Amy R. Wyatt

1.5k total citations
24 papers, 1.1k citations indexed

About

Amy R. Wyatt is a scholar working on Oncology, Molecular Biology and Physiology. According to data from OpenAlex, Amy R. Wyatt has authored 24 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Oncology, 12 papers in Molecular Biology and 6 papers in Physiology. Recurrent topics in Amy R. Wyatt's work include Clusterin in disease pathology (12 papers), Heat shock proteins research (6 papers) and Endoplasmic Reticulum Stress and Disease (4 papers). Amy R. Wyatt is often cited by papers focused on Clusterin in disease pathology (12 papers), Heat shock proteins research (6 papers) and Endoplasmic Reticulum Stress and Disease (4 papers). Amy R. Wyatt collaborates with scholars based in Australia, United Kingdom and United States. Amy R. Wyatt's co-authors include Mark R. Wilson, Justin J. Yerbury, Heath Ecroyd, Christopher M. Dobson, Rebecca A. Dabbs, Elise M. Stewart, Janet R. Kumita, Marie Ranson, Stephen Poon and Ivan Greguric and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Annual Review of Biochemistry.

In The Last Decade

Amy R. Wyatt

24 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Amy R. Wyatt Australia 17 572 373 249 182 144 24 1.1k
John F. Healey United States 32 1.0k 1.8× 257 0.7× 66 0.3× 166 0.9× 120 0.8× 130 2.7k
Chris Bryant United Kingdom 15 593 1.0× 227 0.6× 73 0.3× 81 0.4× 100 0.7× 23 1.0k
Matt Elliott United States 5 1.5k 2.6× 352 0.9× 155 0.6× 270 1.5× 246 1.7× 6 2.2k
Alan L. Chang United States 19 584 1.0× 611 1.6× 84 0.3× 120 0.7× 765 5.3× 45 2.1k
Ruty Mehrian‐Shai United States 21 1.3k 2.3× 242 0.6× 125 0.5× 185 1.0× 205 1.4× 43 2.2k
Manuela Piazzi Italy 21 799 1.4× 128 0.3× 94 0.4× 133 0.7× 107 0.7× 46 1.2k
Satoshi Ohira Japan 18 838 1.5× 375 1.0× 38 0.2× 107 0.6× 112 0.8× 38 1.5k
Tomasz Żemojtel Germany 21 990 1.7× 124 0.3× 102 0.4× 88 0.5× 115 0.8× 50 1.6k
Horst F. Kern Germany 23 540 0.9× 652 1.7× 108 0.4× 219 1.2× 156 1.1× 43 2.1k
Cornelis F. Calkhoven Netherlands 23 1.2k 2.2× 304 0.8× 170 0.7× 144 0.8× 229 1.6× 38 1.8k

Countries citing papers authored by Amy R. Wyatt

Since Specialization
Citations

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

Fields of papers citing papers by Amy R. Wyatt

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Amy R. Wyatt. 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 Amy R. Wyatt. The network helps show where Amy R. Wyatt may publish in the future.

