Richard Charles Garratt

5.7k total citations
153 papers, 4.3k citations indexed

About

Richard Charles Garratt is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Richard Charles Garratt has authored 153 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 117 papers in Molecular Biology, 33 papers in Materials Chemistry and 21 papers in Cell Biology. Recurrent topics in Richard Charles Garratt's work include Enzyme Structure and Function (33 papers), Fungal and yeast genetics research (22 papers) and Protein Structure and Dynamics (21 papers). Richard Charles Garratt is often cited by papers focused on Enzyme Structure and Function (33 papers), Fungal and yeast genetics research (22 papers) and Protein Structure and Dynamics (21 papers). Richard Charles Garratt collaborates with scholars based in Brazil, United Kingdom and United States. Richard Charles Garratt's co-authors include H.M. Pereira, Glaucius Oliva, Ana Paula Ulian de Araújo, Igor Polikarpov, Robert W. Evans, Harren Jhoti, Napoleão Fonseca Valadares, Peter F. Lindley, A.L.B. Ambrosio and S.S. Hasnain and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Richard Charles Garratt

150 papers receiving 4.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Richard Charles Garratt Brazil 35 2.8k 648 507 498 321 153 4.3k
Gilles Labesse France 43 3.1k 1.1× 446 0.7× 562 1.1× 524 1.1× 543 1.7× 127 4.9k
Ambrish Roy United States 17 5.2k 1.8× 658 1.0× 654 1.3× 463 0.9× 436 1.4× 21 7.5k
Marco Biasini Switzerland 8 4.7k 1.7× 630 1.0× 639 1.3× 377 0.8× 500 1.6× 10 7.2k
Xinhua Ji United States 45 5.0k 1.8× 646 1.0× 442 0.9× 336 0.7× 499 1.6× 154 6.4k
Matthew A. Perugini Australia 36 3.2k 1.1× 377 0.6× 1.2k 2.3× 210 0.4× 333 1.0× 132 4.7k
J. Sivaraman Singapore 40 2.7k 1.0× 576 0.9× 369 0.7× 313 0.6× 285 0.9× 153 5.1k
David Eramian United States 7 6.0k 2.1× 813 1.3× 818 1.6× 488 1.0× 555 1.7× 8 8.3k
Matthew C. J. Wilce Australia 51 5.4k 1.9× 774 1.2× 566 1.1× 757 1.5× 458 1.4× 206 9.2k
Milton T. Stubbs Germany 41 3.4k 1.2× 468 0.7× 511 1.0× 255 0.5× 168 0.5× 117 5.6k
C. Geourjon France 28 3.7k 1.3× 683 1.1× 469 0.9× 319 0.6× 449 1.4× 48 5.6k

Countries citing papers authored by Richard Charles Garratt

Since Specialization
Citations

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

Fields of papers citing papers by Richard Charles Garratt

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Richard Charles Garratt. 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 Richard Charles Garratt. The network helps show where Richard Charles Garratt may publish in the future.

