Lindsay Sawyer

9.0k total citations · 3 hit papers
103 papers, 7.3k citations indexed

About

Lindsay Sawyer is a scholar working on Molecular Biology, Food Science and Materials Chemistry. According to data from OpenAlex, Lindsay Sawyer has authored 103 papers receiving a total of 7.3k indexed citations (citations by other indexed papers that have themselves been cited), including 53 papers in Molecular Biology, 37 papers in Food Science and 30 papers in Materials Chemistry. Recurrent topics in Lindsay Sawyer's work include Proteins in Food Systems (36 papers), Enzyme Structure and Function (29 papers) and Enzyme Production and Characterization (24 papers). Lindsay Sawyer is often cited by papers focused on Proteins in Food Systems (36 papers), Enzyme Structure and Function (29 papers) and Enzyme Production and Characterization (24 papers). Lindsay Sawyer collaborates with scholars based in United Kingdom, United States and France. Lindsay Sawyer's co-authors include George Kontopidis, Carl Holt, A.C.T. North, Elias Eliopoulos, Igor Polikarpov, Su‐Ying Wu, Sharon Brownlow, Miroslav Z. Papiz, João H. Morais‐Cabral and Simon Parsons and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Lindsay Sawyer

102 papers receiving 7.0k citations

Hit Papers

The structure of β-lactog... 1986 2026 1999 2012 1986 1997 2004 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Lindsay Sawyer United Kingdom 41 3.5k 3.0k 1.1k 910 813 103 7.3k
Geoffrey B. Jameson New Zealand 49 2.5k 0.7× 1.3k 0.4× 2.7k 2.4× 589 0.6× 385 0.5× 240 7.4k
Faizan Ahmad India 52 6.7k 1.9× 855 0.3× 1.5k 1.3× 410 0.5× 360 0.4× 346 10.2k
Rosangela Marchelli Italy 50 3.4k 1.0× 937 0.3× 538 0.5× 319 0.4× 334 0.4× 239 7.6k
Serge Pérez France 40 2.5k 0.7× 1.3k 0.4× 671 0.6× 1.8k 2.0× 509 0.6× 168 6.3k
Gary M. Gray United States 53 2.4k 0.7× 459 0.2× 507 0.4× 1.3k 1.4× 381 0.5× 266 9.5k
Jen Tsi Yang United States 42 8.9k 2.5× 644 0.2× 1.7k 1.5× 407 0.4× 407 0.5× 127 12.4k
H. Susi United States 31 3.5k 1.0× 979 0.3× 916 0.8× 357 0.4× 247 0.3× 66 6.7k
Lawrence J. Berliner United States 43 2.4k 0.7× 657 0.2× 1.4k 1.2× 733 0.8× 130 0.2× 168 5.9k
Marcia E. Newcomer United States 41 3.4k 1.0× 550 0.2× 576 0.5× 412 0.5× 269 0.3× 102 5.7k
D. Michael Byler United States 24 2.9k 0.8× 916 0.3× 726 0.6× 336 0.4× 216 0.3× 48 5.4k

Countries citing papers authored by Lindsay Sawyer

Since Specialization
Citations

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

Fields of papers citing papers by Lindsay Sawyer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Lindsay Sawyer. 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 Lindsay Sawyer. The network helps show where Lindsay Sawyer may publish in the future.

