Marilyn D. Yoder

1.6k total citations
24 papers, 1.3k citations indexed

About

Marilyn D. Yoder is a scholar working on Molecular Biology, Plant Science and Biotechnology. According to data from OpenAlex, Marilyn D. Yoder has authored 24 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 11 papers in Plant Science and 7 papers in Biotechnology. Recurrent topics in Marilyn D. Yoder's work include Polysaccharides and Plant Cell Walls (11 papers), Enzyme Production and Characterization (7 papers) and Enzyme Structure and Function (5 papers). Marilyn D. Yoder is often cited by papers focused on Polysaccharides and Plant Cell Walls (11 papers), Enzyme Production and Characterization (7 papers) and Enzyme Structure and Function (5 papers). Marilyn D. Yoder collaborates with scholars based in United States and France. Marilyn D. Yoder's co-authors include Frances Jurnak, Noel T. Keen, S. E. Lietzke, Rolf Hilgenfeld, George M. Helmkamp, Jacqueline M. Tremblay, Leonard M. Thomas, Susan Heffron, Bernard Henrissat and N. T. Keen and has published in prestigious journals such as Science, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Marilyn D. Yoder

24 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Marilyn D. Yoder United States 13 822 530 310 192 152 24 1.3k
Richard Virden United Kingdom 23 838 1.0× 155 0.3× 269 0.9× 150 0.8× 186 1.2× 53 1.3k
S.R. Ernst United States 19 971 1.2× 343 0.6× 823 2.7× 70 0.4× 170 1.1× 30 1.6k
Z. Marković-Housley Switzerland 19 662 0.8× 179 0.3× 81 0.3× 112 0.6× 198 1.3× 28 1.5k
Russell L. Wrobel United States 20 937 1.1× 467 0.9× 120 0.4× 157 0.8× 47 0.3× 36 1.3k
J. Albert van Kuik Netherlands 23 1.1k 1.3× 219 0.4× 243 0.8× 141 0.7× 49 0.3× 38 1.6k
Namrita Dhillon United States 20 1.3k 1.6× 276 0.5× 68 0.2× 222 1.2× 85 0.6× 29 1.5k
Christine Gietl Germany 26 1.7k 2.1× 967 1.8× 196 0.6× 123 0.6× 62 0.4× 51 2.1k
Karin D. Breunig Germany 27 1.7k 2.0× 377 0.7× 130 0.4× 120 0.6× 165 1.1× 61 2.0k
Maša Čemažar Australia 20 1.2k 1.4× 324 0.6× 156 0.5× 188 1.0× 79 0.5× 29 1.4k
S. E. Lietzke United States 9 462 0.6× 249 0.5× 145 0.5× 167 0.9× 54 0.4× 10 708

Countries citing papers authored by Marilyn D. Yoder

Since Specialization
Citations

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

Fields of papers citing papers by Marilyn D. Yoder

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Marilyn D. Yoder. 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 Marilyn D. Yoder. The network helps show where Marilyn D. Yoder may publish in the future.