Co-authorship network of co-authors of Richard Charles Garratt

This figure shows the co-authorship network connecting the top 25 collaborators of Richard Charles Garratt. A scholar is included among the top collaborators of Richard Charles Garratt 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 Richard Charles Garratt. Richard Charles Garratt 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.
2.
Pereira, H.M., et al.. (2024). Structural insights into the Smirnoff–Wheeler pathway for vitamin C production in the Amazon fruit camu-camu. Journal of Experimental Botany. 75(9). 2754–2771. 4 indexed citations
3.
Pereira, H.M., et al.. (2023). A key piece of the puzzle: The central tetramer of the Saccharomyces cerevisiae septin protofilament and its implications for self-assembly. Journal of Structural Biology. 215(3). 107983–107983. 5 indexed citations
4.
Blázquez‐Sánchez, Paula, H.M. Pereira, Christian Sonnendecker, et al.. (2023). Engineering the catalytic activity of an Antarctic PET‐degrading enzyme by loop exchange. Protein Science. 32(9). e4757–e4757. 15 indexed citations
5.
Brandão-Neto, J., et al.. (2020). Molecular Recognition at Septin Interfaces: The Switches Hold the Key. Journal of Molecular Biology. 432(21). 5784–5801. 19 indexed citations
6.
Macêdo, Joci Neuby Alves, Fernando Luís Barroso da Silva, Alexandre Cassago, et al.. (2019). A revised order of subunits in mammalian septin complexes. Cytoskeleton. 76(9-10). 457–466. 58 indexed citations
7.
Omrane, Mohyeddine, Cyntia Taveneau, Nassima Benzoubir, et al.. (2019). Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity. iScience. 13(5). 138–153. 33 indexed citations
8.
Komives, Elizabeth A., et al.. (2017). Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics. FEBS Journal. 284(12). 1882–1896. 3 indexed citations
9.
Pereira, H.M., Ana Eliza Zeraik, Frederico Moraes Ferreira, et al.. (2017). Filaments and fingers: Novel structural aspects of the single septin from Chlamydomonas reinhardtii. Journal of Biological Chemistry. 292(26). 10899–10911. 13 indexed citations
10.
Andi, Babak, H.M. Pereira, Allen M. Orville, et al.. (2015). The structure of the giant haemoglobin fromGlossoscolex paulistus. Acta Crystallographica Section D Biological Crystallography. 71(6). 1257–1271. 13 indexed citations
11.
García, Wanius, Joci Neuby Alves Macêdo, José M. Andreu, et al.. (2011). Self assembly of human septin 2 into amyloid filaments. Biochimie. 94(3). 628–636. 26 indexed citations
12.
Cabrera, Ricardo, A.L.B. Ambrosio, Richard Charles Garratt, Victoria Guixé, & Jorge Babul. (2008). Crystallographic Structure of Phosphofructokinase-2 from Escherichia coli in Complex with Two ATP Molecules. Implications for Substrate Inhibition. Journal of Molecular Biology. 383(3). 588–602. 26 indexed citations
13.
Valadares, Napoleão Fonseca, Marcelo S. Castilho, Igor Polikarpov, & Richard Charles Garratt. (2007). 2D QSAR studies on thyroid hormone receptor ligands. Bioorganic & Medicinal Chemistry. 15(13). 4609–4617. 19 indexed citations
14.
Ladhani, Shamez, et al.. (2002). A novel method for rapid production and purification of exfoliative toxin A ofStaphylococcus aureus. FEMS Microbiology Letters. 212(1). 35–39. 3 indexed citations
15.
Souza, Dulce Helena Ferreira de, Heloísa Sobreiro Selistre-de-Araújo, Ana M. Moura‐da‐Silva, et al.. (2001). Crystallization and preliminary X-ray analysis of jararhagin, a metalloproteinase/disintegrin fromBothrops jararacasnake venom. Acta Crystallographica Section D Biological Crystallography. 57(8). 1135–1137. 6 indexed citations
16.
Rosa, José Cesar, Lewis Joel Greene, Richard Charles Garratt, et al.. (1999). KM+, a mannose‐binding lectin from artocarpus integrifolia: Amino acid sequence, predicted tertiary structure, carbohydrate recognition, and analysis of the β‐prism fold. Protein Science. 8(1). 13–24. 62 indexed citations
17.
Franco, Glória Regina, Richard Charles Garratt, Manami Tanaka, Andrew J.G. Simpson, & Sérgio D.J. Pena. (1997). Characterization of a Schistosoma mansoni gene encoding a homologue of the Y-box binding protein. Gene. 198(1-2). 5–16. 22 indexed citations
18.
Oliva, Glaucius, Marcos R.M. Fontes, Richard Charles Garratt, et al.. (1995). Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 å resolution. Structure. 3(12). 1323–1332. 69 indexed citations
19.
Horjales, E., Myriam M. Altamirano, Mario L. Calcagno, et al.. (1992). Crystallization and preliminary crystallographic studies of glucosamine-6-phosphate deaminase from Escherichia coli K12. Journal of Molecular Biology. 226(4). 1283–1286. 9 indexed citations
20.
Bailey, Simon, Harren Jhoti, Richard Charles Garratt, et al.. (1987). Structural studies on serum transferrin: the central protein of iron metabolism. Acta Crystallographica Section A Foundations of Crystallography. 43(a1). C30–C30. 1 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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