Myra E. Conway

1.9k total citations
53 papers, 1.5k citations indexed

About

Myra E. Conway is a scholar working on Molecular Biology, Biochemistry and Physiology. According to data from OpenAlex, Myra E. Conway has authored 53 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 13 papers in Biochemistry and 11 papers in Physiology. Recurrent topics in Myra E. Conway's work include Mitochondrial Function and Pathology (12 papers), Metabolism and Genetic Disorders (9 papers) and Amino Acid Enzymes and Metabolism (8 papers). Myra E. Conway is often cited by papers focused on Mitochondrial Function and Pathology (12 papers), Metabolism and Genetic Disorders (9 papers) and Amino Acid Enzymes and Metabolism (8 papers). Myra E. Conway collaborates with scholars based in United Kingdom, United States and Sweden. Myra E. Conway's co-authors include Susan M. Hutson, Neela H. Yennawar, Mohammad Mainul Islam, Leslie B. Poole, Reidar Wallin, Anna Adlam, Joanna L. Bowtell, Jonathan Fulford, Steven Coles and S.M. Hutson and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Analytical Biochemistry.

In The Last Decade

Myra E. Conway

53 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Myra E. Conway United Kingdom 24 882 380 248 213 173 53 1.5k
Mariarita Bertoldi Italy 25 1.2k 1.3× 374 1.0× 525 2.1× 190 0.9× 313 1.8× 87 2.1k
Oh‐Shin Kwon South Korea 28 1.3k 1.4× 272 0.7× 103 0.4× 492 2.3× 141 0.8× 114 2.4k
Antonella Bobba Italy 27 1.2k 1.4× 598 1.6× 120 0.5× 362 1.7× 122 0.7× 57 2.1k
Song‐Yu Yang United States 25 973 1.1× 371 1.0× 166 0.7× 113 0.5× 301 1.7× 50 1.6k
Sankar Surendran United States 21 736 0.8× 264 0.7× 97 0.4× 161 0.8× 358 2.1× 57 1.6k
Masato Inazu Japan 26 831 0.9× 246 0.6× 224 0.9× 482 2.3× 103 0.6× 78 1.9k
Quentin N. Pye United States 29 969 1.1× 636 1.7× 146 0.6× 351 1.6× 61 0.4× 44 2.7k
Ove Eriksson Finland 30 1.7k 1.9× 484 1.3× 109 0.4× 395 1.9× 255 1.5× 62 2.7k
Jaime Santo‐Domingo Switzerland 22 1.4k 1.5× 375 1.0× 58 0.2× 321 1.5× 142 0.8× 42 2.0k

Countries citing papers authored by Myra E. Conway

Since Specialization
Citations

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

Fields of papers citing papers by Myra E. Conway

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Myra E. Conway. 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 Myra E. Conway. The network helps show where Myra E. Conway may publish in the future.

