S.R. Ernst

2.1k total citations
30 papers, 1.6k citations indexed

About

S.R. Ernst is a scholar working on Molecular Biology, Biotechnology and Immunology. According to data from OpenAlex, S.R. Ernst has authored 30 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 9 papers in Biotechnology and 8 papers in Immunology. Recurrent topics in S.R. Ernst's work include Enzyme Structure and Function (8 papers), Toxin Mechanisms and Immunotoxins (8 papers) and Polyamine Metabolism and Applications (5 papers). S.R. Ernst is often cited by papers focused on Enzyme Structure and Function (8 papers), Toxin Mechanisms and Immunotoxins (8 papers) and Polyamine Metabolism and Applications (5 papers). S.R. Ernst collaborates with scholars based in United States, India and Switzerland. S.R. Ernst's co-authors include Jon D. Robertus, A.F. Monzingo, Marvin L. Hackert, Earl Rutenber, Edward J. Collins, Deb Mlsna, Michael P. Ready, R. Hamlin, W.R. Montfort and J. Ernest Villafranca and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

S.R. Ernst

28 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
S.R. Ernst United States 19 971 845 823 343 188 30 1.6k
A.F. Monzingo United States 30 2.0k 2.1× 1.2k 1.4× 1.2k 1.5× 609 1.8× 70 0.4× 62 3.2k
Yen‐Chywan Liaw Taiwan 21 1.2k 1.2× 212 0.3× 308 0.4× 294 0.9× 110 0.6× 51 1.7k
James W. Bodley United States 34 2.4k 2.5× 874 1.0× 423 0.5× 174 0.5× 33 0.2× 83 3.2k
Maša Čemažar Australia 20 1.2k 1.2× 309 0.4× 156 0.2× 324 0.9× 33 0.2× 29 1.4k
Changsoo Chang United States 24 1.1k 1.1× 121 0.1× 170 0.2× 210 0.6× 61 0.3× 64 1.6k
Hiroki Ishida Japan 21 935 1.0× 113 0.1× 411 0.5× 457 1.3× 71 0.4× 69 1.6k
Earl Rutenber United States 12 743 0.8× 792 0.9× 602 0.7× 174 0.5× 5 0.0× 14 1.4k
Kuakarun Krusong Thailand 18 476 0.5× 143 0.2× 212 0.3× 131 0.4× 67 0.4× 55 1.0k
J. Kocourek Czechia 26 1.5k 1.6× 639 0.8× 296 0.4× 619 1.8× 38 0.2× 99 2.2k
Shinya Hanashima Japan 28 1.6k 1.6× 351 0.4× 151 0.2× 145 0.4× 53 0.3× 100 2.1k

