Rex A. Palmer

2.6k total citations
129 papers, 2.0k citations indexed

About

Rex A. Palmer is a scholar working on Molecular Biology, Organic Chemistry and Materials Chemistry. According to data from OpenAlex, Rex A. Palmer has authored 129 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 56 papers in Molecular Biology, 49 papers in Organic Chemistry and 28 papers in Materials Chemistry. Recurrent topics in Rex A. Palmer's work include Enzyme Structure and Function (21 papers), Crystal structures of chemical compounds (20 papers) and Protein Structure and Dynamics (17 papers). Rex A. Palmer is often cited by papers focused on Enzyme Structure and Function (21 papers), Crystal structures of chemical compounds (20 papers) and Protein Structure and Dynamics (17 papers). Rex A. Palmer collaborates with scholars based in United Kingdom, India and Russia. Rex A. Palmer's co-authors include Mark Ladd, Neera Borkakoti, D. S. Moss, B.S. Potter, Richard E. Dickerson, J. N. Lisgarten, Mark E. Ladd, David S. Moss, C. H. Carlisle and B. Gorinsky and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Rex A. Palmer

121 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rex A. Palmer United Kingdom 24 1.1k 696 405 205 205 129 2.0k
Gábor Náray‐Szabó Hungary 26 1.3k 1.3× 659 0.9× 571 1.4× 372 1.8× 158 0.8× 145 2.9k
Howard Einspahr United States 21 1.1k 1.0× 363 0.5× 308 0.8× 170 0.8× 143 0.7× 58 2.0k
A. Joseph Kalb Israel 27 2.0k 1.9× 788 1.1× 455 1.1× 230 1.1× 121 0.6× 64 2.7k
C.-I. Brändén Sweden 30 2.1k 2.0× 751 1.1× 254 0.6× 227 1.1× 207 1.0× 52 3.2k
Ricardo J. Solá Puerto Rico 15 1.1k 1.1× 266 0.4× 344 0.8× 146 0.7× 229 1.1× 15 1.9k
Monika Haugg Denmark 27 714 0.7× 385 0.6× 966 2.4× 235 1.1× 435 2.1× 161 2.3k
E. Subramanian India 21 950 0.9× 404 0.6× 272 0.7× 171 0.8× 92 0.4× 89 1.5k
N. Sakabe Japan 19 711 0.7× 341 0.5× 331 0.8× 94 0.5× 77 0.4× 59 1.5k
Marjorie M. Harding United Kingdom 22 1.2k 1.1× 715 1.0× 601 1.5× 173 0.8× 489 2.4× 57 2.4k
David M. Rogers United Kingdom 19 1.1k 1.0× 374 0.5× 318 0.8× 206 1.0× 134 0.7× 43 2.0k

Countries citing papers authored by Rex A. Palmer

Since Specialization
Citations

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

Fields of papers citing papers by Rex A. Palmer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Rex A. Palmer. 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 Rex A. Palmer. The network helps show where Rex A. Palmer may publish in the future.

