T. Ramakrishna

3.0k total citations
68 papers, 2.5k citations indexed

About

T. Ramakrishna is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, T. Ramakrishna has authored 68 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 19 papers in Physiology and 13 papers in Materials Chemistry. Recurrent topics in T. Ramakrishna's work include Heat shock proteins research (34 papers), Connexins and lens biology (28 papers) and Enzyme Structure and Function (13 papers). T. Ramakrishna is often cited by papers focused on Heat shock proteins research (34 papers), Connexins and lens biology (28 papers) and Enzyme Structure and Function (13 papers). T. Ramakrishna collaborates with scholars based in India, Japan and United States. T. Ramakrishna's co-authors include Ch. Mohan Rao, Bakthisaran Raman, Saloni Pasta, Shabbir Ahmad, Tirumala Kumar Chowdary, K. Sridhar Rao, Rajaraman Krishnan, M.W. Pandit, Bhairab N. Singh and Nandini Rangaraj and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and PLoS ONE.

In The Last Decade

T. Ramakrishna

67 papers receiving 2.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
T. Ramakrishna India 28 2.1k 540 486 410 271 68 2.5k
Bakthisaran Raman India 27 2.2k 1.1× 496 0.9× 675 1.4× 467 1.1× 258 1.0× 46 2.6k
J. Andrew Aquilina Australia 33 2.3k 1.1× 418 0.8× 571 1.2× 476 1.2× 217 0.8× 61 2.9k
Anat Ben‐Zvi Israel 22 2.3k 1.1× 804 1.5× 422 0.9× 465 1.1× 191 0.7× 42 3.0k
Usha P. Andley United States 34 3.2k 1.5× 625 1.2× 608 1.3× 218 0.5× 504 1.9× 104 3.7k
Gudrun Lutsch Germany 24 2.6k 1.3× 504 0.9× 471 1.0× 250 0.6× 345 1.3× 45 3.1k
Jens Tyedmers Germany 18 1.7k 0.8× 694 1.3× 235 0.5× 189 0.5× 191 0.7× 28 2.2k
Bingdong Sha United States 27 1.9k 0.9× 754 1.4× 295 0.6× 223 0.5× 124 0.5× 54 2.5k
Nikolai B. Gusev Russia 37 3.3k 1.6× 982 1.8× 501 1.0× 550 1.3× 138 0.5× 148 4.4k
Daniel R. Southworth United States 34 2.8k 1.4× 588 1.1× 304 0.6× 576 1.4× 241 0.9× 59 3.4k
L. Takemoto United States 33 3.4k 1.6× 444 0.8× 825 1.7× 205 0.5× 460 1.7× 143 3.8k

Countries citing papers authored by T. Ramakrishna

Since Specialization
Citations

This map shows the geographic impact of T. Ramakrishna'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 T. Ramakrishna with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T. Ramakrishna more than expected).