Countries citing papers authored by S.R. Ernst

Since Specialization
Citations

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

Fields of papers citing papers by S.R. Ernst

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of S.R. Ernst

This figure shows the co-authorship network connecting the top 25 collaborators of S.R. Ernst. A scholar is included among the top collaborators of S.R. Ernst 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 S.R. Ernst. S.R. Ernst 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.
Monzingo, A.F., et al.. (2002). The Structure of an Allosamidin Complex with the Coccidioides immitis Chitinase Defines a Role for a Second Acid Residue in Substrate-assisted Mechanism. Journal of Molecular Biology. 320(2). 293–302. 64 indexed citations
2.
Monzingo, A.F., et al.. (2002). Structure and cooperativity of a T‐state mutant of histidine decarboxylase from Lactobacillus 30a. Proteins Structure Function and Bioinformatics. 46(3). 321–329. 7 indexed citations
3.
Pascal, John M., Philip J. Day, A.F. Monzingo, et al.. (2001). 2.8‐Å crystal structure of a nontoxic type‐II ribosome‐inactivating protein, ebulin l. Proteins Structure Function and Bioinformatics. 43(3). 319–326. 76 indexed citations
4.
Monzingo, A.F., et al.. (2001). pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a. Journal of Molecular Biology. 306(4). 727–732. 33 indexed citations
5.
6.
Hollis, Thomas, et al.. (2000). The X‐ray structure of a chitinase from the pathogenic fungus Coccidioides immitis. Protein Science. 9(3). 544–551. 99 indexed citations
7.
Knapp, James E., Marcos Antônio de Oliveira, Qiang Xie, et al.. (1999). The Structural and Functional Analysis of the Hemoglobin D Component from Chicken. Journal of Biological Chemistry. 274(10). 6411–6420. 53 indexed citations
8.
Day, Philip J., S.R. Ernst, Arthur E. Frankel, et al.. (1996). Structure and Activity of an Active Site Substitution of Ricin A Chain,. Biochemistry. 35(34). 11098–11103. 49 indexed citations
9.
Robertus, Jon D., Xinjian Yan, S.R. Ernst, et al.. (1996). Structural analysis of ricin and implications for inhibitor design. Toxicon. 34(11-12). 1325–1334. 20 indexed citations
10.
Kern, Andrew D., Marcos Antônio de Oliveira, Ning‐Leh Chang, et al.. (1996). Crystallization of a mammalian ornithine decarboxylase. Proteins Structure Function and Bioinformatics. 24(2). 266–268. 4 indexed citations
11.
Momany, Cory, S.R. Ernst, Ratna Ghosh, Ning‐Leh Chang, & Marvin L. Hackert. (1995). Crystallographic Structure of a PLP-Dependent Ornithine Decarboxylase fromLactobacillus30a to 3.0 Å Resolution. Journal of Molecular Biology. 252(5). 643–655. 101 indexed citations
12.
Mlsna, Deb, et al.. (1993). Structure of recombinant ricin A chain at 2.3 Å. Protein Science. 2(3). 429–435. 85 indexed citations
13.
Hart, P. John, A.F. Monzingo, Michael P. Ready, S.R. Ernst, & Jon D. Robertus. (1993). Crystal Structure of an Endochitinase from Hordeum vulgare L. Seeds. Journal of Molecular Biology. 229(1). 189–193. 71 indexed citations
14.
Kolatkar, Prasanna R., S.R. Ernst, Marvin L. Hackert, et al.. (1992). Structure determination and refinement of homotetrameric hemoglobin from Urechis caupo at 2.5 Å resolution. Acta Crystallographica Section B Structural Science. 48(2). 191–199. 16 indexed citations
15.
Gallagher, Timothy, Michael J. Taylor, S.R. Ernst, Marvin L. Hackert, & N. S. Poonia. (1991). Dipotassium and sodium/potassium crystalline picrate complexes with the crown ether 6,7,9,10,12,13,20,21,23,24,26,27-dodecahydrodibenzo[b,n][1,4,7,10,13,16,19,22]octaoxacyclotetracosin (dibenzo-24-crown-8). Acta Crystallographica Section B Structural Science. 47(3). 362–368. 9 indexed citations
16.
17.
Rutenber, Earl, S.R. Ernst, Edward J. Collins, et al.. (1991). Crystallographic refinement of ricin to 2.5 Å. Proteins Structure Function and Bioinformatics. 10(3). 240–250. 214 indexed citations
18.
Venkatasubramanian, K., Khashti Ballabh Joshi, N. S. Poonia, et al.. (1985). Coordination chemistry of alkali and alkaline earth cations: Synthesis and X-ray crystal structure of cesium (picrate) (benzo-15-crown-5) Cs+C6H2N3O 7 ? (C14H20O5). Journal of Inclusion Phenomena and Macrocyclic Chemistry. 3(4). 453–459. 12 indexed citations
19.
Montfort, W.R., et al.. (1984). The X-ray structure of ricin and implications for immunotoxin design. Acta Crystallographica Section A Foundations of Crystallography. 40(a1). C36–C36.
20.
Ernst, S.R., et al.. (1974). Crystal data for some mescaline salts. Journal of Applied Crystallography. 7(1). 88–90.

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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