Manju Hingorani

3.5k total citations
69 papers, 2.8k citations indexed

About

Manju Hingorani is a scholar working on Molecular Biology, Pathology and Forensic Medicine and Genetics. According to data from OpenAlex, Manju Hingorani has authored 69 papers receiving a total of 2.8k indexed citations (citations by other indexed papers that have themselves been cited), including 66 papers in Molecular Biology, 22 papers in Pathology and Forensic Medicine and 19 papers in Genetics. Recurrent topics in Manju Hingorani's work include DNA Repair Mechanisms (44 papers), RNA and protein synthesis mechanisms (25 papers) and Genetic factors in colorectal cancer (22 papers). Manju Hingorani is often cited by papers focused on DNA Repair Mechanisms (44 papers), RNA and protein synthesis mechanisms (25 papers) and Genetic factors in colorectal cancer (22 papers). Manju Hingorani collaborates with scholars based in United States, Germany and Saudi Arabia. Manju Hingorani's co-authors include Mike O’Donnell, Smita S. Patel, Edwin Antony, X. Yu, Robert Wild, Edward H. Egelman, Miho Sakato, Jelena Stewart, Dorothy A. Erie and Yayan Zhou and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Manju Hingorani

68 papers receiving 2.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Manju Hingorani United States 32 2.5k 848 440 227 209 69 2.8k
Keith P. Bjornson United States 15 1.5k 0.6× 401 0.5× 390 0.9× 159 0.7× 87 0.4× 16 1.7k
Hans‐Joachim Fritz Germany 27 2.8k 1.1× 948 1.1× 157 0.4× 404 1.8× 252 1.2× 62 3.3k
Meindert H. Lamers Netherlands 22 1.8k 0.7× 378 0.4× 423 1.0× 79 0.3× 122 0.6× 46 2.2k
Joyce H.G. Lebbink Netherlands 28 1.6k 0.6× 248 0.3× 278 0.6× 114 0.5× 368 1.8× 52 2.0k
Roxana E. Georgescu United States 26 2.6k 1.0× 797 0.9× 68 0.2× 181 0.8× 335 1.6× 45 2.8k
David Jeruzalmi United States 18 2.0k 0.8× 872 1.0× 79 0.2× 298 1.3× 186 0.9× 36 2.4k
Linda B. Bloom United States 30 2.3k 0.9× 648 0.8× 65 0.1× 162 0.7× 94 0.4× 71 2.5k
Michael J. Osborne Canada 24 1.4k 0.6× 283 0.3× 86 0.2× 94 0.4× 240 1.1× 53 1.9k
Peggy Hsieh United States 28 3.0k 1.2× 482 0.6× 1.5k 3.5× 111 0.5× 102 0.5× 34 3.5k
Susan E. Tsutakawa United States 34 2.6k 1.0× 327 0.4× 70 0.2× 114 0.5× 410 2.0× 66 2.8k

