Stewart N. Loh

3.8k total citations
80 papers, 3.0k citations indexed

About

Stewart N. Loh is a scholar working on Molecular Biology, Oncology and Materials Chemistry. According to data from OpenAlex, Stewart N. Loh has authored 80 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 71 papers in Molecular Biology, 16 papers in Oncology and 15 papers in Materials Chemistry. Recurrent topics in Stewart N. Loh's work include Protein Structure and Dynamics (24 papers), RNA and protein synthesis mechanisms (19 papers) and Enzyme Structure and Function (13 papers). Stewart N. Loh is often cited by papers focused on Protein Structure and Dynamics (24 papers), RNA and protein synthesis mechanisms (19 papers) and Enzyme Structure and Function (13 papers). Stewart N. Loh collaborates with scholars based in United States, China and Netherlands. Stewart N. Loh's co-authors include James S. Butler, Jeung‐Hoi Ha, Shu‐ou Shan, Daniel Herschlag, John L. Markley, Andrew P. Hinck, Adam R. Blanden, Darren R. Carpizo, Robert L. Baldwin and Margaret M. Stratton and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Stewart N. Loh

79 papers receiving 2.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Stewart N. Loh United States 32 2.2k 646 606 311 284 80 3.0k
James G. Omichinski United States 38 3.7k 1.7× 806 1.2× 506 0.8× 217 0.7× 490 1.7× 106 4.8k
John Spurlino United States 24 1.6k 0.7× 538 0.8× 707 1.2× 177 0.6× 168 0.6× 42 2.8k
Shigetoshi Sugio Japan 23 2.1k 1.0× 467 0.7× 584 1.0× 281 0.9× 239 0.8× 57 2.8k
Dale E. Tronrud United States 22 2.3k 1.0× 282 0.4× 1.1k 1.8× 215 0.7× 197 0.7× 34 2.9k
Nobutoshi Ito Japan 31 2.9k 1.3× 518 0.8× 487 0.8× 302 1.0× 146 0.5× 120 4.4k
William M. Atkins United States 32 2.4k 1.1× 772 1.2× 277 0.5× 186 0.6× 450 1.6× 107 3.9k
John S. Sack United States 27 2.2k 1.0× 370 0.6× 592 1.0× 387 1.2× 277 1.0× 53 3.5k
David G. Nettesheim United States 26 4.0k 1.8× 898 1.4× 324 0.5× 242 0.8× 203 0.7× 37 4.9k
Petr Pančoška United States 27 2.4k 1.1× 931 1.4× 377 0.6× 154 0.5× 666 2.3× 76 3.4k
Jun Yin United States 33 2.8k 1.2× 407 0.6× 250 0.4× 419 1.3× 209 0.7× 91 3.8k