Co-authorship network of co-authors of Myra E. Conway

This figure shows the co-authorship network connecting the top 25 collaborators of Myra E. Conway. A scholar is included among the top collaborators of Myra E. Conway 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 Myra E. Conway. Myra E. Conway 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.
Makkar, Aaisha, et al.. (2025). A Comprehensive Review of Open-Source Federated Learning Frameworks. Procedia Computer Science. 260. 540–551. 3 indexed citations
2.
Ademowo, Opeyemi Stella, et al.. (2024). Effects of carotenoids on mitochondrial dysfunction. Biochemical Society Transactions. 52(1). 65–74. 9 indexed citations
3.
Crompton, Lucy, et al.. (2024). Differentiation of SH-SY5Y neuroblastoma cells using retinoic acid and BDNF: a model for neuronal and synaptic differentiation in neurodegeneration. In Vitro Cellular & Developmental Biology - Animal. 60(9). 1058–1067. 8 indexed citations
4.
Knerr, Julian, Wei He, Gianluca Sigismondo, et al.. (2022). BCAT1 redox function maintains mitotic fidelity. Cell Reports. 41(3). 111524–111524. 19 indexed citations
5.
Conway, Myra E.. (2020). Emerging Moonlighting Functions of the Branched-Chain Aminotransferase Proteins. Antioxidants and Redox Signaling. 34(13). 1048–1067. 15 indexed citations
6.
Conway, Myra E.. (2020). Alzheimer’s disease: targeting the glutamatergic system. Biogerontology. 21(3). 257–274. 120 indexed citations
7.
Conway, Myra E., et al.. (2019). Crystal structure of an oxidized mutant of human mitochondrial branched-chain aminotransferase. Acta Crystallographica Section F Structural Biology Communications. 76(1). 14–19. 2 indexed citations
9.
Tsivos, Demitra, Michael J. Knight, Catherine Pennington, et al.. (2017). The impact of ageing reveals distinct roles for human dentate gyrus and CA3 in pattern separation and object recognition memory. Scientific Reports. 7(1). 14069–14069. 47 indexed citations
10.
Ashby, Emma L., et al.. (2016). Altered Expression of Human Mitochondrial Branched Chain Aminotransferase in Dementia with Lewy Bodies and Vascular Dementia. Neurochemical Research. 42(1). 306–319. 18 indexed citations
11.
Corry, David B., Christopher Lee, Andrew J. Wilson, et al.. (2013). The Branched-Chain Aminotransferase Proteins: Novel Redox Chaperones for Protein Disulfide Isomerase–Implications in Alzheimer's Disease. Antioxidants and Redox Signaling. 20(16). 2497–2513. 25 indexed citations
12.
Anderson, Elizabeth, Margaret A. Smith, Mark W. Ruddock, et al.. (2013). A novel bioluminescent bacterial biosensor for measurement of Ara-CTP and cytarabine potentiation by fludarabine in seven leukaemic cell lines. Leukemia Research. 37(6). 690–696. 6 indexed citations
13.
Coles, Steven, John T. Hancock, & Myra E. Conway. (2011). Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase. Acta Biochimica et Biophysica Sinica. 44(2). 172–176. 9 indexed citations
14.
Yennawar, Neela H., Mohammad Mainul Islam, Myra E. Conway, Reidar Wallin, & Susan M. Hutson. (2006). Human Mitochondrial Branched Chain Aminotransferase Isozyme. Journal of Biological Chemistry. 281(51). 39660–39671. 35 indexed citations
15.
Goto, Masaru, I. Miyahara, Ken Hirotsu, et al.. (2005). Structural Determinants for Branched-chain Aminotransferase Isozyme-specific Inhibition by the Anticonvulsant Drug Gabapentin. Journal of Biological Chemistry. 280(44). 37246–37256. 75 indexed citations
16.
Conway, Myra E., Neela H. Yennawar, Reidar Wallin, Leslie B. Poole, & Susan M. Hutson. (2003). Human mitochondrial branched chain aminotransferase: structural basis for substrate specificity and role of redox active cysteines. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647(1-2). 61–65. 29 indexed citations
17.
Cooper, Arthur J.L., Myra E. Conway, & Susan M. Hutson. (2002). A continuous 96-well plate spectrophotometric assay for branched-chain amino acid aminotransferases. Analytical Biochemistry. 308(1). 100–105. 31 indexed citations
18.
Cooper, Arthur J.L., Sam A. Bruschi, Myra E. Conway, & Susan M. Hutson. (2002). Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation. Biochemical Pharmacology. 65(2). 181–192. 20 indexed citations
19.
Yennawar, Neela H., et al.. (2001). The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallographica Section D Biological Crystallography. 57(4). 506–515. 39 indexed citations
20.
Conway, Myra E. & Susan M. Hutson. (2000). Mammalian Branched-Chain Aminotransferases. Methods in enzymology on CD-ROM/Methods in enzymology. 324. 355–365. 22 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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