Co-authorship network of co-authors of Marilyn D. Yoder

This figure shows the co-authorship network connecting the top 25 collaborators of Marilyn D. Yoder. A scholar is included among the top collaborators of Marilyn D. Yoder 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 Marilyn D. Yoder. Marilyn D. Yoder 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.
Wyckoff, Gerald J., et al.. (2010). Phosphatidylinositol transfer proteins: sequence motifs in structural and evolutionary analyses. Journal of Biomedical Science and Engineering. 3(1). 65–77. 3 indexed citations
2.
Yoder, Marilyn D., et al.. (2006). Differences in Crystal and Solution Structures of the Cytolethal Distending Toxin B Subunit. Journal of Biological Chemistry. 281(35). 25365–25372. 11 indexed citations
3.
Dreyfus, Lawrence A., et al.. (2006). Crystallization ofEscherichia coliCdtB, the biologically active subunit of cytolethal distending toxin. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(3). 192–195. 3 indexed citations
4.
Tremblay, Jacqueline M., et al.. (2005). Structure of PITPβ in Complex with Phosphatidylcholine:  Comparison of Structure and Lipid Transfer to Other PITP Isoforms,. Biochemistry. 44(45). 14760–14771. 36 indexed citations
5.
Dehdashti, Seameen, et al.. (2003). Effect of mutations in the T1.5 loop of pectate lyase A fromErwinia chrysanthemiEC16. Acta Crystallographica Section D Biological Crystallography. 59(7). 1339–1342. 7 indexed citations
6.
Thomas, Leonard M., et al.. (2002). Structure of pectate lyase A: comparison to other isoforms. Acta Crystallographica Section D Biological Crystallography. 58(6). 1008–1015. 25 indexed citations
7.
Tuganova, Alina, Marilyn D. Yoder, & Kirill M. Popov. (2001). An Essential Role of Glu-243 and His-239 in the Phosphotransfer Reaction Catalyzed by Pyruvate Dehydrogenase Kinase. Journal of Biological Chemistry. 276(21). 17994–17999. 21 indexed citations
8.
Yoder, Marilyn D., et al.. (2001). Structure of a Multifunctional Protein. Journal of Biological Chemistry. 276(12). 9246–9252. 120 indexed citations
9.
Tremblay, Jacqueline M., et al.. (1999). X-ray analysis of crystals of rat phosphatidylinositol-transfer protein with bound phosphatidylcholine. Acta Crystallographica Section D Biological Crystallography. 55(2). 522–524. 2 indexed citations
10.
Yoder, Marilyn D., et al.. (1996). An α to β conformational switch in EF-Tu. Structure. 4(10). 1153–1159. 155 indexed citations
11.
Lietzke, S. E., R.D. Scavetta, Marilyn D. Yoder, & Frances Jurnak. (1996). The Refined Three-Dimensional Structure of Pectate Lyase E from Erwinia chrysanthemi at 2.2 A Resolution. PLANT PHYSIOLOGY. 111(1). 73–92. 55 indexed citations
12.
Yoder, Marilyn D. & Frances Jurnak. (1995). The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism). PLANT PHYSIOLOGY. 107(2). 349–364. 62 indexed citations
13.
Yoder, Marilyn D. & Mark A. Schell. (1995). X-ray analysis of crystals of polygalacturonase A fromPseudomonas solanacearum. Acta Crystallographica Section D Biological Crystallography. 51(6). 1097–1098. 2 indexed citations
14.
Henrissat, Bernard, Susan Heffron, Marilyn D. Yoder, S. E. Lietzke, & Frances Jurnak. (1995). Functional Implications of Structure-Based Sequence Alignment of Proteins in the Extracellular Pectate Lyase Superfamily. PLANT PHYSIOLOGY. 107(3). 963–976. 108 indexed citations
15.
Yoder, Marilyn D. & Frances Jurnak. (1995). The parallel β helix and other coiled folds. The FASEB Journal. 9(5). 335–342. 77 indexed citations
16.
Jurnak, Frances, et al.. (1994). Parallel β-domains: a new fold in protein structures. Current Opinion in Structural Biology. 4(6). 802–806. 23 indexed citations
17.
Lietzke, S. E., Marilyn D. Yoder, N. T. Keen, & Frances Jurnak. (1994). The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi. PLANT PHYSIOLOGY. 106(3). 849–862. 81 indexed citations
18.
Yoder, Marilyn D., S. E. Lietzke, & Frances Jurnak. (1993). Unusual structural features in the parallel β-helix in pectate lyases. Structure. 1(4). 241–251. 129 indexed citations
19.
Yoder, Marilyn D., Noel T. Keen, & Frances Jurnak. (1993). New Domain Motif: the Structure of Pectate Lyase C, a Secreted Plant Virulence Factor. Science. 260(5113). 1503–1507. 380 indexed citations
20.
Yoder, Marilyn D., et al.. (1984). An improved bulk purification method for Escherichia coli elongation factor, Ts. Analytical Biochemistry. 141(2). 351–354. 2 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Richard Virden Breakdown of academic impact, for papers by S.R. Ernst Breakdown of academic impact, for papers by Z. Marković-Housley Breakdown of academic impact, for papers by Russell L. Wrobel Breakdown of academic impact, for papers by J. Albert van Kuik Breakdown of academic impact, for papers by Namrita Dhillon Breakdown of academic impact, for papers by Christine Gietl Breakdown of academic impact, for papers by Karin D. Breunig Breakdown of academic impact, for papers by Maša Čemažar Breakdown of academic impact, for papers by S. E. Lietzke
Rankless by CCL
2026