Jayant B. Udgaonkar

6.2k total citations
171 papers, 5.2k citations indexed

About

Jayant B. Udgaonkar is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, Jayant B. Udgaonkar has authored 171 papers receiving a total of 5.2k indexed citations (citations by other indexed papers that have themselves been cited), including 159 papers in Molecular Biology, 92 papers in Materials Chemistry and 29 papers in Physiology. Recurrent topics in Jayant B. Udgaonkar's work include Protein Structure and Dynamics (110 papers), Enzyme Structure and Function (89 papers) and Prion Diseases and Protein Misfolding (42 papers). Jayant B. Udgaonkar is often cited by papers focused on Protein Structure and Dynamics (110 papers), Enzyme Structure and Function (89 papers) and Prion Diseases and Protein Misfolding (42 papers). Jayant B. Udgaonkar collaborates with scholars based in India, United States and Germany. Jayant B. Udgaonkar's co-authors include Vishwas R. Agashe, Jogender Singh, G. Krishnamoorthy, Shweta Jain, M.C.R. Shastry, Santosh Kumar Jha, Abani K. Bhuyan, Robert L. Baldwin, P.K. Malhotra and Utpal Nath and has published in prestigious journals such as Nature, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Jayant B. Udgaonkar

171 papers receiving 5.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jayant B. Udgaonkar India 41 4.4k 2.3k 792 637 532 171 5.2k
Mikael Oliveberg Sweden 48 4.5k 1.0× 2.0k 0.9× 672 0.8× 640 1.0× 500 0.9× 100 6.0k
Irina М. Kuznetsova Russia 40 3.8k 0.9× 1.1k 0.5× 1.3k 1.7× 638 1.0× 568 1.1× 200 5.8k
Konstantin К. Turoverov Russia 42 4.1k 0.9× 1.2k 0.5× 1.3k 1.7× 677 1.1× 586 1.1× 208 6.2k
Jonathan P. Waltho United Kingdom 45 4.6k 1.0× 1.3k 0.6× 626 0.8× 448 0.7× 720 1.4× 143 6.0k
Alfonso De Simone United Kingdom 39 3.5k 0.8× 1.0k 0.5× 1.8k 2.3× 572 0.9× 934 1.8× 131 6.1k
Anders Ø. Madsen Denmark 23 3.2k 0.7× 1.3k 0.6× 2.1k 2.7× 190 0.3× 559 1.1× 66 5.2k
Kazuyuki Akasaka Japan 38 3.0k 0.7× 1.6k 0.7× 296 0.4× 468 0.7× 1.1k 2.0× 146 4.1k
C. Robert Matthews United States 46 5.1k 1.2× 3.0k 1.3× 282 0.4× 613 1.0× 547 1.0× 148 6.1k
Andrew D. Miranker United States 41 5.1k 1.1× 1.2k 0.5× 2.8k 3.5× 760 1.2× 815 1.5× 73 6.6k
John Christodoulou United Kingdom 39 3.7k 0.8× 922 0.4× 1.0k 1.3× 592 0.9× 505 0.9× 111 5.5k

Countries citing papers authored by Jayant B. Udgaonkar

Since Specialization
Citations

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

Fields of papers citing papers by Jayant B. Udgaonkar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jayant B. Udgaonkar. 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 Jayant B. Udgaonkar. The network helps show where Jayant B. Udgaonkar may publish in the future.

