Eva I. Hyde

1.9k total citations
57 papers, 1.5k citations indexed

About

Eva I. Hyde is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, Eva I. Hyde has authored 57 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 28 papers in Genetics and 14 papers in Materials Chemistry. Recurrent topics in Eva I. Hyde's work include RNA and protein synthesis mechanisms (19 papers), Bacterial Genetics and Biotechnology (17 papers) and Enzyme Structure and Function (14 papers). Eva I. Hyde is often cited by papers focused on RNA and protein synthesis mechanisms (19 papers), Bacterial Genetics and Biotechnology (17 papers) and Enzyme Structure and Function (14 papers). Eva I. Hyde collaborates with scholars based in United Kingdom, United States and Australia. Eva I. Hyde's co-authors include Peter F. Searle, Scott A. White, Andrew L. Lovering, Paul R. Race, Gordon C. K. Roberts, A. S. V. Burgen, Stephen Busby, B. Birdsall, J. Feeney and Christopher J. Wrighton and has published in prestigious journals such as Nature, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Eva I. Hyde

56 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Eva I. Hyde United Kingdom 24 1.0k 420 291 143 131 57 1.5k
Kyriacos Petratos Greece 19 1.7k 1.7× 285 0.7× 445 1.5× 177 1.2× 97 0.7× 47 2.0k
Mark Okon Canada 26 1.4k 1.4× 222 0.5× 208 0.7× 211 1.5× 140 1.1× 55 1.9k
Nand K. Vyas United States 21 1.5k 1.5× 304 0.7× 586 2.0× 332 2.3× 193 1.5× 27 2.1k
Nicolas Doucet Canada 25 1.4k 1.4× 211 0.5× 335 1.2× 195 1.4× 93 0.7× 81 1.9k
M.E. Fraser Canada 24 1.3k 1.2× 146 0.3× 587 2.0× 186 1.3× 89 0.7× 60 2.1k
K.H. Kalk Netherlands 13 1.2k 1.1× 274 0.7× 255 0.9× 178 1.2× 44 0.3× 17 1.6k
T. Yano Japan 20 1.0k 1.0× 190 0.5× 296 1.0× 87 0.6× 67 0.5× 74 1.5k
Renate Ulbrich‐Hofmann Germany 28 1.8k 1.8× 205 0.5× 324 1.1× 136 1.0× 125 1.0× 102 2.1k
Jordi Benach United States 22 1.4k 1.4× 299 0.7× 511 1.8× 84 0.6× 41 0.3× 34 2.1k
Ingar Leiros Norway 21 1.3k 1.3× 229 0.5× 241 0.8× 106 0.7× 38 0.3× 49 1.7k

Countries citing papers authored by Eva I. Hyde

Since Specialization
Citations

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

Fields of papers citing papers by Eva I. Hyde

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eva I. Hyde. 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 Eva I. Hyde. The network helps show where Eva I. Hyde may publish in the future.