Co-authorship network of co-authors of Lindsay Sawyer

This figure shows the co-authorship network connecting the top 25 collaborators of Lindsay Sawyer. A scholar is included among the top collaborators of Lindsay Sawyer 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 Lindsay Sawyer. Lindsay Sawyer 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.
Thireou, Trias, Yvan Choiset, Thomas Haertlé, et al.. (2018). Thermodynamic, crystallographic and computational studies of non-mammalian fatty acid binding to bovine β-Lactoglobulin. International Journal of Biological Macromolecules. 118(Pt A). 296–303. 15 indexed citations
2.
Shafaei, Zahra, Behafarid Ghalandari, Akbar Vaseghi, et al.. (2017). β-Lactoglobulin: An efficient nanocarrier for advanced delivery systems. Nanomedicine Nanotechnology Biology and Medicine. 13(5). 1685–1692. 85 indexed citations
3.
Kontopidis, George, et al.. (2014). Ovine β-lactoglobulin at atomic resolution. Acta Crystallographica Section F Structural Biology Communications. 70(11). 1498–1503. 6 indexed citations
4.
Kontopidis, George, Carl Holt, & Lindsay Sawyer. (2004). Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function. Journal of Dairy Science. 87(4). 785–796. 580 indexed citations breakdown →
5.
Gaudin, Jean‐Charles, Jean‐Marc Chobert, Tatiana V. Burova, et al.. (2004). A Recombinant C121S Mutant of Bovine β-Lactoglobulin Is More Susceptible to Peptic Digestion and to Denaturation by Reducing Agents and Heating. Biochemistry. 43(20). 6312–6321. 47 indexed citations
6.
Clarke, David J., et al.. (2004). Cloning, expression, purification, crystallization and preliminary X-ray characterization of the full-length single-stranded DNA-binding protein from the hyperthermophilic bacteriumAquifex aeolicus. Acta Crystallographica Section D Biological Crystallography. 60(11). 2009–2012. 1 indexed citations
7.
Alexeev, Dmitry, Paul N. Barlow, Jean‐Damien Charrier, et al.. (2003). Synthesis, Structural and Biological Studies of Ubiquitin Mutants Containing (2S, 4S)‐5‐Fluoroleucine Residues Strategically Placed in the Hydrophobic Core. ChemBioChem. 4(9). 894–896. 28 indexed citations
8.
Valente‐Mesquita, Vera Lúcia, et al.. (2001). Crystal structures of bovine β‐lactoglobulin in the orthorhombic space group C2221. European Journal of Biochemistry. 268(2). 477–484. 81 indexed citations
9.
Burova, T. V., et al.. (2000). Why has porcine VEG protein unusually high stability and suppressed binding ability?. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1478(2). 267–279. 9 indexed citations
10.
Alexeev, Dmitry, Marina Alexeeva, Robert L. Baxter, et al.. (1998). The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme 1 1Edited by R. Huber. Journal of Molecular Biology. 284(2). 401–419. 114 indexed citations
11.
Muir, Tom W., R. Ramage, Kevin Shaw, et al.. (1997). Synthetic, structural and biological studies of the ubiquitin system: synthesis and crystal structure of an analogue containing unnatural amino acids. Biochemical Journal. 323(3). 727–734. 17 indexed citations
12.
Morais‐Cabral, João H., Gordon L. Atkins, Luis Sánchez‐Pulido, et al.. (1995). Arachidonic acid binds to apolipoprotein D: implications for the protein's function. FEBS Letters. 366(1). 53–56. 118 indexed citations
13.
Alexeev, Dmitry, et al.. (1995). Substrate binding and carboxylation by dethiobiotin synthetase — a kinetic and X-ray study. Structure. 3(11). 1207–1215. 21 indexed citations
14.
Alexeev, Dmitry, Charlotte Boys, Lindsay Sawyer, et al.. (1994). Sequence and Crystallization of Escherichia coli Dethiobiotin Synthetase, the Penultimate Enzyme of Biotin Biosynthesis. Journal of Molecular Biology. 235(2). 774–776. 16 indexed citations
15.
Coussons, Peter J., Nicholas C. Price, Sharon M. Kelly, Bradley J. Smith, & Lindsay Sawyer. (1992). Transglutaminase catalyses the modification of glutamine side chains in the C-terminal region of bovine β-lactoglobulin. Biochemical Journal. 283(3). 803–806. 23 indexed citations
16.
Adams, Paul D. & Lindsay Sawyer. (1990). Structure of rodent urinary proteins. Biochemical Society Transactions. 18(5). 936–937. 7 indexed citations
17.
Holt, Carl & Lindsay Sawyer. (1988). Primary and predicted secondary structures of the caseins in relation to their biological functions. Protein Engineering Design and Selection. 2(4). 251–259. 110 indexed citations
18.
Monaco, Hugo L., Giuseppe Zanotti, Paola Spadon, et al.. (1987). Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution. Journal of Molecular Biology. 197(4). 695–706. 303 indexed citations
19.
Meyer, T.E., et al.. (1981). A reassessment of the structure of Paracoccus cytochrome c-550. Journal of Molecular Biology. 147(2). 351–356. 39 indexed citations
20.
Sawyer, Lindsay. (1972). A fourth crystal form of rabbit muscle aldolase. Journal of Molecular Biology. 71(2). 503–505. 10 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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