Jill L. Johnson

4.7k total citations
78 papers, 3.7k citations indexed

About

Jill L. Johnson is a scholar working on Molecular Biology, Immunology and Materials Chemistry. According to data from OpenAlex, Jill L. Johnson has authored 78 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 18 papers in Immunology and 13 papers in Materials Chemistry. Recurrent topics in Jill L. Johnson's work include Heat shock proteins research (49 papers), Toxin Mechanisms and Immunotoxins (18 papers) and Enzyme Structure and Function (13 papers). Jill L. Johnson is often cited by papers focused on Heat shock proteins research (49 papers), Toxin Mechanisms and Immunotoxins (18 papers) and Enzyme Structure and Function (13 papers). Jill L. Johnson collaborates with scholars based in United States, United Kingdom and Canada. Jill L. Johnson's co-authors include D O Toft, Elizabeth A. Craig, Abbey D. Zuehlke, Gary A. Flom, James Neuberger, Mark A. Sager, David A. Agard, Chari M. Noddings, Jane Mahoney and James Richards and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Jill L. Johnson

77 papers receiving 3.7k citations

Peers

Jill L. Johnson

IMMUN

EPIDE

Tom C. Karagiannis Australia

Peter Lackner Austria

Massimo Santoro Italy

Xiao‐Ping Dong China

Udai P. Singh United States

Lucia Nencioni Italy

Volker Burkart Germany

Akira Shirahata Japan

Dmitry Alexeev Russia

Anthony Jaworowski Australia

Tom C. Karagiannis Australia

Jill L. Johnson

3.6k ×1.3

427 ×0.8

IMMUN

130 ×0.3

143 ×0.3

251 ×0.7

EPIDE

Citations per year, relative to Jill L. Johnson Jill L. Johnson (= 1×) peers Tom C. Karagiannis

Countries citing papers authored by Jill L. Johnson

Since Specialization

Citations

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

Fields of papers citing papers by Jill L. Johnson

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jill L. Johnson. 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 Jill L. Johnson. The network helps show where Jill L. Johnson may publish in the future.

Co-authorship network of co-authors of Jill L. Johnson

This figure shows the co-authorship network connecting the top 25 collaborators of Jill L. Johnson. A scholar is included among the top collaborators of Jill L. Johnson 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 Jill L. Johnson. Jill L. Johnson is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Morano, Kevin A., et al.. (2024). Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions. Genetics. 227(2). 2 indexed citations

Fulton, Melody D., et al.. (2024). Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function. PLoS Genetics. 20(12). e1011508–e1011508. 2 indexed citations

Johnson, Jill L., et al.. (2024). Ordered ATP hydrolysis in the Hsp90 chaperone is regulated by Aha1 and a conserved post‐translational modification. Protein Science. 34(1). e5255–e5255. 1 indexed citations

Noddings, Chari M., Jill L. Johnson, & David A. Agard. (2023). Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor. Nature Structural & Molecular Biology. 30(12). 1867–1877. 38 indexed citations

Mercier, Rebecca, et al.. (2023). Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle. PLoS Genetics. 19(5). e1010772–e1010772. 7 indexed citations

Wang, Ray Yu‐Ruei, Chari M. Noddings, Elaine Kirschke, et al.. (2021). Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism. Nature. 601(7893). 460–464. 135 indexed citations

Nayak, Dipti D., M.G. Davlieva, Jessica A. Lee, et al.. (2021). EfgA is a conserved formaldehyde sensor that leads to bacterial growth arrest in response to elevated formaldehyde. PLoS Biology. 19(5). e3001208–e3001208. 20 indexed citations

Morano, Kevin A., et al.. (2021). Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects. Genetics. 217(3). 8 indexed citations

Noddings, Chari M., Ray Yu‐Ruei Wang, Jill L. Johnson, & David A. Agard. (2021). Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism. Nature. 601(7893). 465–469. 99 indexed citations

10.

Johnson, Jill L., et al.. (2020). Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions. Cell Stress and Chaperones. 26(1). 3–13. 37 indexed citations

11.

Mercier, Rebecca, et al.. (2019). The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation. Nature Communications. 10(1). 1273–1273. 24 indexed citations

12.

Williams, Felicity, Thomas Faulkner, Derek Kyte, et al.. (2018). Home-based exercise therapy in patients awaiting liver transplantation: protocol for an observational feasibility trial. BMJ Open. 8(1). e019298–e019298. 14 indexed citations

13.

Zuehlke, Abbey D., Michael Reidy, Paul LaPointe, et al.. (2017). An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans. Nature Communications. 8(1). 15328–15328. 33 indexed citations

14.

Bao, Xin, Jill L. Johnson, & Hai Rao. (2015). Rad25 Protein Is Targeted for Degradation by the Ubc4-Ufd4 Pathway. Journal of Biological Chemistry. 290(13). 8606–8612. 3 indexed citations

15.

Armstrong, Matthew J., Jonathan Hazlehurst, Richard Parker, et al.. (2013). Severe asymptomatic non-alcoholic fatty liver disease in routine diabetes care; a multi-disciplinary team approach to diagnosis and management. QJM. 107(1). 33–41. 34 indexed citations

16.

Zuehlke, Abbey D. & Jill L. Johnson. (2009). Hsp90 and co‐chaperones twist the functions of diverse client proteins. Biopolymers. 93(3). 211–217. 202 indexed citations

17.

Johnson, Jill L., et al.. (2006). Nucleotide-Dependent Interaction of Saccharomyces cerevisiae Hsp90 with the Cochaperone Proteins Sti1, Cpr6, and Sba1. Molecular and Cellular Biology. 27(2). 768–776. 63 indexed citations

18.

Flom, Gary A., et al.. (2005). Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae. Current Genetics. 47(6). 368–380. 29 indexed citations

19.

Hon, Thomas, Hee Chul Lee, Angela Hach, et al.. (2001). The Hsp70-Ydj1 Molecular Chaperone Represses the Activity of the Heme Activator Protein Hap1 in the Absence of Heme. Molecular and Cellular Biology. 21(23). 7923–7932. 44 indexed citations

20.

Johnson, Jill L. & Elizabeth A. Craig. (2000). A Role for the Hsp40 Ydj1 in Repression of Basal Steroid Receptor Activity in Yeast. Molecular and Cellular Biology. 20(9). 3027–3036. 47 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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