Countries citing papers authored by Stewart N. Loh

Since Specialization
Citations

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

Fields of papers citing papers by Stewart N. Loh

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Stewart N. Loh

This figure shows the co-authorship network connecting the top 25 collaborators of Stewart N. Loh. A scholar is included among the top collaborators of Stewart N. Loh 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 Stewart N. Loh. Stewart N. Loh 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.
Ha, Jeung‐Hoi, et al.. (2023). Adaptable, turn-on maturation (ATOM) fluorescent biosensors for multiplexed detection in cells. Nature Methods. 20(12). 1920–1929. 7 indexed citations
2.
Ha, Jeung‐Hoi, et al.. (2022). Engineering a Fluorescent Protein Color Switch Using Entropy-Driven β-Strand Exchange. ACS Sensors. 7(1). 263–271. 14 indexed citations
3.
Ha, Jeung‐Hoi, et al.. (2022). Engineering protein and DNA tools for creating DNA-dependent protein switches. Methods in enzymology on CD-ROM/Methods in enzymology. 675. 1–32. 1 indexed citations
4.
Loh, Stewart N., et al.. (2022). Engineering protein activity into off-the-shelf DNA devices. Cell Reports Methods. 2(4). 100202–100202. 4 indexed citations
5.
Bogetti, Anthony T., et al.. (2021). The Next Frontier for Designing Switchable Proteins: Rational Enhancement of Kinetics. The Journal of Physical Chemistry B. 125(32). 9069–9077. 3 indexed citations
6.
Zaman, Saif, Xin Yu, Adam R. Blanden, et al.. (2019). Combinatorial Therapy of Zinc Metallochaperones with Mutant p53 Reactivation and Diminished Copper Binding. Molecular Cancer Therapeutics. 18(8). 1355–1365. 25 indexed citations
7.
Yu, Xin, Samuel Kogan, Ying Chen, et al.. (2018). Zinc Metallochaperones Reactivate Mutant p53 Using an ON/OFF Switch Mechanism: A New Paradigm in Cancer Therapeutics. Clinical Cancer Research. 24(18). 4505–4517. 33 indexed citations
8.
Woodford, Mark R., Rebecca Sager, Diana M. Dunn, et al.. (2017). Tumor suppressor Tsc1 is a new Hsp90 co‐chaperone that facilitates folding of kinase and non‐kinase clients. The EMBO Journal. 36(24). 3650–3665. 68 indexed citations
9.
Wolfe, Aaron J., Wei Si, Zhengqi Zhang, et al.. (2017). Quantification of Membrane Protein-Detergent Complex Interactions. The Journal of Physical Chemistry B. 121(44). 10228–10241. 22 indexed citations
10.
Blanden, Adam R., Xin Yu, Stewart N. Loh, Arnold J. Levine, & Darren R. Carpizo. (2015). Reactivating mutant p53 using small molecules as zinc metallochaperones: awakening a sleeping giant in cancer. Drug Discovery Today. 20(11). 1391–1397. 68 indexed citations
11.
Walker‐Kopp, Nancy, et al.. (2015). Engineered Domain Swapping as an On/Off Switch for Protein Function. Chemistry & Biology. 22(10). 1384–1393. 25 indexed citations
12.
Ha, Jeung‐Hoi, Stephen A. Shinsky, & Stewart N. Loh. (2013). Stepwise Conversion of a Binding Protein to a Fluorescent Switch: Application to Thermoanaerobacter tengcongensis Ribose Binding Protein. Biochemistry. 52(4). 600–612. 16 indexed citations
13.
Stratton, Margaret M., et al.. (2010). Probing local structural fluctuations in myoglobin by size‐dependent thiol‐disulfide exchange. Protein Science. 19(8). 1587–1594. 5 indexed citations
14.
Loh, Stewart N.. (2010). The missing Zinc: p53 misfolding and cancer. Metallomics. 2(7). 442–442. 103 indexed citations
15.
Butler, James S., et al.. (2009). Folding of Tetrameric p53: Oligomerization and Tumorigenic Mutations Induce Misfolding and Loss of Function. Journal of Molecular Biology. 395(4). 705–716. 36 indexed citations
16.
Butler, James S. & Stewart N. Loh. (2006). Folding and misfolding mechanisms of the p53 DNA binding domain at physiological temperature. Protein Science. 15(11). 2457–2465. 30 indexed citations
17.
Markley, John L., Andrew P. Hinck, Stewart N. Loh, et al.. (1994). Case study of protein structure, stability, and function: NMR investigations of the proline residues in staphylococcal nuclease. Pure and Applied Chemistry. 66(1). 65–69. 4 indexed citations
18.
19.
Loh, Stewart N., Lyle A. Dethlefsen, Gerald L. Newton, Joseph Aguilera, & Robert C. Fahey. (1990). Nuclear Thiols: Technical Limitations on the Determination of Endogenous Nuclear Glutathione and the Potential Importance of Sulfhydryl Proteins. Radiation Research. 121(1). 98–98. 32 indexed citations
20.

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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