Hays S. Rye

4.7k total citations · 1 hit paper
42 papers, 3.8k citations indexed

About

Hays S. Rye is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Hays S. Rye has authored 42 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 13 papers in Materials Chemistry and 6 papers in Cell Biology. Recurrent topics in Hays S. Rye's work include Protein Structure and Dynamics (18 papers), Heat shock proteins research (18 papers) and Enzyme Structure and Function (13 papers). Hays S. Rye is often cited by papers focused on Protein Structure and Dynamics (18 papers), Heat shock proteins research (18 papers) and Enzyme Structure and Function (13 papers). Hays S. Rye collaborates with scholars based in United States, Germany and Netherlands. Hays S. Rye's co-authors include Alexander N. Glazer, Wayne A. Fenton, Arthur L. Horwich, Zong Lin, Richard A. Mathies, Mark A. Quesada, Steven G. Burston, Zhaohui Xu, Paul B. Sigler and Joseph Beechem and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Hays S. Rye

41 papers receiving 3.7k citations

Hit Papers

Stable fluorescent complexes of double-stranded DNA with ... 1992 2026 2003 2014 1992 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Hays S. Rye United States 25 3.2k 1.4k 458 302 248 42 3.8k
Véronique Receveur‐Brechot France 27 2.5k 0.8× 976 0.7× 361 0.8× 158 0.5× 291 1.2× 52 3.5k
José Luís Corchero Spain 36 2.8k 0.9× 660 0.5× 511 1.1× 245 0.8× 219 0.9× 102 4.1k
Grzegorz Piszczek United States 33 2.1k 0.7× 509 0.4× 182 0.4× 160 0.5× 566 2.3× 92 3.3k
Uno Carlsson Sweden 32 1.8k 0.6× 520 0.4× 129 0.3× 196 0.6× 324 1.3× 97 2.7k
Gail J. Bartlett United Kingdom 31 3.0k 0.9× 881 0.6× 157 0.3× 76 0.3× 179 0.7× 44 3.7k
Hisakazu Mihara Japan 36 3.4k 1.1× 681 0.5× 468 1.0× 131 0.4× 164 0.7× 230 4.7k
Eckhard Hofmann Germany 32 2.2k 0.7× 494 0.4× 201 0.4× 131 0.4× 172 0.7× 93 3.6k
Amy E. Keating United States 36 3.7k 1.2× 516 0.4× 116 0.3× 281 0.9× 455 1.8× 94 4.7k
Patrick Tauc France 26 1.3k 0.4× 755 0.5× 290 0.6× 76 0.3× 162 0.7× 66 2.3k
Anatoly I. Dragan United States 29 1.9k 0.6× 530 0.4× 534 1.2× 119 0.4× 48 0.2× 65 2.6k

Countries citing papers authored by Hays S. Rye

Since Specialization
Citations

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

Fields of papers citing papers by Hays S. Rye

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Hays S. Rye. 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 Hays S. Rye. The network helps show where Hays S. Rye may publish in the future.

Co-authorship network of co-authors of Hays S. Rye

This figure shows the co-authorship network connecting the top 25 collaborators of Hays S. Rye. A scholar is included among the top collaborators of Hays S. Rye 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 Hays S. Rye. Hays S. Rye 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.
Walker, T.G., et al.. (2023). Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time. ACS Central Science. 9(3). 466–475. 22 indexed citations
2.
Walker, T.G., Mehdi Shirzadeh, Jacob W. McCabe, et al.. (2022). Temperature Regulates Stability, Ligand Binding (Mg 2+ and ATP), and Stoichiometry of GroEL–GroES Complexes. Journal of the American Chemical Society. 144(6). 2667–2678. 29 indexed citations
3.
Naqvi, Mohsin M., Mario J. Avellaneda, Eline J. Koers, et al.. (2022). Protein chain collapse modulation and folding stimulation by GroEL-ES. Science Advances. 8(9). eabl6293–eabl6293. 17 indexed citations
4.
Gong, Xue, Wei Gai, Junjie Zhang, et al.. (2022). GTP‐stimulated membrane fission by the N‐BAR protein AMPH‐1. Traffic. 24(1). 34–47. 1 indexed citations
5.
Weaver, Jeremy, et al.. (2017). GroEL actively stimulates folding of the endogenous substrate protein PepQ. Nature Communications. 8(1). 15934–15934. 47 indexed citations
6.
Weaver, Jeremy, et al.. (2014). Structural Basis of Substrate Selectivity of E. coli Prolidase. PLoS ONE. 9(10). e111531–e111531. 14 indexed citations
7.
Lin, Zong, et al.. (2013). Repetitive Protein Unfolding by the trans Ring of the GroEL-GroES Chaperonin Complex Stimulates Folding. Journal of Biological Chemistry. 288(43). 30944–30955. 23 indexed citations
8.
Puchalla, Jason, et al.. (2013). Clathrin Coat Disassembly by the Yeast Hsc70/Ssa1p and Auxilin/Swa2p Proteins Observed by Single-particle Burst Analysis Spectroscopy. Journal of Biological Chemistry. 288(37). 26721–26730. 20 indexed citations
9.
Lin, Zong, Damian Madan, & Hays S. Rye. (2008). GroEL stimulates protein folding through forced unfolding. Nature Structural & Molecular Biology. 15(3). 303–311. 124 indexed citations
10.
Lin, Zong & Hays S. Rye. (2004). Expansion and Compression of a Protein Folding Intermediate by GroEL. Molecular Cell. 16(1). 23–34. 69 indexed citations
11.
Rye, Hays S.. (2001). Application of Fluorescence Resonance Energy Transfer to the GroEL-GroES Chaperonin Reaction. Methods. 24(3). 278–288. 36 indexed citations
12.
Rye, Hays S., Alan M. Roseman, Shaoxia Chen, et al.. (1999). GroEL-GroES Cycling. Cell. 97(3). 325–338. 262 indexed citations
13.
Horwich, Arthur L., Steven G. Burston, Hays S. Rye, Jonathan S. Weissman, & Wayne A. Fenton. (1998). [11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods in enzymology on CD-ROM/Methods in enzymology. 290. 141–146. 22 indexed citations
14.
Rye, Hays S., Steven G. Burston, Wayne A. Fenton, et al.. (1997). Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature. 388(6644). 792–798. 338 indexed citations
15.
Drees, Becky, et al.. (1996). Environment-sensitive Labels in Multiplex Fluorescence Analyses of Protein-DNA Complexes. Journal of Biological Chemistry. 271(50). 32168–32173. 24 indexed citations
16.
Rye, Hays S. & Alexander N. Glazer. (1995). Interaction of dimeric intercalating dyes with single-stranded DNA. Nucleic Acids Research. 23(7). 1215–1222. 93 indexed citations
17.
Clark, Steven M., et al.. (1994). High-Sensitivity Capillary Electrophoresis of Double-Stranded DNA Fragments Using Monomeric and Dimeric Fluorescent Intercalating Dyes. Analytical Chemistry. 66(13). 1941–1948. 111 indexed citations
18.
Rye, Hays S., et al.. (1993). Fluorometric Assay Using Dimeric Dyes for Double- and Single-Stranded DNA and RNA with Picogram Sensitivity. Analytical Biochemistry. 208(1). 144–150. 216 indexed citations
19.
Glazer, Alexander N. & Hays S. Rye. (1992). Stable dye–DNA intercalation complexes as reagents for high-sensitivity fluorescence detection. Nature. 359(6398). 859–861. 309 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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