N R Thotakura

1.3k total citations
30 papers, 1.0k citations indexed

About

N R Thotakura is a scholar working on Molecular Biology, Endocrinology, Diabetes and Metabolism and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, N R Thotakura has authored 30 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 16 papers in Endocrinology, Diabetes and Metabolism and 6 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in N R Thotakura's work include Glycosylation and Glycoproteins Research (14 papers), Growth Hormone and Insulin-like Growth Factors (11 papers) and Thyroid Disorders and Treatments (10 papers). N R Thotakura is often cited by papers focused on Glycosylation and Glycoproteins Research (14 papers), Growth Hormone and Insulin-like Growth Factors (11 papers) and Thyroid Disorders and Treatments (10 papers). N R Thotakura collaborates with scholars based in United States, France and Australia. N R Thotakura's co-authors include O.P. Bahl, Mariusz W. Szkudlinski, Bruce D. Weintraub, B D Weintraub, Diana Blithe, Leon A. Bach, Matthew M. Rechler, Joseph E. Tropea, Mathis Grossmann and Edward S. Cole and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Immunology.

In The Last Decade

N R Thotakura

30 papers receiving 991 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
N R Thotakura United States 21 507 472 257 168 145 30 1.0k
Cathérine Ronin France 20 573 1.1× 495 1.0× 186 0.7× 138 0.8× 127 0.9× 41 1.2k
Nachum Reiss Israel 18 883 1.7× 195 0.4× 303 1.2× 159 0.9× 383 2.6× 31 1.5k
Prema Narayan United States 24 1.3k 2.6× 252 0.5× 361 1.4× 47 0.3× 288 2.0× 48 1.8k
T. Kawashima Japan 7 369 0.7× 170 0.4× 98 0.4× 45 0.3× 515 3.6× 21 927
Venkataraman Sriraman United States 17 432 0.9× 162 0.3× 445 1.7× 49 0.3× 304 2.1× 32 1.1k
Hyun S. Nahm United States 9 387 0.8× 161 0.3× 123 0.5× 37 0.2× 169 1.2× 15 760
M.E. Meyer France 11 399 0.8× 219 0.5× 147 0.6× 88 0.5× 692 4.8× 29 980
Beth Lynn Maxwell United States 11 407 0.8× 200 0.4× 197 0.8× 49 0.3× 618 4.3× 14 1.0k
Valérie Frémont France 12 458 0.9× 243 0.5× 94 0.4× 94 0.6× 199 1.4× 16 739
Candace A. Beck United States 19 499 1.0× 283 0.6× 248 1.0× 49 0.3× 939 6.5× 23 1.3k

