Matthew P. Blakeley

3.1k total citations
92 papers, 2.4k citations indexed

About

Matthew P. Blakeley is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Matthew P. Blakeley has authored 92 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 66 papers in Molecular Biology, 64 papers in Materials Chemistry and 19 papers in Spectroscopy. Recurrent topics in Matthew P. Blakeley's work include Enzyme Structure and Function (61 papers), Protein Structure and Dynamics (29 papers) and Mass Spectrometry Techniques and Applications (18 papers). Matthew P. Blakeley is often cited by papers focused on Enzyme Structure and Function (61 papers), Protein Structure and Dynamics (29 papers) and Mass Spectrometry Techniques and Applications (18 papers). Matthew P. Blakeley collaborates with scholars based in France, United Kingdom and United States. Matthew P. Blakeley's co-authors include A. Podjarny, Andrey Kovalevsky, Paul Langan, Dean A. A. Myles, V. Trevor Forsyth, Michael Haertlein, Flora Meilleur, David A. Keen, Kevin L. Weiss and John R. Helliwell and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Chemical Society Reviews.

In The Last Decade

Matthew P. Blakeley

90 papers receiving 2.4k citations

Peers

Matthew P. Blakeley
Flora Meilleur United States
Charles M. Weeks United States
Kevin L. Weiss United States
S. Zoë Fisher United States
Arwen R. Pearson United Kingdom
Leighton Coates United States
Flora Meilleur United States
Matthew P. Blakeley
Citations per year, relative to Matthew P. Blakeley Matthew P. Blakeley (= 1×) peers Flora Meilleur

Countries citing papers authored by Matthew P. Blakeley

Since Specialization
Citations

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

Fields of papers citing papers by Matthew P. Blakeley

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Matthew P. Blakeley

This figure shows the co-authorship network connecting the top 25 collaborators of Matthew P. Blakeley. A scholar is included among the top collaborators of Matthew P. Blakeley 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 Matthew P. Blakeley. Matthew P. Blakeley 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.
Campos, Cláudia Barbosa Ladeira de, M. Hooper, Oksana Gerlits, et al.. (2023). Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography. Communications Chemistry. 6(1). 162–162. 4 indexed citations
2.
Kneller, Daniel W., Hui Li, G.N. Phillips, et al.. (2022). Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease. Nature Communications. 13(1). 93 indexed citations
3.
Laulumaa, Saara, et al.. (2021). Human myelin protein P2: from crystallography to time‐lapse membrane imaging and neuropathy‐associated variants. FEBS Journal. 288(23). 6716–6735. 10 indexed citations
4.
Caldararu, Octav, Matthew P. Blakeley, Nicolas Coquelle, et al.. (2021). Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps. IUCrJ. 8(4). 633–643. 8 indexed citations
5.
Gerlits, Oksana, Kevin L. Weiss, Matthew P. Blakeley, et al.. (2020). Protein kinase A in the neutron beam: Insights for catalysis from directly observing protons. Methods in enzymology on CD-ROM/Methods in enzymology. 634. 311–331. 1 indexed citations
6.
Aldeghi, Matteo, Matthew P. Blakeley, Andreas Ostermann, et al.. (2019). A molecular mechanism for transthyretin amyloidogenesis. Nature Communications. 10(1). 925–925. 100 indexed citations
7.
Gerlits, Oksana, Kevin L. Weiss, Matthew P. Blakeley, et al.. (2019). Zooming in on protons: Neutron structure of protein kinase A trapped in a product complex. Science Advances. 5(3). eaav0482–eaav0482. 22 indexed citations
8.
Mahon, Brian P., Matthew P. Blakeley, Andreas Ostermann, et al.. (2019). Using neutron crystallography to elucidate the basis of selective inhibition of carbonic anhydrase by saccharin and a derivative. Journal of Structural Biology. 205(2). 147–154. 12 indexed citations
9.
Blakeley, Matthew P. & A. Podjarny. (2018). Neutron macromolecular crystallography. Emerging Topics in Life Sciences. 2(1). 39–55. 17 indexed citations
10.
Schrader, Tobias E., Andreas Ostermann, Leighton Coates, et al.. (2018). Elucidation of Hydrogen Bonding Patterns in Ligand-Free, Lactose- and Glycerol-Bound Galectin-3C by Neutron Crystallography to Guide Drug Design. Journal of Medicinal Chemistry. 61(10). 4412–4420. 32 indexed citations
11.
Saraboji, K., Janina Sprenger, Ulf J. Nilsson, et al.. (2016). Perdeuteration, crystallization, data collection and comparison of five neutron diffraction data sets of complexes of human galectin-3C. Acta Crystallographica Section D Structural Biology. 72(11). 1194–1202. 15 indexed citations
12.
Blakeley, Matthew P.. (2016). Neutron crystallography aids in drug design. IUCrJ. 3(5). 296–297. 5 indexed citations
13.
Casadei, Cecilia M., Andrea Gumiero, Clive Metcalfe, et al.. (2014). Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase. Science. 345(6193). 193–197. 118 indexed citations
15.
Fisher, Stuart, Matthew P. Blakeley, Michele Cianci, Seán McSweeney, & John R. Helliwell. (2012). Determining protonation states in proteins using high-resolution X-ray crystallography. Acta Crystallographica Section A Foundations of Crystallography. 68(a1). s90–s90. 2 indexed citations
16.
Blakeley, Matthew P., et al.. (2012). A joint neutron/X-ray crystallographic study on the mechanism of pectate lyase. Acta Crystallographica Section A Foundations of Crystallography. 68(a1). s91–s91.
17.
Kovalevsky, Andrey, B. Leif Hanson, Sax A. Mason, et al.. (2012). Inhibition ofD-xylose isomerase by polyols: atomic details by joint X-ray/neutron crystallography. Acta Crystallographica Section D Biological Crystallography. 68(9). 1201–1206. 18 indexed citations
18.
Hughes, R.C., Leighton Coates, Matthew P. Blakeley, et al.. (2011). X-ray and neutron crystallographic structure-based mechanism of archaeal inorganic pyrophophatase fromThermococcus thioreducins. Acta Crystallographica Section A Foundations of Crystallography. 67(a1). C773–C774. 1 indexed citations
19.
Leal, Ricardo M. F., Susana C. M. Teixeira, Matthew P. Blakeley, Edward P. Mitchell, & V. Trevor Forsyth. (2009). A preliminary neutron crystallographic study of an A-DNA crystal. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(3). 232–235. 7 indexed citations
20.
Hazemann, Isabelle, Marie-Thérèse Dauvergne, Matthew P. Blakeley, et al.. (2005). High-resolution neutron protein crystallography with radically small crystal volumes: application of perdeuteration to human aldose reductase. Acta Crystallographica Section D Biological Crystallography. 61(10). 1413–1417. 52 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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