Todd Weaver

796 total citations
24 papers, 620 citations indexed

About

Todd Weaver is a scholar working on Molecular Biology, Materials Chemistry and Pulmonary and Respiratory Medicine. According to data from OpenAlex, Todd Weaver has authored 24 papers receiving a total of 620 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 14 papers in Materials Chemistry and 3 papers in Pulmonary and Respiratory Medicine. Recurrent topics in Todd Weaver's work include Enzyme Structure and Function (14 papers), Protein Structure and Dynamics (10 papers) and Glycosylation and Glycoproteins Research (6 papers). Todd Weaver is often cited by papers focused on Enzyme Structure and Function (14 papers), Protein Structure and Dynamics (10 papers) and Glycosylation and Glycoproteins Research (6 papers). Todd Weaver collaborates with scholars based in United States, United Kingdom and France. Todd Weaver's co-authors include Leonard Banaszak, David G. Levitt, M I Donnelly, Patricia Stevens, Irwin A. Rose, Chenglong Li, T. Joseph Kappock, S.E. Ealick, Andrew Rowan and Irene M. Leigh and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Immunology.

In The Last Decade

Todd Weaver

24 papers receiving 602 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Todd Weaver United States 14 460 229 70 63 61 24 620
Fan Chang China 15 480 1.0× 122 0.5× 76 1.1× 25 0.4× 28 0.5× 44 726
Koshiki Mino Japan 17 912 2.0× 99 0.4× 39 0.6× 25 0.4× 32 0.5× 25 1.0k
Susumu Nagasaki Japan 13 256 0.6× 107 0.5× 100 1.4× 113 1.8× 115 1.9× 74 660
Tetsuo Ohmachi Japan 17 612 1.3× 50 0.2× 97 1.4× 92 1.5× 113 1.9× 48 937
Ykelien L. Boersma Netherlands 15 602 1.3× 73 0.3× 17 0.2× 22 0.3× 45 0.7× 25 859
Hans‐Georg Beisel Germany 9 225 0.5× 99 0.4× 25 0.4× 19 0.3× 42 0.7× 11 516
Muneaki Hashimoto Japan 18 431 0.9× 174 0.8× 11 0.2× 115 1.8× 20 0.3× 51 1.0k
Andreas Knapp Germany 14 414 0.9× 73 0.3× 13 0.2× 26 0.4× 44 0.7× 27 685
Kathleen M. Moreton United Kingdom 14 337 0.7× 110 0.5× 31 0.4× 12 0.2× 13 0.2× 22 587
Elena Presecan France 9 661 1.4× 193 0.8× 51 0.7× 73 1.2× 17 0.3× 15 774

Countries citing papers authored by Todd Weaver

Since Specialization
Citations

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

Fields of papers citing papers by Todd Weaver

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Todd Weaver

This figure shows the co-authorship network connecting the top 25 collaborators of Todd Weaver. A scholar is included among the top collaborators of Todd Weaver 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 Todd Weaver. Todd Weaver 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.
May, John F., et al.. (2019). Closed fumarase C active‐site structures reveal SS Loop residue contribution in catalysis. FEBS Letters. 594(2). 337–357. 4 indexed citations
2.
Weaver, Todd, et al.. (2018). Biochemical Characterization of Two Clinically-Relevant Human Fumarase Variants Defective for Oligomerization. PubMed. 12(1). 1–15. 13 indexed citations
3.
Novak, Walter R. P., et al.. (2017). Proteolysis of truncated hemolysin A yields a stable dimerization interface. Acta Crystallographica Section F Structural Biology Communications. 73(3). 138–145. 2 indexed citations
4.
Novak, Walter R. P., et al.. (2015). Sequential unfolding of the hemolysin two‐partner secretion domain from Proteus mirabilis. Protein Science. 24(11). 1841–1855. 3 indexed citations
5.
Weaver, Todd, L.J. Bailey, Grayson T. Wawrzyn, et al.. (2013). Structural and functional studies of truncated hemolysin A from Proteus mirabilis.. Journal of Biological Chemistry. 288(14). 10092–10092. 1 indexed citations
6.
Weaver, Todd, L.J. Bailey, Grayson T. Wawrzyn, et al.. (2009). Structural and Functional Studies of Truncated Hemolysin A from Proteus mirabilis. Journal of Biological Chemistry. 284(33). 22297–22309. 32 indexed citations
7.
Alam, Neyaz, S. E. Olpin, Andrew Rowan, et al.. (2005). Missense Mutations in Fumarate Hydratase in Multiple Cutaneous and Uterine Leiomyomatosis and Renal Cell Cancer. Journal of Molecular Diagnostics. 7(4). 437–443. 49 indexed citations
8.
Weaver, Todd & Scott Cooper. (2005). Exploring protein function and evolution using free online bioinformatics tools. Biochemistry and Molecular Biology Education. 33(5). 319–322. 6 indexed citations
9.
Weaver, Todd. (2005). Structure of free fumarase C fromEscherichia coli. Acta Crystallographica Section D Biological Crystallography. 61(10). 1395–1401. 16 indexed citations
10.
Bailey, Luke, et al.. (2005). Crystallization of truncated hemolysin A fromProteus mirabilis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(4). 448–450. 2 indexed citations
11.
Cox, Bryan D., et al.. (2005). Organelle and translocatable forms of glyoxysomal malate dehydrogenase. FEBS Journal. 272(3). 643–654. 18 indexed citations
12.
Pasula, Rajamouli, et al.. (2002). Morphologic Detection and Functional Assessment of Reconstituted Normal Alveolar Macrophages in the Lungs of SCID Mice. The Journal of Immunology. 169(8). 4504–4510. 12 indexed citations
13.
Banaszak, Leonard, et al.. (2002). X‐ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation. Protein Science. 11(6). 1552–1557. 35 indexed citations
14.
Weaver, Todd. (2000). The π‐helix translates structure into function. Protein Science. 9(1). 201–206. 93 indexed citations
15.
16.
Weaver, Todd, Weiru Wang, & S. E. Ealick. (1999). Purification, crystallization and preliminary X-ray diffraction data from selenomethionine glycinamide ribonucleotide synthetase. Acta Crystallographica Section D Biological Crystallography. 55(2). 518–521. 1 indexed citations
17.
Weaver, Todd, В. Н. Зайцев, I. Zaitseva, et al.. (1998). Crystal structures of native and recombinant yeast fumarase 1 1Edited by D. Rees. Journal of Molecular Biology. 280(3). 431–442. 44 indexed citations
18.
Weaver, Todd, et al.. (1997). Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Protein Science. 6(4). 834–842. 32 indexed citations
19.
Weaver, Todd, Christopher L. Hall, Diane L. Kachel, et al.. (1996). Assessment of in vivo attachment/phagocytosis by alveolar macrophages. Journal of Immunological Methods. 193(2). 149–156. 12 indexed citations
20.
Weaver, Todd, David G. Levitt, M I Donnelly, Patricia Stevens, & Leonard Banaszak. (1995). The multisubunit active site of fumarase C from Escherichia coli. Nature Structural Biology. 2(8). 654–662. 91 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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