Co-authorship network of co-authors of Rex A. Palmer

This figure shows the co-authorship network connecting the top 25 collaborators of Rex A. Palmer. A scholar is included among the top collaborators of Rex A. Palmer 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 Rex A. Palmer. Rex A. Palmer 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.
Palmer, Rex A., Jon Cooper, C.E. Naylor, et al.. (2023). Ultra-high resolution X-ray structure of orthorhombic bovine pancreatic Ribonuclease A at 100K. BMC Chemistry. 17(1). 91–91. 2 indexed citations
2.
Palmer, Rex A., Carina M. C. Lobley, C.E. Naylor, et al.. (2017). Ultra-high resolution X-ray structures of two forms of human recombinant insulin at 100 K. Chemistry Central Journal. 11(1). 73–73. 8 indexed citations
3.
Palmer, Rex A., et al.. (2016). Synthesis, Crystal Structure and Comparative DFT Studies of a 1D Ni(II) Polymeric Complex of 2-Hydroxypyridine-N-oxide. Journal of Chemical Crystallography. 46(6-7). 269–279. 1 indexed citations
4.
Maveyraud, Laurent, Hideaki Niwa, Valérie Guillet, et al.. (2008). Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA‐II from Sambucus nigra. Proteins Structure Function and Bioinformatics. 75(1). 89–103. 29 indexed citations
5.
Palmer, Rex A., et al.. (2004). Antagonist binding in the rat muscarinic receptor. Computational Biology and Chemistry. 28(5-6). 375–385. 13 indexed citations
6.
Niwa, Hideaki, et al.. (2003). Crystal structure at 3 Å of mistletoe lectin I, a dimeric type‐II ribosome‐inactivating protein, complexed with galactose. European Journal of Biochemistry. 270(13). 2739–2749. 48 indexed citations
7.
Potter, B.S., Rex A. Palmer, Robert Withnall, Terence C. Jenkins, & Babur Z. Chowdhry. (2003). Two new cyclosporin folds observed in the structures of the immunosuppressant cyclosporin G and the formyl peptide receptor antagonist cyclosporin H at ultra-high resolution. Organic & Biomolecular Chemistry. 1(9). 1466–1474. 13 indexed citations
8.
Kar, Tanusree, et al.. (2000). (24R)-24,25-Dihydroxycycloartan-3-one. Acta Crystallographica Section C Crystal Structure Communications. 56(8). 979–980. 1 indexed citations
9.
Chattopadhyay, T., et al.. (1999). Crystallization of Pleurotus ostreatus (oyster mushroom) lectin. Acta Crystallographica Section D Biological Crystallography. 55(9). 1589–1590. 7 indexed citations
10.
Lisgarten, J. N., et al.. (1999). Crystallization of Helix pomatia agglutinin (HPA), a protein from the edible snail. Acta Crystallographica Section D Biological Crystallography. 55(11). 1903–1905. 5 indexed citations
11.
Wright, Colin W., et al.. (1999). Structure of the tetraphenyl borate complex of the indoloquinoline alkaloid cryptolepine. Journal of Chemical Crystallography. 29(4). 449–455. 4 indexed citations
12.
Агапов, И. И., et al.. (1998). In Vitro Efficacy of Conjugates of Anti-CD45 Monoclonal Antibodies With Plant Toxin A-Chains. Transplantation Proceedings. 30(4). 971–973. 2 indexed citations
13.
Tonevitsky, Alexander, Rex A. Palmer, Hideaki Niwa, et al.. (1998). Mistletoe lectin I forms a double trefoil structure. FEBS Letters. 431(3). 367–370. 37 indexed citations
14.
Tonevitsky, Alexander, et al.. (1997). Preliminary crystallographic characterization of ricin agglutinin. Proteins Structure Function and Bioinformatics. 28(4). 586–589. 62 indexed citations
15.
Агапов, И. И., Alexander Tonevitsky, Abdijapar Shamshiev, et al.. (1997). The role of structural domains in RIP II toxin model membrane binding. FEBS Letters. 402(1). 91–93. 15 indexed citations
16.
Palmer, Rex A., et al.. (1993). Crystallization of the Ribosome Inactivating Protein ML1 from Viscum Album (Mistletoe) Complexed with β-d-Galactose. Journal of Molecular Biology. 234(4). 1279–1281. 10 indexed citations
17.
Lisgarten, J. N., Dominique Maes, L. Wyns, et al.. (1993). Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 Å resolution. Conservation of solvent sites in RNase-A high-resolution structures. Acta Crystallographica Section D Biological Crystallography. 49(6). 541–547. 30 indexed citations
18.
Palmer, Rex A., et al.. (1988). Crystallization of mouse pancreatic ribonuclease. Journal of Molecular Biology. 201(3). 659–660. 1 indexed citations
19.
Howlin, Brendan J., G. W. Harris, David S. Moss, & Rex A. Palmer. (1987). X-ray refinement study on the binding of cytidylic acid (2′-CMP) to ribonuclease A. Journal of Molecular Biology. 196(1). 159–164. 23 indexed citations
20.
Palmer, Rex A., et al.. (1983). Acetylcholine receptor site: a proposed model. Journal of Molecular Graphics. 1(4). 94–106. 6 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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