Matthew S. Kelker

1.3k total citations
14 papers, 1.0k citations indexed

About

Matthew S. Kelker is a scholar working on Molecular Biology, Immunology and Insect Science. According to data from OpenAlex, Matthew S. Kelker has authored 14 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 6 papers in Immunology and 3 papers in Insect Science. Recurrent topics in Matthew S. Kelker's work include Immune Response and Inflammation (3 papers), Enzyme Structure and Function (3 papers) and Insect Resistance and Genetics (3 papers). Matthew S. Kelker is often cited by papers focused on Immune Response and Inflammation (3 papers), Enzyme Structure and Function (3 papers) and Insect Resistance and Genetics (3 papers). Matthew S. Kelker collaborates with scholars based in United States, United Kingdom and Hong Kong. Matthew S. Kelker's co-authors include Ian A. Wilson, Jungwoo Choe, Wolfgang Peti, Rebecca Page, Jeffery W. Kelly, Ted R. Foss, R. Luke Wiseman, Erik Debler, Steven M. Johnson and Luc Teyton and has published in prestigious journals such as Nature, Science and Journal of the American Chemical Society.

In The Last Decade

Matthew S. Kelker

14 papers receiving 983 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Matthew S. Kelker United States 13 502 483 110 102 85 14 1.0k
Ross Cocklin United States 14 800 1.6× 222 0.5× 63 0.6× 86 0.8× 133 1.6× 20 1.4k
F. J. Kezdy United States 16 503 1.0× 150 0.3× 122 1.1× 103 1.0× 114 1.3× 18 998
R. Chalk United Kingdom 17 599 1.2× 178 0.4× 23 0.2× 114 1.1× 46 0.5× 36 982
Xiao Tao China 5 213 0.4× 556 1.2× 122 1.1× 120 1.2× 26 0.3× 11 850
Liane Mende‐Mueller United States 20 1.2k 2.4× 257 0.5× 73 0.7× 64 0.6× 121 1.4× 26 1.8k
César de Haro Spain 18 1.2k 2.4× 210 0.4× 132 1.2× 134 1.3× 435 5.1× 29 1.5k
Yingliang Wu China 22 972 1.9× 188 0.4× 74 0.7× 153 1.5× 26 0.3× 46 1.3k
Javier Delgado Spain 18 900 1.8× 80 0.2× 128 1.2× 130 1.3× 80 0.9× 33 1.3k
Sergey V. Kostrov Russia 16 547 1.1× 82 0.2× 66 0.6× 32 0.3× 61 0.7× 65 913
Søren Naaby‐Hansen United States 22 977 1.9× 247 0.5× 34 0.3× 20 0.2× 163 1.9× 34 1.9k

Countries citing papers authored by Matthew S. Kelker

Since Specialization
Citations

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

Fields of papers citing papers by Matthew S. Kelker

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Matthew S. Kelker

This figure shows the co-authorship network connecting the top 25 collaborators of Matthew S. Kelker. A scholar is included among the top collaborators of Matthew S. Kelker 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 S. Kelker. Matthew S. Kelker is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

14 of 14 papers shown
1.
Padi, Sathish K.R., James R. Fuller, Thomas Kruse, et al.. (2023). Cryo-EM structures of PP2A:B55–FAM122A and PP2A:B55–ARPP19. Nature. 625(7993). 195–203. 19 indexed citations
2.
Dementiev, Alexey, Anand Sitaram, Timothy Hey, et al.. (2016). The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins. BMC Biology. 14(1). 71–71. 33 indexed citations
3.
Tan, Sek Yee, Murugesan Rangasamy, Haichuan Wang, et al.. (2016). RNAi induced knockdown of a cadherin-like protein (EF531715) does not affect toxicity of Cry34/35Ab1 or Cry3Aa to Diabrotica virgifera virgifera larvae (Coleoptera: Chrysomelidae). Insect Biochemistry and Molecular Biology. 75. 117–124. 15 indexed citations
4.
Kelker, Matthew S., Colin Berry, Steven L. Evans, et al.. (2014). Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1. PLoS ONE. 9(11). e112555–e112555. 56 indexed citations
5.
Kelker, Matthew S., Rebecca Page, & Wolfgang Peti. (2008). Crystal Structures of Protein Phosphatase-1 Bound to Nodularin-R and Tautomycin: A Novel Scaffold for Structure-based Drug Design of Serine/Threonine Phosphatase Inhibitors. Journal of Molecular Biology. 385(1). 11–21. 98 indexed citations
6.
Kelker, Matthew S., Barbara Dancheck, Tingting Ju, et al.. (2007). Structural Basis for Spinophilin−Neurabin Receptor Interaction. Biochemistry. 46(9). 2333–2344. 24 indexed citations
7.
Choe, Jungwoo, Matthew S. Kelker, & Ian A. Wilson. (2005). Crystal Structure of Human Toll-Like Receptor 3 (TLR3) Ectodomain. Science. 309(5734). 581–585. 471 indexed citations
8.
Foss, Ted R., Matthew S. Kelker, R. Luke Wiseman, Ian A. Wilson, & Jeffery W. Kelly. (2005). Kinetic Stabilization of the Native State by Protein Engineering: Implications for Inhibition of Transthyretin Amyloidogenesis. Journal of Molecular Biology. 347(4). 841–854. 57 indexed citations
9.
Choe, Jungwoo, Matthew S. Kelker, & Ian A. Wilson. (2005). Structure of Human Toll-like Receptor 3 (TLR3) Ligand- binding Domain. 1 indexed citations
10.
Wiseman, R. Luke, Steven M. Johnson, Matthew S. Kelker, et al.. (2005). Kinetic Stabilization of an Oligomeric Protein by a Single Ligand Binding Event. Journal of the American Chemical Society. 127(15). 5540–5551. 85 indexed citations
11.
Kelker, Matthew S., Erik Debler, & Ian A. Wilson. (2004). Crystal Structure of Mouse Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) at 1.76Å. Journal of Molecular Biology. 344(5). 1175–1181. 50 indexed citations
12.
Kelker, Matthew S., Wolfgang Peti, Luc Teyton, et al.. (2004). Crystal Structure of Human Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) at 1.47Å. Journal of Molecular Biology. 342(4). 1237–1248. 53 indexed citations
13.
Rudolph, M.G., Matthew S. Kelker, T. Schneider, et al.. (2003). Use of multiple anomalous dispersion to phase highly merohedrally twinned crystals of interleukin-1β. Acta Crystallographica Section D Biological Crystallography. 59(2). 290–298. 15 indexed citations
14.
Kelker, Matthew S., et al.. (2001). Cancer Isoform of a Tumor-Associated Cell Surface NADH Oxidase (tNOX) Has Properties of a Prion. Biochemistry. 40(25). 7351–7354. 29 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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