Co-authorship network of co-authors of Jayant B. Udgaonkar

This figure shows the co-authorship network connecting the top 25 collaborators of Jayant B. Udgaonkar. A scholar is included among the top collaborators of Jayant B. Udgaonkar 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 Jayant B. Udgaonkar. Jayant B. Udgaonkar 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.
Bhatia, Sandhya & Jayant B. Udgaonkar. (2023). Understanding the heterogeneity intrinsic to protein folding. Current Opinion in Structural Biology. 84. 102738–102738. 5 indexed citations
2.
Udgaonkar, Jayant B., et al.. (2022). Elongation of Fibrils Formed by a Tau Fragment is Inhibited by a Transient Dimeric Intermediate. The Journal of Physical Chemistry B. 126(18). 3385–3397. 1 indexed citations
3.
Udgaonkar, Jayant B., et al.. (2022). Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein. Protein Science. 31(12). e4513–e4513. 3 indexed citations
4.
Udgaonkar, Jayant B., et al.. (2021). Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization. Protein Science. 30(11). 2258–2271. 7 indexed citations
5.
6.
Bhatia, Sandhya, Guruswamy Krishnamoorthy, & Jayant B. Udgaonkar. (2021). Mapping Distinct Sequences of Structure Formation Differentiating Multiple Folding Pathways of a Small Protein. Journal of the American Chemical Society. 143(3). 1447–1457. 9 indexed citations
7.
Bhatia, Sandhya, Guruswamy Krishnamoorthy, & Jayant B. Udgaonkar. (2021). Resolving Site-Specific Heterogeneity of the Unfolded State under Folding Conditions. The Journal of Physical Chemistry Letters. 12(13). 3295–3302. 2 indexed citations
8.
Udgaonkar, Jayant B., et al.. (2019). Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein. eLife. 8. 19 indexed citations
9.
Sengupta, Ishita & Jayant B. Udgaonkar. (2019). Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein. eLife. 8. 15 indexed citations
10.
Udgaonkar, Jayant B., et al.. (2018). The Osmolyte TMAO Modulates Protein Folding Cooperativity by Altering Global Protein Stability. Biochemistry. 57(40). 5851–5863. 25 indexed citations
11.
Udgaonkar, Jayant B., et al.. (2017). Stepwise Assembly of β-Sheet Structure during the Folding of an SH3 Domain Revealed by a Pulsed Hydrogen Exchange Mass Spectrometry Study. Biochemistry. 56(29). 3754–3769. 10 indexed citations
12.
Malhotra, P.K., et al.. (2017). Chemical Denaturants Smoothen Ruggedness on the Free Energy Landscape of Protein Folding. Biochemistry. 56(31). 4053–4063. 8 indexed citations
13.
Udgaonkar, Jayant B., et al.. (2017). Modulation of the Extent of Cooperative Structural Change During Protein Folding by Chemical Denaturant. The Journal of Physical Chemistry B. 121(35). 8263–8275. 10 indexed citations
14.
Udgaonkar, Jayant B., et al.. (2017). A Dry Transition State More Compact Than the Native State Is Stabilized by Non-Native Interactions during the Unfolding of a Small Protein. Biochemistry. 56(29). 3699–3703. 5 indexed citations
15.
16.
Udgaonkar, Jayant B., et al.. (2011). Understanding the Kinetic Roles of the Inducer Heparin and of Rod-like Protofibrils during Amyloid Fibril Formation by Tau Protein. Journal of Biological Chemistry. 286(45). 38948–38959. 112 indexed citations
17.
Jha, Santosh Kumar & Jayant B. Udgaonkar. (2009). Direct evidence for a dry molten globule intermediate during the unfolding of a small protein. Proceedings of the National Academy of Sciences. 106(30). 12289–12294. 114 indexed citations
18.
Jain, Shweta & Jayant B. Udgaonkar. (2008). Evidence for Stepwise Formation of Amyloid Fibrils by the Mouse Prion Protein. Journal of Molecular Biology. 382(5). 1228–1241. 78 indexed citations
19.
Udgaonkar, Jayant B., et al.. (2001). Reversible formation of on‐pathway macroscopic aggregates during the folding of maltose binding protein. Protein Science. 10(8). 1635–1644. 26 indexed citations
20.
Bhuyan, Abani K. & Jayant B. Udgaonkar. (1999). Real-time NMR measurements of protein folding and hydrogen exchange dynamics. Current Science. 77(7). 942–950. 3 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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