Jonathan P. Waltho

7.3k total citations
143 papers, 6.0k citations indexed

About

Jonathan P. Waltho is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Jonathan P. Waltho has authored 143 papers receiving a total of 6.0k indexed citations (citations by other indexed papers that have themselves been cited), including 108 papers in Molecular Biology, 49 papers in Materials Chemistry and 18 papers in Spectroscopy. Recurrent topics in Jonathan P. Waltho's work include Enzyme Structure and Function (47 papers), Protein Structure and Dynamics (41 papers) and Prion Diseases and Protein Misfolding (21 papers). Jonathan P. Waltho is often cited by papers focused on Enzyme Structure and Function (47 papers), Protein Structure and Dynamics (41 papers) and Prion Diseases and Protein Misfolding (21 papers). Jonathan P. Waltho collaborates with scholars based in United Kingdom, United States and France. Jonathan P. Waltho's co-authors include Laszlo L. P. Hosszu, Graham S. Jackson, John Collinge, Anthony R. Clarke, Nicola J. Baxter, Peter E. Wright, Andrea M. Hounslow, H. Jane Dyson, Gene Merutka and Dudley H. Williams and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Jonathan P. Waltho

140 papers receiving 5.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jonathan P. Waltho United Kingdom 45 4.6k 1.3k 917 720 667 143 6.0k
Jerson L. Silva Brazil 53 6.3k 1.4× 1.2k 0.9× 559 0.6× 279 0.4× 440 0.7× 233 9.0k
Jayant B. Udgaonkar India 41 4.4k 1.0× 2.3k 1.7× 327 0.4× 532 0.7× 326 0.5× 171 5.2k
Michael A. Baldwin United States 39 4.3k 1.0× 344 0.3× 1.1k 1.2× 1.9k 2.6× 1.2k 1.8× 99 6.1k
Kazuo Kuwata Japan 34 2.4k 0.5× 458 0.3× 500 0.5× 311 0.4× 353 0.5× 128 3.6k
Ronald L. Cerny United States 50 3.9k 0.9× 445 0.3× 258 0.3× 998 1.4× 284 0.4× 136 8.3k
Hassane S. Mchaourab United States 49 5.6k 1.2× 2.2k 1.6× 426 0.5× 1.3k 1.8× 145 0.2× 160 8.7k
Guy Lippens France 50 4.7k 1.0× 673 0.5× 193 0.2× 923 1.3× 236 0.4× 210 7.5k
Rebecca A. Nelson United States 14 3.8k 0.8× 775 0.6× 291 0.3× 359 0.5× 316 0.5× 37 5.2k
Marcus Fändrich Germany 52 7.2k 1.6× 1.1k 0.8× 484 0.5× 615 0.9× 562 0.8× 131 10.5k
Stephen C. Meredith United States 44 4.8k 1.0× 546 0.4× 327 0.4× 884 1.2× 211 0.3× 110 8.5k

Countries citing papers authored by Jonathan P. Waltho

Since Specialization
Citations

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

Fields of papers citing papers by Jonathan P. Waltho

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jonathan P. Waltho. 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 Jonathan P. Waltho. The network helps show where Jonathan P. Waltho may publish in the future.

