Vanitha Thulasiraman

1.7k total citations
19 papers, 1.3k citations indexed

About

Vanitha Thulasiraman is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Vanitha Thulasiraman has authored 19 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 5 papers in Spectroscopy and 5 papers in Materials Chemistry. Recurrent topics in Vanitha Thulasiraman's work include Heat shock proteins research (10 papers), Advanced Proteomics Techniques and Applications (5 papers) and Enzyme Structure and Function (5 papers). Vanitha Thulasiraman is often cited by papers focused on Heat shock proteins research (10 papers), Advanced Proteomics Techniques and Applications (5 papers) and Enzyme Structure and Function (5 papers). Vanitha Thulasiraman collaborates with scholars based in United States, China and Italy. Vanitha Thulasiraman's co-authors include Robert L. Matts, Raúl G. Ferreyra, Judith Frydman, Douglas E. Feldman, Lee Lomas, Shanhua Lin, Egisto Boschetti, Eric T. Fung, Scot R. Weinberger and David J. Hammond and has published in prestigious journals such as The EMBO Journal, Molecular Cell and Molecular and Cellular Biology.

In The Last Decade

Vanitha Thulasiraman

19 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Vanitha Thulasiraman United States 13 1.1k 367 190 157 134 19 1.3k
Erik J. Spek United States 12 1.2k 1.1× 529 1.4× 136 0.7× 191 1.2× 71 0.5× 13 1.5k
Elisabeth Bragado‐Nilsson Spain 11 1.7k 1.6× 161 0.4× 351 1.8× 131 0.8× 91 0.7× 16 2.0k
Sandra L. Harper United States 20 823 0.7× 127 0.3× 194 1.0× 68 0.4× 97 0.7× 43 1.3k
Henrik Rahbek-Nielsen Denmark 13 537 0.5× 290 0.8× 82 0.4× 46 0.3× 99 0.7× 14 1.0k
Séverine Boulon France 17 2.0k 1.8× 137 0.4× 267 1.4× 90 0.6× 111 0.8× 21 2.3k
David H. Perlman United States 15 964 0.9× 473 1.3× 75 0.4× 41 0.3× 101 0.8× 20 1.4k
Werner Streicher Denmark 21 1.7k 1.6× 100 0.3× 321 1.7× 156 1.0× 106 0.8× 42 2.0k
Naveid Ali Australia 10 665 0.6× 295 0.8× 127 0.7× 27 0.2× 121 0.9× 13 1.0k
Dirk Brehmer Belgium 16 1.1k 1.0× 107 0.3× 174 0.9× 153 1.0× 179 1.3× 23 1.3k
Greg Cantin United States 19 1.2k 1.1× 309 0.8× 165 0.9× 28 0.2× 207 1.5× 24 1.6k

Countries citing papers authored by Vanitha Thulasiraman

Since Specialization
Citations

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

Fields of papers citing papers by Vanitha Thulasiraman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Vanitha Thulasiraman

This figure shows the co-authorship network connecting the top 25 collaborators of Vanitha Thulasiraman. A scholar is included among the top collaborators of Vanitha Thulasiraman 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 Vanitha Thulasiraman. Vanitha Thulasiraman is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