Countries citing papers authored by N R Thotakura

Since Specialization
Citations

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

Fields of papers citing papers by N R Thotakura

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of N R Thotakura

This figure shows the co-authorship network connecting the top 25 collaborators of N R Thotakura. A scholar is included among the top collaborators of N R Thotakura 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 N R Thotakura. N R Thotakura 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.
Zhang, Junli, Pedro J. Alfonso, N R Thotakura, et al.. (1998). Expression, Purification, and Bioassay of Human Stanniocalcin from Baculovirus-Infected Insect Cells and Recombinant CHO Cells. Protein Expression and Purification. 12(3). 390–398. 34 indexed citations
2.
Thotakura, N R, et al.. (1998). Developmental Changes in the Glycosylation of Glycoprotein Hormone Free α Subunit during Pregnancy. Journal of Biological Chemistry. 273(20). 12068–12076. 25 indexed citations
3.
Seetharamaiah, Gattadahalli S., John S. Dallas, Sai A. Patibandla, N R Thotakura, & Bellur S. Prabhakar. (1997). Requirement of glycosylation of the human thyrotropin receptor ectodomain for its reactivity with autoantibodies in patients' sera. The Journal of Immunology. 158(6). 2798–2804. 40 indexed citations
4.
Patibandla, Sai A., et al.. (1997). Differential Reactivities of Recombinant Glycosylated Ectodomains of Mouse and Human Thyrotropin Receptors with Patient Autoantibodies1. Endocrinology. 138(4). 1559–1566. 20 indexed citations
5.
Coleman, Timothy A., David C. Parmelee, N R Thotakura, et al.. (1997). Production and purification of novel secreted human proteins. Gene. 190(1). 163–171. 14 indexed citations
6.
Grossmann, Mathis, Mariusz W. Szkudlinski, Joseph E. Tropea, et al.. (1995). Expression of Human Thyrotropin in Cell Lines with Different Glycosylation Patterns Combined with Mutagenesis of Specific Glycosylation Sites. Journal of Biological Chemistry. 270(49). 29378–29385. 46 indexed citations
7.
Szkudlinski, Mariusz W., et al.. (1995). A Novel, Nonradioactive in Vivo Bioassay of Thyrotropin (TSH). Thyroid. 5(1). 55–59. 41 indexed citations
8.
Szkudlinski, Mariusz W., N R Thotakura, Joseph E. Tropea, Mathis Grossmann, & B D Weintraub. (1995). Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropin.. Endocrinology. 136(8). 3325–3330. 68 indexed citations
9.
Thotakura, N R & Diana Blithe. (1995). Glycoprotein hormones: glycobiology of gonadotrophins, thyrotrophin and free α subunit. Glycobiology. 5(1). 3–10. 75 indexed citations
10.
Leitolf, Holger, Mariusz W. Szkudlinski, C Hoang-Vu, et al.. (1995). Effects of Continuous and Pulsatile Administration of Pituitary Rat Thyrotropin and Recombinant Human Thyrotropin in a Chronically Cannulated Rat. Hormone and Metabolic Research. 27(4). 173–178. 12 indexed citations
11.
Thotakura, N R, Mariusz W. Szkudlinski, & Bruce D. Weintraub. (1994). Structure—function studies of oligosaccharides of recombinant human thyrotrophin by sequential deglycosylation and resialylation. Glycobiology. 4(4). 525–533. 22 indexed citations
12.
Bach, Leon A., N R Thotakura, & Matthew M. Rechler. (1992). Human insulin-like growth factor binding protein-6 is O-glycosylated. Biochemical and Biophysical Research Communications. 186(1). 301–307. 67 indexed citations
13.
Thotakura, N R, et al.. (1991). Biological Activity and Metabolic Clearance of a Recombinant Human Thyrotropin Produced in Chinese Hamster Ovary Cells. Endocrinology. 128(1). 341–348. 105 indexed citations
14.
Sethumadhavan, Kandan, Francis L. Bellino, & N R Thotakura. (1991). Estrogen synthetase (aromatase). The cytochrome P-450 component of the human placental enzyme is a glycoprotein. Molecular and Cellular Endocrinology. 78(1-2). 25–32. 30 indexed citations
15.
Thotakura, N R, Bruce D. Weintraub, & O.P. Bahl. (1990). The role of carbohydrate in human choriogonadotropin (hCG) action. Effects of N-linked carbohydrate chains from hCG and other glycoproteins on hormonal activity. Molecular and Cellular Endocrinology. 70(3). 263–272. 33 indexed citations
16.
Gesundheit, Neil, et al.. (1990). Changes in the sialylation and sulfation of secreted thyrotropin in congenital hypothyroidism.. Proceedings of the National Academy of Sciences. 87(10). 3792–3796. 25 indexed citations
17.
Stannard, Bethel, et al.. (1989). Differential effect of inhibitors of oligosaccharide processing on the secretion of thyrotropin from dispersed rodent pituitary cells. Biochemical and Biophysical Research Communications. 165(2). 788–794. 5 indexed citations
18.
Thotakura, N R & O.P. Bahl. (1987). [28] Enzymatic deglycosylation of glycoproteins. Methods in enzymology on CD-ROM/Methods in enzymology. 138. 350–359. 44 indexed citations
19.
Bruch, Richard C., N R Thotakura, & O.P. Bahl. (1986). The rat ovarian lutropin receptor. Purification, hormone binding properties, and subunit composition.. Journal of Biological Chemistry. 261(20). 9450–9460. 26 indexed citations
20.
Thotakura, N R & O.P. Bahl. (1985). Highly Specific and Sensitive Hybridoma Antibodies against the α-Subunit of Human Glycoprotein Hormones*. Endocrinology. 117(4). 1300–1308. 26 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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