James P. Robblee

809 total citations
20 papers, 645 citations indexed

About

James P. Robblee is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Epidemiology. According to data from OpenAlex, James P. Robblee has authored 20 papers receiving a total of 645 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 4 papers in Cardiology and Cardiovascular Medicine and 4 papers in Epidemiology. Recurrent topics in James P. Robblee's work include Protein Structure and Dynamics (8 papers), Cardiomyopathy and Myosin Studies (4 papers) and Enzyme Structure and Function (4 papers). James P. Robblee is often cited by papers focused on Protein Structure and Dynamics (8 papers), Cardiomyopathy and Myosin Studies (4 papers) and Enzyme Structure and Function (4 papers). James P. Robblee collaborates with scholars based in United States, France and United Kingdom. James P. Robblee's co-authors include Robert Fairman, Enrique M. De La Cruz, Adrian O. Olivares, Daniel P. Raleigh, Wenxiang Cao, Frederick M. Hughson, Stefan A. Carp, Minghui Wang, Zachary S. Hendsch and Shari Spector and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Journal of Molecular Biology.

In The Last Decade

James P. Robblee

19 papers receiving 638 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
James P. Robblee United States 13 450 196 156 116 87 20 645
Bipasha Barua United States 17 640 1.4× 157 0.8× 407 2.6× 138 1.2× 82 0.9× 26 890
Yasushi Nitanai Japan 10 286 0.6× 155 0.8× 152 1.0× 55 0.5× 32 0.4× 18 508
I. Fita Spain 8 436 1.0× 139 0.7× 76 0.5× 39 0.3× 20 0.2× 12 566
Kim Le France 13 395 0.9× 174 0.9× 37 0.2× 54 0.5× 23 0.3× 21 580
José A. Poveda Spain 19 772 1.7× 70 0.4× 100 0.6× 45 0.4× 48 0.6× 44 946
Guillaume Lenoir France 19 1.1k 2.3× 261 1.3× 39 0.3× 39 0.3× 28 0.3× 42 1.3k
Yadaiah Madasu India 8 193 0.4× 126 0.6× 53 0.3× 40 0.3× 36 0.4× 12 326
Michelle E. McCully United States 10 349 0.8× 76 0.4× 70 0.4× 121 1.0× 20 0.2× 15 455
Karl Bihlmaier Germany 6 1.1k 2.4× 186 0.9× 26 0.2× 42 0.4× 51 0.6× 8 1.2k
Shawn Witham United States 10 559 1.2× 57 0.3× 23 0.1× 120 1.0× 86 1.0× 12 738

Countries citing papers authored by James P. Robblee

Since Specialization
Citations

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

Fields of papers citing papers by James P. Robblee

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by James P. Robblee. 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 James P. Robblee. The network helps show where James P. Robblee may publish in the future.

Co-authorship network of co-authors of James P. Robblee

This figure shows the co-authorship network connecting the top 25 collaborators of James P. Robblee. A scholar is included among the top collaborators of James P. Robblee 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 James P. Robblee. James P. Robblee 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.
Robblee, James P., Julien Robert‐Paganin, Daniel Auguin, et al.. (2023). Mechanism of small molecule inhibition of Plasmodium falciparum myosin A informs antimalarial drug design. Nature Communications. 14(1). 3463–3463. 6 indexed citations
2.
Auguin, Daniel, James P. Robblee, Carlos Kikuti, et al.. (2023). Small molecules modulating force production: A new perspective against myosin-associated diseases. Biophysical Journal. 122(3). 260a–260a.
3.
Robert‐Paganin, Julien, Xiao-Ping Xu, Mark F. Swift, et al.. (2021). The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity. Nature Communications. 12(1). 1892–1892. 18 indexed citations
4.
Robblee, James P., Daniel Auguin, Elena B. Krementsova, et al.. (2020). Full-length Plasmodium falciparum myosin A and essential light chain PfELC structures provide new anti-malarial targets. eLife. 9. 19 indexed citations
5.
Robert‐Paganin, Julien, James P. Robblee, Daniel Auguin, et al.. (2019). Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism. Nature Communications. 10(1). 3286–3286. 39 indexed citations
6.
Robblee, James P., et al.. (2015). Effect of helix length on the stability of the lac repressor antiparallel coiled coil. Biopolymers. 104(4). 395–404. 1 indexed citations
7.
Bain, David L., Qin Yang, James P. Robblee, et al.. (2012). Glucocorticoid Receptor–DNA Interactions: Binding Energetics Are the Primary Determinant of Sequence-Specific Transcriptional Activity. Journal of Molecular Biology. 422(1). 18–32. 31 indexed citations
8.
Robblee, James P., Michael T. Miura, & David L. Bain. (2012). Glucocorticoid Receptor–Promoter Interactions: Energetic Dissection Suggests a Framework for the Specificity of Steroid Receptor-Mediated Gene Regulation. Biochemistry. 51(22). 4463–4472. 26 indexed citations
9.
Robblee, James P., et al.. (2011). From steroid receptors to cytokines: The thermodynamics of self-associating systems. Biophysical Chemistry. 159(1). 24–32. 1 indexed citations
10.
Robblee, James P., et al.. (2011). Dissecting the Linkage Between Transcription Factor Self-Assembly and Site-Specific DNA Binding: The Role of the Analytical Ultracentrifuge. Methods in molecular biology. 796. 187–204. 1 indexed citations
11.
Cao, Wenxiang, et al.. (2005). Magnesium, ADP, and Actin Binding Linkage of Myosin V:  Evidence for Multiple Myosin V−ADP and Actomyosin V−ADP States. Biochemistry. 44(24). 8826–8840. 74 indexed citations
12.
Robblee, James P., et al.. (2005). Thermodynamics of Nucleotide Binding to Actomyosin V and VI:  A Positive Heat Capacity Change Accompanies Strong ADP Binding. Biochemistry. 44(30). 10238–10249. 49 indexed citations
13.
Cedervall, Tommy, Ingemar André, James P. Robblee, et al.. (2005). Calbindin D28k EF-Hand Ligand Binding and Oligomerization:  Four High-Affinity SitesThree Modes of Action. Biochemistry. 44(41). 13522–13532. 9 indexed citations
14.
Robblee, James P., Adrian O. Olivares, & Enrique M. De La Cruz. (2004). Mechanism of Nucleotide Binding to Actomyosin VI. Journal of Biological Chemistry. 279(37). 38608–38617. 48 indexed citations
15.
Julenius, Karin, James P. Robblee, Eva Thulin, et al.. (2002). Coupling of ligand binding and dimerization of helix‐loop‐helix peptides: Spectroscopic and sedimentation analyses of calbindin D9k EF‐hands. Proteins Structure Function and Bioinformatics. 47(3). 323–333. 23 indexed citations
16.
Robblee, James P., et al.. (2001). Effects of charged amino acids at b and c heptad positions on specificity and stability of four‐chain coiled coils. Protein Science. 10(3). 631–637. 19 indexed citations
17.
18.
Demarest, Stephen J., et al.. (2000). Local interactions and the role of the 6-120 disulfide bond in α-lactalbumin: implications for formation of the molten globule state. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1476(1). 9–19. 7 indexed citations
19.
Robblee, James P., et al.. (2000). Structural Analysis of the Neuronal SNARE Protein Syntaxin-1A,. Biochemistry. 39(29). 8470–8479. 92 indexed citations
20.
Spector, Shari, Minghui Wang, Stefan A. Carp, et al.. (2000). Rational Modification of Protein Stability by the Mutation of Charged Surface Residues. Biochemistry. 39(5). 872–879. 170 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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