Countries citing papers authored by Manju Hingorani

Since Specialization
Citations

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

Fields of papers citing papers by Manju Hingorani

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Manju Hingorani

This figure shows the co-authorship network connecting the top 25 collaborators of Manju Hingorani. A scholar is included among the top collaborators of Manju Hingorani 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 Manju Hingorani. Manju Hingorani 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.
Jayaraj, Abhilash, Kelly M. Thayer, David L. Beveridge, & Manju Hingorani. (2023). Molecular dynamics of mismatch detection—How MutS uses indirect readout to find errors in DNA. Biophysical Journal. 122(15). 3031–3043. 4 indexed citations
2.
Li, Yan, et al.. (2019). Msh4-Msh5 Induced DNA Conformational Changes Provide Insights into Its Role in Meiotic Recombination. Biophysical Journal. 116(3). 21a–21a. 1 indexed citations
3.
Li, Yan, et al.. (2018). MutSγ-Induced DNA Conformational Changes Provide Insights into Its Role in Meiotic Recombination. Biophysical Journal. 115(11). 2087–2101. 17 indexed citations
4.
Hamdan, Samir M., et al.. (2018). Positioning the 5′-flap junction in the active site controls the rate of flap endonuclease-1–catalyzed DNA cleavage. Journal of Biological Chemistry. 293(13). 4792–4804. 10 indexed citations
5.
Thayer, Kelly M., et al.. (2017). Evolutionary Covariance Combined with Molecular Dynamics Predicts a Framework for Allostery in the MutS DNA Mismatch Repair Protein. The Journal of Physical Chemistry B. 121(9). 2049–2061. 16 indexed citations
6.
Qiu, Ruoyi, Miho Sakato, Elizabeth J. Sacho, et al.. (2015). MutL traps MutS at a DNA mismatch. Proceedings of the National Academy of Sciences. 112(35). 10914–10919. 45 indexed citations
7.
Hingorani, Manju. (2015). Mismatch binding, ADP–ATP exchange and intramolecular signaling during mismatch repair. DNA repair. 38. 24–31. 33 indexed citations
8.
Liu, Cassie, et al.. (2013). E. Coli Heptosyltransferase I: Exploring Function and Dynamics to Create Better Inhibitors for GT-B Enzymes. Biophysical Journal. 104(2). 61a–61a. 1 indexed citations
9.
Heinen, Christopher D., Christopher Cook, Miho Sakato, et al.. (2011). Human MSH2 (hMSH2) Protein Controls ATP Processing by hMSH2-hMSH6. Journal of Biological Chemistry. 286(46). 40287–40295. 27 indexed citations
10.
Sakato, Miho, Yayan Zhou, & Manju Hingorani. (2011). ATP Binding and Hydrolysis-Driven Rate-Determining Events in the RFC-Catalyzed PCNA Clamp Loading Reaction. Journal of Molecular Biology. 416(2). 176–191. 27 indexed citations
11.
Zhai, Jie, et al.. (2010). Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein. Journal of Visualized Experiments. 6 indexed citations
12.
Chen, Siying, Mikhail K. Levin, Miho Sakato, Yayan Zhou, & Manju Hingorani. (2009). Mechanism of ATP-Driven PCNA Clamp Loading by S. cerevisiae RFC. Journal of Molecular Biology. 388(3). 431–442. 38 indexed citations
13.
Teßmer, Ingrid, Yong Yang, Jie Zhai, et al.. (2008). Mechanism of MutS Searching for DNA Mismatches and Signaling Repair. Journal of Biological Chemistry. 283(52). 36646–36654. 57 indexed citations
14.
Chen, Siying, Maria Magdalena Coman, Miho Sakato, Mike O’Donnell, & Manju Hingorani. (2008). Conserved residues in the δ subunit help the E. coli clamp loader, γ complex, target primer-template DNA for clamp assembly. Nucleic Acids Research. 36(10). 3274–3286. 8 indexed citations
15.
Finkelstein, Jeff, Edwin Antony, Manju Hingorani, & Mike O’Donnell. (2003). Overproduction and analysis of eukaryotic multiprotein complexes in Escherichia coli using a dual-vector strategy. Analytical Biochemistry. 319(1). 78–87. 67 indexed citations
16.
Jeruzalmi, David, Olga Yurieva, Yanxiang Zhao, et al.. (2001). Mechanism of Processivity Clamp Opening by the Delta Subunit Wrench of the Clamp Loader Complex of E. coli DNA Polymerase III. Cell. 106(4). 417–428. 206 indexed citations
17.
Ason, Brandon, Jeffrey G. Bertram, Manju Hingorani, et al.. (2000). A Model for Escherichia coli DNA Polymerase III Holoenzyme Assembly at Primer/Template Ends. Journal of Biological Chemistry. 275(4). 3006–3015. 51 indexed citations
18.
Hingorani, Manju & Mike O’Donnell. (2000). Sliding clamps: A (tail)ored fit. Current Biology. 10(1). R25–R29. 97 indexed citations
19.
Hingorani, Manju & Mike O’Donnell. (1998). Toroidal proteins: Running rings around DNA. Current Biology. 8(3). R83–R86. 48 indexed citations
20.
Hingorani, Manju & Smita S. Patel. (1993). Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs. Biochemistry. 32(46). 12478–12487. 91 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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