Co-authorship network of co-authors of Jonathan P. Waltho

This figure shows the co-authorship network connecting the top 25 collaborators of Jonathan P. Waltho. A scholar is included among the top collaborators of Jonathan P. Waltho 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 Jonathan P. Waltho. Jonathan P. Waltho 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.
Baxter, Nicola J., et al.. (2024). Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase. Communications Biology. 7(1). 909–909.
2.
Baxter, Nicola J., et al.. (2021). Enzymatic production of β-glucose 1,6-bisphosphate through manipulation of catalytic magnesium coordination. Green Chemistry. 23(2). 752–762. 3 indexed citations
3.
Baxter, Nicola J., Clare R. Trevitt, Angus J. Robertson, et al.. (2020). Allomorphy as a mechanism of post-translational control of enzyme activity. Nature Communications. 11(1). 5538–5538. 8 indexed citations
4.
Souilhol, Céline, Jovana Serbanovic‐Canic, Hannah Roddie, et al.. (2019). β1 integrin is a sensor of blood flow direction. Journal of Cell Science. 132(11). 48 indexed citations
5.
Cliff, Matthew J., Pavel Macek, Martin Blackledge, et al.. (2019). Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration. Structure. 27(10). 1537–1546.e4. 18 indexed citations
6.
7.
Jin, Yi, Robert W. Molt, Erika Pellegrini, et al.. (2017). Assessing the Influence of Mutation on GTPase Transition States by Using X‐ray Crystallography, 19F NMR, and DFT Approaches. Angewandte Chemie. 129(33). 9864–9867. 1 indexed citations
8.
Trevitt, Clare R., Laszlo L. P. Hosszu, Mark Batchelor, et al.. (2014). N-terminal Domain of Prion Protein Directs Its Oligomeric Association. Journal of Biological Chemistry. 289(37). 25497–25508. 16 indexed citations
9.
Paudel, Liladhar, Ralph W. Adams, P. Király, et al.. (2013). Simultaneously Enhancing Spectral Resolution and Sensitivity in Heteronuclear Correlation NMR Spectroscopy. Angewandte Chemie International Edition. 52(44). 11616–11619. 142 indexed citations
10.
Baxter, Nicola J., et al.. (2011). Prioritization of Charge over Geometry in Transition State Analogues of a Dual Specificity Protein Kinase. Journal of the American Chemical Society. 133(11). 3989–3994. 18 indexed citations
11.
Baxter, Nicola J., Matthew W. Bowler, Matthew J. Cliff, et al.. (2010). Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF3- rather than by phosphoranes. Proceedings of the National Academy of Sciences. 107(10). 4555–4560. 72 indexed citations
12.
Cliff, Matthew J., Matthew W. Bowler, Andrea Varga, et al.. (2010). Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis. Journal of the American Chemical Society. 132(18). 6507–6516. 80 indexed citations
13.
Vilfan, Andrej, Marus̆a Pompe‐Novak, Vito Türk, et al.. (2008). The mechanism of amyloid‐fibril formation by stefin B: Temperature and protein concentration dependence of the rates. Proteins Structure Function and Bioinformatics. 74(2). 425–436. 43 indexed citations
14.
Trevitt, Clare R., C. Jeremy Craven, Julie Perkins, et al.. (2005). Enhanced Ligand Affinity for Receptors in which Components of the Binding Site Are Independently Mobile. Chemistry & Biology. 12(1). 89–97. 8 indexed citations
15.
Zhong, Qi, Martin Watson, Cheri S. Lazar, et al.. (2005). Determinants of the Endosomal Localization of Sorting Nexin 1. Molecular Biology of the Cell. 16(4). 2049–2057. 33 indexed citations
16.
Whitehead, Brian, C. Jeremy Craven, & Jonathan P. Waltho. (2003). Double and Triple Resonance NMR Methods for Protein Assignment. Humana Press eBooks. 60. 29–52. 13 indexed citations
17.
Jackson, Graham S., Laszlo L. P. Hosszu, Andrew F. Hill, et al.. (1999). Reversible Conversion of Monomeric Human Prion Protein Between Native and Fibrilogenic Conformations. Science. 283(5409). 1935–1937. 312 indexed citations
18.
Merutka, Gene, et al.. (1993). Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal. Biochemistry. 32(25). 6348–6355. 63 indexed citations
19.
Waltho, Jonathan P. & Dudley H. Williams. (1989). Aspects of molecular recognition: solvent exclusion and dimerization of the antibiotic ristocetin when bound to a model bacterial cell-wall precursor. Journal of the American Chemical Society. 111(7). 2475–2480. 90 indexed citations
20.
Williams, Dudley H. & Jonathan P. Waltho. (1988). Molecular basis of the activity of antibiotics of the vancomycin group. Biochemical Pharmacology. 37(1). 133–141. 70 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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