Design and Selection. 12(12). 1105–1111. 5 indexed citations
7.
Gottfried, David, et al.. (1997). Probing the Hemoglobin Central Cavity by Direct Quantification of Effector Binding Using Fluorescence Lifetime Methods. Journal of Biological Chemistry. 272(3). 1571–1578. 18 indexed citations
8.
Nacharaju, Parimala, Rajendra P. Roy, Steven P. White, Ronald L. Nagel, & A. Seetharama Acharya. (1997). Inhibition of Sickle β-Chain (βS)-dependent Polymerization by Nonhuman α-Chains. Journal of Biological Chemistry. 272(44). 27869–27876. 12 indexed citations
9.
Rao, Mingjun, et al.. (1995). Polymerization of Hemoglobin S. Journal of Biological Chemistry. 270(33). 19250–19255. 10 indexed citations
10.
Roy, Rajendra P. & A. Seetharama Acharya. (1994). [12] Semisynthesis of hemoglobin. Methods in enzymology on CD-ROM/Methods in enzymology. 231. 194–215. 17 indexed citations
11.
Roy, Rajendra P., Kiran Khandke, Belur N. Manjula, & A. Seetharama Acharya. (1992). Helix formation in enzymically ligated peptides as a driving force for the synthetic reaction: example of .alpha.-globin semisynthetic reaction. Biochemistry. 31(32). 7249–7255. 12 indexed citations
12.
Mallia, A. Krishna, et al.. (1991). Proteosynthetic activity of immobilized Staphylococcus aureus V8 protease: Application in the semisynthesis of molecular variants of α-globin. Analytical Biochemistry. 193(2). 178–185. 6 indexed citations
13.
Khandke, Kiran, Thomas Fairwell, A. Seetharama Acharya, & Belur N. Manjula. (1990). Domain structure and molecular flexibility of streptococcal M proteinIn Situ probed by limited proteolysis. Journal of Protein Chemistry. 9(5). 511–522. 3 indexed citations
14.
Acharya, A. Seetharama & Lakshmi Khandke. (1989). Selective amidation of carboxyl groups of the intermolecular contact regions of hemoglobin S: Structural aspects. Journal of Protein Chemistry. 8(2). 231–237. 3 indexed citations
15.
Khan, Shabbir Ahmed, et al.. (1989). Semisynthetic hemoglobin A: reconstitution of functional tetramer from semisynthetic .alpha.-globin. Biochemistry. 28(13). 5456–5461. 20 indexed citations
16.
Fairwell, Thomas, et al.. (1988). Domain structure of streptococcal M protein: Correlation with sites of limited proteolysis with pepsin. Journal of Protein Chemistry. 7(3). 262–263. 1 indexed citations
17.
Acharya, A. Seetharama, et al.. (1984). The reversibility of the ketoamine linkages of aldoses with proteins.. Journal of Biological Chemistry. 259(7). 4372–4378. 31 indexed citations
18.
Seetharam, Ramnath, James M. Manning, & A. Seetharama Acharya. (1983). Specific modification of the carboxyl groups of hemoglobin S.. Journal of Biological Chemistry. 258(24). 14810–14815. 14 indexed citations
19.
Benesch, R, R Benesch, Suzanna Kwong, A. Seetharama Acharya, & James M. Manning. (1982). Labeling of hemoglobin with pyridoxal phosphate.. Journal of Biological Chemistry. 257(3). 1320–1324. 64 indexed citations
20.
Acharya, A. Seetharama & Hiroshi Taniuchi. (1978). Reduction and renaturation of hen egg lysozyme containing carboxymethylcysteine-6 and -127. Biochemistry. 17(15). 3064–3070. 17 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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