James D. Lear

9.2k total citations · 1 hit paper
87 papers, 7.8k citations indexed

About

James D. Lear is a scholar working on Molecular Biology, Epidemiology and Biomaterials. According to data from OpenAlex, James D. Lear has authored 87 papers receiving a total of 7.8k indexed citations (citations by other indexed papers that have themselves been cited), including 72 papers in Molecular Biology, 11 papers in Epidemiology and 9 papers in Biomaterials. Recurrent topics in James D. Lear's work include Lipid Membrane Structure and Behavior (33 papers), RNA and protein synthesis mechanisms (26 papers) and Protein Structure and Dynamics (22 papers). James D. Lear is often cited by papers focused on Lipid Membrane Structure and Behavior (33 papers), RNA and protein synthesis mechanisms (26 papers) and Protein Structure and Dynamics (22 papers). James D. Lear collaborates with scholars based in United States, Canada and Italy. James D. Lear's co-authors include William F. DeGrado, Holly Gratkowski, Zelda R. Wasserman, Christin T. Choma, Joel Bennett, P. Leslie Dutton, Lawrence H. Pinto, Robert A. Lamb, Dan E. Robertson and A. Joshua Wand and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

James D. Lear

87 papers receiving 7.7k citations

Hit Papers

Design and synthesis of m... 1994 2026 2004 2015 1994 100 200 300 400

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
James D. Lear 6.1k 905 848 754 687 87 7.8k
Karl Harlos 5.4k 0.9× 734 0.8× 819 1.0× 793 1.1× 270 0.4× 156 10.5k
Christian Herrmann 6.5k 1.1× 1.7k 1.9× 1.1k 1.3× 380 0.5× 281 0.4× 162 9.1k
Timothy R. Dafforn 5.0k 0.8× 1.0k 1.1× 566 0.7× 166 0.2× 707 1.0× 152 7.4k
Tom Alber 10.3k 1.7× 1.2k 1.4× 3.0k 3.6× 890 1.2× 633 0.9× 131 13.1k
Shiroh Futaki 15.0k 2.5× 654 0.7× 944 1.1× 258 0.3× 425 0.6× 330 17.4k
Rodolfo Ghirlando 9.9k 1.6× 1.6k 1.8× 965 1.1× 435 0.6× 540 0.8× 213 12.4k
Maxim V. Petoukhov 6.8k 1.1× 856 0.9× 3.0k 3.5× 381 0.5× 604 0.9× 86 9.5k
Shohei Koide 7.0k 1.1× 532 0.6× 955 1.1× 156 0.2× 571 0.8× 169 9.7k
Yves Engelborghs 5.0k 0.8× 928 1.0× 1.0k 1.2× 332 0.4× 334 0.5× 202 8.3k
Carlo Pedone 8.8k 1.4× 379 0.4× 1.1k 1.3× 446 0.6× 926 1.3× 401 11.9k