19 of 19 papers shown
1.
Lomas, Lee, Charlotte H. Clarke, Vanitha Thulasiraman, & Eric T. Fung. (2011). Optimized Conditions for a Quantitative SELDI TOF MS Protein Assay. Methods in molecular biology. 818. 1–10. 3 indexed citations
2.
Thulasiraman, Vanitha, et al.. (2010). Evaluation of Oriole Fluorescent Gel Stain and Comparison to SYPRO Ruby. Journal of Biomolecular Techniques JBT. 21(5). 343–344. 4 indexed citations
3.
Guerrier, Luc, Vanitha Thulasiraman, Annalisa Castagna, et al.. (2006). Reducing protein concentration range of biological samples using solid-phase ligand libraries☆. Journal of Chromatography B. 833(1). 33–40. 84 indexed citations
4.
Thulasiraman, Vanitha, Shanhua Lin, Liliana Gheorghiu, et al.. (2005). Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands. Electrophoresis. 26(18). 3561–3571. 184 indexed citations
5.
Thulasiraman, Vanitha, et al.. (2004). Simultaneous Monitoring of Multiple Kinase Activities by SELDI-TOF Mass Spectrometry. Humana Press eBooks. 264. 205–214. 8 indexed citations
6.
Cho, William C., Timothy T. C. Yip, Christine Yip, et al.. (2004). Identification of Serum Amyloid A Protein As a Potentially Useful Biomarker to Monitor Relapse of Nasopharyngeal Cancer by Serum Proteomic Profiling. Clinical Cancer Research. 10(1). 43–52. 167 indexed citations
7.
Thulasiraman, Vanitha, Raúl G. Ferreyra, & Judith Frydman. (2003). Monitoring Actin Folding: Purification Protocols for Labeled Proteins and Binding to DNase I-Sepharose Beads. Humana Press eBooks. 140. 161–167. 6 indexed citations
8.
Thulasiraman, Vanitha, Raúl G. Ferreyra, & Judith Frydman. (2003). Folding Assays: Assessing the Native Conformation of Proteins. Humana Press eBooks. 140. 169–177. 11 indexed citations
9.
Thulasiraman, Vanitha & Robert L. Matts. (2003). Luciferase Renaturation Assays of Chaperones and Chaperone Antagonists. Humana Press eBooks. 102. 129–141. 8 indexed citations
10.
Thulasiraman, Vanitha, Bo-Geon Yun, Sheri Uma, et al.. (2002). Differential Inhibition of Hsc70 Activities by Two Hsc70-Binding Peptides. Biochemistry. 41(11). 3742–3753. 13 indexed citations
11.
Fung, Eric T., et al.. (2001). Protein biochips for differential profiling. Current Opinion in Biotechnology. 12(1). 65–69. 137 indexed citations
12.
Thulasiraman, Vanitha, Sandra L. McCutchen‐Maloney, Vladimir L. Motin, & Emilio García García. (2001). Detection and Identification of Virulence Factors in Yersinia pestis Using SELDI ProteinChip ® System. BioTechniques. 30(2). 428–432. 37 indexed citations
13.
Thulasiraman, Vanitha. (1999). In vivo newly translated polypeptides are sequestered in a protected folding environment. The EMBO Journal. 18(1). 85–95. 265 indexed citations
14.
Feldman, Douglas E., Vanitha Thulasiraman, Raúl G. Ferreyra, & Judith Frydman. (1999). Formation of the VHL–Elongin BC Tumor Suppressor Complex Is Mediated by the Chaperonin TRiC. Molecular Cell. 4(6). 1051–1061. 196 indexed citations
15.
Uma, Sheri, Vanitha Thulasiraman, & Robert L. Matts. (1999). Dual Role for Hsc70 in the Biogenesis and Regulation of the Heme-Regulated Kinase of the α Subunit of Eukaryotic Translation Initiation Factor 2. Molecular and Cellular Biology. 19(9). 5861–5871. 39 indexed citations
16.
Hartson, Steven D., Vanitha Thulasiraman, Wenjun Huang, Luke Whitesell, & Robert L. Matts. (1999). Molybdate Inhibits Hsp90, Induces Structural Changes in Its C-Terminal Domain, and Alters Its Interactions with Substrates. Biochemistry. 38(12). 3837–3849. 59 indexed citations
17.
Thulasiraman, Vanitha, et al.. (1998). Evidence that Hsc70 negatively modulates the activation of the heme‐regulated eIF‐2α kinase in rabbit reticulocyte lysate. European Journal of Biochemistry. 255(3). 552–562. 30 indexed citations
18.
19.
Thulasiraman, Vanitha & Robert L. Matts. (1996). Effect of Geldanamycin on the Kinetics of Chaperone-Mediated Renaturation of Firefly Luciferase in Rabbit Reticulocyte Lysate. Biochemistry. 35(41). 13443–13450. 61 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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