Fields of papers citing papers by T. Ramakrishna

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of T. Ramakrishna

This figure shows the co-authorship network connecting the top 25 collaborators of T. Ramakrishna. A scholar is included among the top collaborators of T. Ramakrishna 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 T. Ramakrishna. T. Ramakrishna 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.
Ramakrishna, T., et al.. (2022). Protein Aggregation and Cataract: Role of Age-Related Modifications and Mutations in α-Crystallins. Biochemistry (Moscow). 87(3). 225–241. 20 indexed citations
2.
Saad, Mohammad A., Bakthisaran Raman, T. Ramakrishna, & Ch. Mohan Rao. (2021). Nucleosomal association and altered interactome underlie the mechanism of cataract caused by the R54C mutation of αA-crystallin. Biochimica et Biophysica Acta (BBA) - General Subjects. 1865(5). 129846–129846. 4 indexed citations
3.
Ramakrishna, T., et al.. (2017). Clusterin: full-length protein and one of its chains show opposing effects on cellular lipid accumulation. Scientific Reports. 7(1). 41235–41235. 29 indexed citations
4.
Raman, Bakthisaran, T. Ramakrishna, & Ch. Mohan Rao. (2014). Small heat shock proteins: Role in cellular functions and pathology. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(4). 291–319. 363 indexed citations
5.
Raman, Bakthisaran, et al.. (2012). HspB2/Myotonic Dystrophy Protein Kinase Binding Protein (MKBP) as a Novel Molecular Chaperone: Structural and Functional Aspects. PLoS ONE. 7(1). e29810–e29810. 26 indexed citations
6.
Thambisetty, Madhav, et al.. (2008). Utility of the Malayalam translation of the 7- minute screen for <i>Alzheimer's disease</i> risk in an Indian community. Neurology India. 56(2). 161–161. 7 indexed citations
7.
Ahmad, Shabbir, Bakthisaran Raman, T. Ramakrishna, & Ch. Mohan Rao. (2007). Effect of Phosphorylation on αB-crystallin: Differences in Stability, Subunit Exchange and Chaperone Activity of Homo and Mixed Oligomers of αB-Crystallin and its Phosphorylation-mimicking Mutant. Journal of Molecular Biology. 375(4). 1040–1051. 72 indexed citations
8.
Raman, Bakthisaran, et al.. (2007). Mixed Oligomer Formation between Human αA-Crystallin and its Cataract-causing G98R Mutant: Structural, Stability and Functional Differences. Journal of Molecular Biology. 373(5). 1293–1304. 15 indexed citations
9.
Singh, Bhairab N., K. Sridhar Rao, T. Ramakrishna, Nandini Rangaraj, & Ch. Mohan Rao. (2006). Association of αB-Crystallin, a Small Heat Shock Protein, with Actin: Role in Modulating Actin Filament Dynamics in Vivo. Journal of Molecular Biology. 366(3). 756–767. 95 indexed citations
10.
Raman, Bakthisaran, et al.. (2003). Structural perturbation and enhancement of the chaperone‐like activity of α‐crystallin by arginine hydrochloride. Protein Science. 12(6). 1262–1270. 51 indexed citations
11.
Pasta, Saloni, Bakthisaran Raman, T. Ramakrishna, & Ch. Mohan Rao. (2002). Role of the C-terminal Extensions of α-Crystallins. Journal of Biological Chemistry. 277(48). 45821–45828. 46 indexed citations
12.
Raman, Bakthisaran, et al.. (2001). Unfolding and refolding of a quinone oxidoreductase: α-crystallin, a molecular chaperone, assists its reactivation. Biochemical Journal. 359(3). 547–547. 31 indexed citations
13.
Ramakrishna, T., et al.. (1999). Structural and Functional Consequences of the Mutation of a Conserved Arginine Residue in αA and αB Crystallins. Journal of Biological Chemistry. 274(34). 24137–24141. 128 indexed citations
14.
Trivedi, Vishwa D., Bakthisaran Raman, T. Ramakrishna, & Ch. Mohan Rao. (1999). Detection and assay of proteases using calf lens β-crystallin aggregate as substrate. Journal of Biochemical and Biophysical Methods. 40(1-2). 49–55. 11 indexed citations
15.
Ramakrishna, T., et al.. (1998). Betaine reverses toxic effects of aluminium: Implications in Alzheimer's disease (AD) and AD-like pathology. Current Science. 75(11). 1153–1156. 5 indexed citations
16.
Trivedi, Vishwa D., Bakthisaran Raman, Ch. Mohan Rao, & T. Ramakrishna. (1997). Co‐refolding denatured‐reduced hen egg white lysozyme with acidic and basic proteins. FEBS Letters. 418(3). 363–366. 23 indexed citations
17.
Narayanan, K., Sushil Chandani, T. Ramakrishna, & Chintalagiri Mohan Rao. (1997). Depth profiling of mammalian cells by photoacoustic spectroscopy: localization of ligands. Biophysical Journal. 72(5). 2365–2368. 11 indexed citations
18.
Ramakrishna, T., et al.. (1996). Heart rate in female rat in response to snout contact by normal, gonadectomised and testosterone--pretreated gonadectomised male.. PubMed. 40(4). 335–9. 1 indexed citations
19.
Ramakrishna, T., et al.. (1996). Preservation of native conformation during aluminium-induced aggregation of tau protein. Neuroreport. 7(5). 1072–1076. 9 indexed citations
20.
Raman, Bakthisaran, T. Ramakrishna, & Ch. Mohan Rao. (1996). Refolding of Denatured and Denatured/Reduced Lysozyme at High Concentrations. Journal of Biological Chemistry. 271(29). 17067–17072. 87 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Bakthisaran Raman Breakdown of academic impact, for papers by J. Andrew Aquilina Breakdown of academic impact, for papers by Anat Ben‐Zvi Breakdown of academic impact, for papers by Usha P. Andley Breakdown of academic impact, for papers by Gudrun Lutsch Breakdown of academic impact, for papers by Jens Tyedmers Breakdown of academic impact, for papers by Bingdong Sha Breakdown of academic impact, for papers by Nikolai B. Gusev Breakdown of academic impact, for papers by Daniel R. Southworth Breakdown of academic impact, for papers by L. Takemoto
Rankless by CCL
2026