Co-authorship network of co-authors of Eva I. Hyde

This figure shows the co-authorship network connecting the top 25 collaborators of Eva I. Hyde. A scholar is included among the top collaborators of Eva I. Hyde 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 Eva I. Hyde. Eva I. Hyde 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.
Christofferson, Andrew J., J. L. Ross Anderson, A. Evans, et al.. (2023). Structure and Dynamics of Three Escherichia coli NfsB Nitro-Reductase Mutants Selected for Enhanced Activity with the Cancer Prodrug CB1954. International Journal of Molecular Sciences. 24(6). 5987–5987. 2 indexed citations
2.
White, Scott A., et al.. (2022). The 3D‐structure, kinetics and dynamics of the E. coli nitroreductase NfsA with NADP+ provide glimpses of its catalytic mechanism. FEBS Letters. 596(18). 2425–2440. 11 indexed citations
3.
Rehman, Muhammad Fayyaz ur, Mark Jeeves, & Eva I. Hyde. (2021). Backbone assignments, and effect of Asn deamidation, of the N-terminal region of the partitioning protein IncC1 from the plasmid RK2. Biomolecular NMR Assignments. 15(2). 305–310.
4.
Hyde, Eva I., et al.. (2021). Backbone assignment of E. coli NfsB and the effects of addition of the cofactor analogue nicotinic acid. Biomolecular NMR Assignments. 15(1). 143–151. 3 indexed citations
5.
Ride, Jon P., et al.. (2019). Structure of SPH (self-incompatibility protein homologue) proteins: a widespread family of small, highly stable, secreted proteins. Biochemical Journal. 476(5). 809–826. 8 indexed citations
6.
Ride, Jon P., et al.. (2018). 1H, 13C and 15N NMR assignments of self-incompatibility protein homologue 15 from Arabidopsis thaliana. Biomolecular NMR Assignments. 13(1). 67–70. 1 indexed citations
7.
Tame, Jeremy R. H., Gordon A. Morris, Christopher W. Wharton, et al.. (2010). Order and Disorder in the Domain Organization of the Plasmid Partition Protein KorB. Journal of Biological Chemistry. 285(20). 15440–15449. 11 indexed citations
8.
Jaberipour, Mansooreh, Christopher P. Guise, Jane I. Grove, et al.. (2009). Testing double mutants of the enzyme nitroreductase for enhanced cell sensitisation to prodrugs: Effects of combining beneficial single mutations. Biochemical Pharmacology. 79(2). 102–111. 27 indexed citations
9.
Bingle, Lewis, et al.. (2008). A single aromatic residue in transcriptional repressor protein KorA is critical for cooperativity with its co‐regulator KorB. Molecular Microbiology. 70(6). 1502–1514. 13 indexed citations
10.
Guise, Christopher P., et al.. (2007). Direct positive selection for improved nitroreductase variants using SOS triggering of bacteriophage lambda lytic cycle. Gene Therapy. 14(8). 690–698. 17 indexed citations
11.
Searle, Peter F., Ming‐Jen Chen, Longqin Hu, et al.. (2004). NITROREDUCTASE: A PRODRUG‐ACTIVATING ENZYME FOR CANCER GENE THERAPY. Clinical and Experimental Pharmacology and Physiology. 31(11). 811–816. 107 indexed citations
12.
Grove, Jane I., Andrew L. Lovering, Christopher P. Guise, et al.. (2003). Generation of Escherichia coli nitroreductase mutants conferring improved cell sensitization to the prodrug CB1954.. University of Birmingham Research Portal (University of Birmingham). 63(17). 5532–7. 60 indexed citations
13.
Lovering, Andrew L., Eva I. Hyde, Peter F. Searle, & Scott A. White. (2001). The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 Å, 1.8 Å and 2.4 Å resolution. Journal of Molecular Biology. 309(1). 203–213. 95 indexed citations
14.
Jeeves, Mark, et al.. (1999). Studies of the Escherichia coli Trp repressor binding to its five operators and to variant operator sequences. European Journal of Biochemistry. 265(3). 919–928. 23 indexed citations
15.
Jaseja, Mahesh, et al.. (1999). Secondary Structure of the C-Terminal DNA-Binding Domain of the Transcriptional Activator NifA fromKlebsiella pneumoniae:Spectroscopic Analyses. Archives of Biochemistry and Biophysics. 361(2). 173–182. 4 indexed citations
16.
Michán, Carmen, et al.. (1997). DNA binding and DNA bending by the MelR transcription activator protein from Escherichia coli. Nucleic Acids Research. 25(9). 1685–1693. 32 indexed citations
17.
Jaseja, Mahesh, et al.. (1996). Three‐dimensional structure of the RGD‐containing snake toxin albolabrin in solution, based on 1H NMR spectroscopy and simulated annealing calculations. International journal of peptide & protein research. 48(3). 220–228. 41 indexed citations
18.
Jaseja, Mahesh, Xinjie Lu, Janice A. Williams, et al.. (1994). 1H‐NMR Assignments and Secondary Structure of Dendroaspin, an RGD‐Containing Glycoprotein IIb‐IIIa (αIIb‐β3) Antagonist with a Neurotoxin Fold. European Journal of Biochemistry. 226(3). 861–868. 14 indexed citations
19.
Sutcliffe, Michael J., Mahesh Jaseja, Eva I. Hyde, Xinjie Lu, & Janice A. Williams. (1994). Three-dimensional structure of the RGD-containing neurotoxin homologue dendroaspin. Nature Structural Biology. 1(11). 802–807. 43 indexed citations
20.
Hyde, Eva I., Vasudevan Ramesh, Ronnie O. Frederick, & Gordon C. K. Roberts. (1991). NMR studies of the activation of the Escherichia coli trp repressor. European Journal of Biochemistry. 201(3). 569–579. 7 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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