Countries citing papers authored by James D. Lear

Since Specialization
Citations

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

Fields of papers citing papers by James D. Lear

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of James D. Lear

This figure shows the co-authorship network connecting the top 25 collaborators of James D. Lear. A scholar is included among the top collaborators of James D. Lear 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 D. Lear. James D. Lear 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.
Polishchuk, Alexei L., Lidia Cristian, Lawrence H. Pinto, James D. Lear, & William F. DeGrado. (2013). Mechanistic insights from functional characterization of an unnatural His37 mutant of the influenza A/M2 protein. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1838(4). 1082–1087. 4 indexed citations
2.
Wu, Wenman, Dipali Sinha, Calvin K. Yip, et al.. (2008). Factor XI Homodimer Structure Is Essential for Normal Proteolytic Activation by Factor XIIa, Thrombin, and Factor XIa. Journal of Biological Chemistry. 283(27). 18655–18664. 35 indexed citations
3.
Yin, Hang, Joanna S.G. Slusky, Bryan W. Berger, et al.. (2007). Computational Design of Peptides That Target Transmembrane Helices. Science. 315(5820). 1817–1822. 239 indexed citations
4.
Carnini, Anna, James D. Lear, & Roderic G. Eckenhoff. (2007). Inhaled Anesthetic Modulation of Amyloid β 1-40 Assembly and Growth. Current Alzheimer Research. 4(3). 233–241. 35 indexed citations
5.
North, Benjamin, et al.. (2006). Characterization of a Membrane Protein Folding Motif, the Ser Zipper, Using Designed Peptides. Journal of Molecular Biology. 359(4). 930–939. 46 indexed citations
6.
Kono, Hidetoshi, et al.. (2004). Computational design of water-soluble analogues of the potassium channel KcsA. Proceedings of the National Academy of Sciences. 101(7). 1828–1833. 88 indexed citations
7.
Lear, James D., Amanda L. Stouffer, Holly Gratkowski, Vikas Nanda, & William F. DeGrado. (2004). Association of a Model Transmembrane Peptide Containing Gly in a Heptad Sequence Motif. Biophysical Journal. 87(5). 3421–3429. 34 indexed citations
9.
Gratkowski, Holly, et al.. (2002). Cooperativity and Specificity of Association of a Designed Transmembrane Peptide. Biophysical Journal. 83(3). 1613–1619. 25 indexed citations
10.
Ghirlanda, Giovanna, James D. Lear, N.L. Ogihara, David Eisenberg, & William F. DeGrado. (2002). A Hierarchic Approach to the Design of Hexameric Helical Barrels. Journal of Molecular Biology. 319(1). 243–253. 28 indexed citations
11.
Li, Renhao, Charles R. Babu, James D. Lear, et al.. (2001). Oligomerization of the integrin αIIbβ3: Roles of the transmembrane and cytoplasmic domains. Proceedings of the National Academy of Sciences. 98(22). 12462–12467. 139 indexed citations
12.
Lear, James D., William F. DeGrado, Christin T. Choma, & Holly Gratkowski. (2000). Asparagine-mediated self-association of a model transmembrane helix.. Nature Structural Biology. 7(2). 161–166. 320 indexed citations
13.
Zhong, Qingfeng, D. M. Newns, Pratap Pattnaik, James D. Lear, & Michael L. Klein. (2000). Two possible conducting states of the influenza A virus M2 ion channel. FEBS Letters. 473(2). 195–198. 33 indexed citations
14.
Gandhi, Chris S., James D. Lear, Gregg R. Dieckmann, et al.. (1999). Cu(II) Inhibition of the Proton Translocation Machinery of the Influenza A Virus M2 Protein. Journal of Biological Chemistry. 274(9). 5474–5482. 102 indexed citations
15.
Lear, James D., et al.. (1998). Characterization of Actinobacillus actinomycetemcomitans leukotoxin pore formation in HL60 cells. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1406(2). 175–187. 27 indexed citations
16.
Ghirlanda, Giovanna, James D. Lear, Angela Lombardi, & William F. DeGrado. (1998). From synthetic coiled coils to functional proteins: automated design of a receptor for the calmodulin-binding domain of calcineurin. Journal of Molecular Biology. 281(2). 379–391. 32 indexed citations
17.
Siegel, David P., et al.. (1998). Morphological Changes and Fusogenic Activity of Influenza Virus Hemagglutinin. Biophysical Journal. 74(1). 54–62. 59 indexed citations
18.
Pantoliano, Michael W., Robert A. Horlick, Barry A. Springer, et al.. (1994). Multivalent Ligand-Receptor Binding Interactions in the Fibroblast Growth Factor System Produce a Cooperative Growth Factor and Heparin Mechanism for Receptor Dimerization. Biochemistry. 33(34). 10229–10248. 219 indexed citations
19.
Chung, Laura A., James D. Lear, & William F. DeGrado. (1992). Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesicles. Biochemistry. 31(28). 6608–6616. 107 indexed citations
20.
DeGrado, William F. & James D. Lear. (1990). Conformationally constrained α‐helical peptide models for protein ion channels. Biopolymers. 29(1). 205–213. 64 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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