Co-authorship network of co-authors of Amy R. Wyatt

This figure shows the co-authorship network connecting the top 25 collaborators of Amy R. Wyatt. A scholar is included among the top collaborators of Amy R. Wyatt 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 Amy R. Wyatt. Amy R. Wyatt 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.
Wyatt, Amy R., et al.. (2023). Music in medical education: A critical interpretive synthesis. Medical Education. 58(5). 507–522. 2 indexed citations
2.
Wellman, Charles H., et al.. (2022). Low tropical diversity during the adaptive radiation of early land plants. Nature Plants. 8(2). 104–109. 16 indexed citations
3.
Mañucat‐Tan, Noralyn B., et al.. (2020). Hypochlorite-induced aggregation of fibrinogen underlies a novel antioxidant role in blood plasma. Redox Biology. 40. 101847–101847. 11 indexed citations
4.
Kumita, Janet R., Guomao Zhao, Amanda Henry, et al.. (2019). Human pregnancy zone protein stabilizes misfolded proteins including preeclampsia- and Alzheimer’s-associated amyloid beta peptide. Proceedings of the National Academy of Sciences. 116(13). 6101–6110. 59 indexed citations
5.
McMillin, Matthew, Gabriel Frampton, Stephanie Grant, et al.. (2017). Bile Acid-Mediated Sphingosine-1-Phosphate Receptor 2 Signaling Promotes Neuroinflammation during Hepatic Encephalopathy in Mice. Frontiers in Cellular Neuroscience. 11. 191–191. 79 indexed citations
6.
Wyatt, Amy R., et al.. (2017). Amorphous protein aggregates stimulate plasminogen activation, leading to release of cytotoxic fragments that are clients for extracellular chaperones. Journal of Biological Chemistry. 292(35). 14425–14437. 23 indexed citations
7.
Wyatt, Amy R., et al.. (2016). PZP and PAI-2: Structurally-diverse, functionally similar pregnancy proteins?. The International Journal of Biochemistry & Cell Biology. 79. 113–117. 25 indexed citations
8.
Wyatt, Amy R., Janet R. Kumita, Natalie E. Farrawell, Christopher M. Dobson, & Mark R. Wilson. (2015). Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies. PLoS ONE. 10(6). e0130036–e0130036. 13 indexed citations
9.
Wyatt, Amy R., et al.. (2014). Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin. Proceedings of the National Academy of Sciences. 111(20). E2081–90. 68 indexed citations
10.
Wyatt, Amy R., Heath Ecroyd, Christopher M. Dobson, et al.. (2013). Protease‐activated alpha‐2‐macroglobulin can inhibit amyloid formation via two distinct mechanisms. FEBS Letters. 587(5). 398–403. 36 indexed citations
11.
Wyatt, Amy R., Justin J. Yerbury, Heath Ecroyd, & Mark R. Wilson. (2013). Extracellular Chaperones and Proteostasis. Annual Review of Biochemistry. 82(1). 295–322. 143 indexed citations
12.
Wyatt, Amy R., Justin J. Yerbury, Rebecca A. Dabbs, & Mark R. Wilson. (2012). Roles of Extracellular Chaperones in Amyloidosis. Journal of Molecular Biology. 421(4-5). 499–516. 49 indexed citations
13.
Wyatt, Amy R. & Mark R. Wilson. (2012). Acute phase proteins are major clients for the chaperone action of α2-macroglobulin in human plasma. Cell Stress and Chaperones. 18(2). 161–170. 25 indexed citations
14.
Dabbs, Rebecca A., Amy R. Wyatt, Justin J. Yerbury, Heath Ecroyd, & Mark R. Wilson. (2011). Extracellular Chaperones. Topics in current chemistry. 328. 241–268. 24 indexed citations
15.
Wyatt, Amy R., Justin J. Yerbury, Paula Berghofer, et al.. (2011). Clusterin facilitates in vivo clearance of extracellular misfolded proteins. Cellular and Molecular Life Sciences. 68(23). 3919–3931. 108 indexed citations
16.
Dabbs, Rebecca A., Amy R. Wyatt, Justin J. Yerbury, Heath Ecroyd, & Mark R. Wilson. (2010). Extracellular Chaperones. Topics in current chemistry. 2 indexed citations
17.
Wyatt, Amy R., Justin J. Yerbury, Stephen Poon, & Mark R. Wilson. (2009). Therapeutic Targets in Extracellular Protein Deposition Diseases. Current Medicinal Chemistry. 16(22). 2855–2866. 14 indexed citations
18.
Wyatt, Amy R., Justin J. Yerbury, & Mark R. Wilson. (2009). Structural Characterization of Clusterin-Chaperone Client Protein Complexes. Journal of Biological Chemistry. 284(33). 21920–21927. 68 indexed citations
19.
Wyatt, Amy R. & Mark R. Wilson. (2009). Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin. Journal of Biological Chemistry. 285(6). 3532–3539. 39 indexed citations
20.
Wyatt, Amy R., Justin J. Yerbury, Stephen Poon, Rebecca A. Dabbs, & Mark R. Wilson. (2009). Chapter 6 The Chaperone Action of Clusterin and Its Putative Role in Quality Control of Extracellular Protein Folding. Advances in cancer research. 104. 89–114. 63 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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