Barry A. Springer

5.2k total citations · 2 hit papers
29 papers, 4.5k citations indexed

About

Barry A. Springer is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, Barry A. Springer has authored 29 papers receiving a total of 4.5k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 17 papers in Cell Biology and 5 papers in Physiology. Recurrent topics in Barry A. Springer's work include Hemoglobin structure and function (15 papers), Protein Structure and Dynamics (7 papers) and Erythrocyte Function and Pathophysiology (5 papers). Barry A. Springer is often cited by papers focused on Hemoglobin structure and function (15 papers), Protein Structure and Dynamics (7 papers) and Erythrocyte Function and Pathophysiology (5 papers). Barry A. Springer collaborates with scholars based in United States, United Kingdom and Italy. Barry A. Springer's co-authors include Stephen G. Sligar, John S. Olson, G.N. Phillips, Michael W. Pantoliano, Karen D. Egeberg, Ronald J. Rohlfs, Antony J. Mathews, L D Thompson, Theodore E. Carver and Dimitrios Morikis and has published in prestigious journals such as Nature, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Barry A. Springer

28 papers receiving 4.4k citations

Hit Papers

High-Density Miniaturized Thermal Shift Assays as a Gener... 1994 2026 2004 2015 2001 1994 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Barry A. Springer United States 23 3.2k 2.7k 627 538 422 29 4.5k
Boaz Shaanan Israel 24 2.2k 0.7× 1.3k 0.5× 484 0.8× 398 0.7× 472 1.1× 39 3.3k
G. Fermi United Kingdom 20 1.7k 0.5× 2.1k 0.8× 785 1.3× 639 1.2× 340 0.8× 33 3.1k
Hilary Muirhead United Kingdom 27 2.3k 0.7× 1.2k 0.5× 723 1.2× 372 0.7× 961 2.3× 42 3.6k
Robert M. Sweet United States 23 3.0k 0.9× 1.1k 0.4× 234 0.4× 148 0.3× 1.0k 2.4× 40 4.4k
H.C. Watson United Kingdom 35 3.8k 1.2× 1.2k 0.5× 395 0.6× 229 0.4× 1.9k 4.5× 68 5.4k
Franca Ascoli Italy 27 1.5k 0.5× 1.2k 0.5× 441 0.7× 294 0.5× 172 0.4× 145 2.5k
Sherman Beychok United States 31 2.4k 0.7× 1.1k 0.4× 432 0.7× 286 0.5× 450 1.1× 73 3.6k
Sushmita Mukherjee United States 34 3.5k 1.1× 1.1k 0.4× 564 0.9× 61 0.1× 259 0.6× 74 5.6k
Sherwin S. Lehrer United States 42 4.3k 1.3× 1.0k 0.4× 209 0.3× 77 0.1× 783 1.9× 104 6.6k
Doug Barrick United States 38 3.6k 1.1× 1.1k 0.4× 245 0.4× 144 0.3× 1.3k 3.0× 89 4.2k

Countries citing papers authored by Barry A. Springer

Since Specialization
Citations

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

Fields of papers citing papers by Barry A. Springer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Barry A. Springer

This figure shows the co-authorship network connecting the top 25 collaborators of Barry A. Springer. A scholar is included among the top collaborators of Barry A. Springer 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 Barry A. Springer. Barry A. Springer 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.
Xu, Guozhang, Terry V. Hughes, Peter J. Connolly, et al.. (2008). Discovery of novel 4-amino-6-arylaminopyrimidine-5-carbaldehyde oximes as dual inhibitors of EGFR and ErbB-2 protein tyrosine kinases. Bioorganic & Medicinal Chemistry Letters. 18(12). 3495–3499. 48 indexed citations
2.
Xu, Guozhang, M.C. Abad, Peter J. Connolly, et al.. (2008). 4-Amino-6-arylamino-pyrimidine-5-carbaldehyde hydrazones as potent ErbB-2/EGFR dual kinase inhibitors. Bioorganic & Medicinal Chemistry Letters. 18(16). 4615–4619. 80 indexed citations
3.
Kranz, James K., Winnie Chan, Geoffrey T. Struble, et al.. (2007). Enhancing Recombinant Protein Quality and Yield by Protein Stability Profiling. SLAS DISCOVERY. 12(3). 418–428. 71 indexed citations
4.
Schalk‐Hihi, Céline, Hongchang Ma, Geoffrey T. Struble, et al.. (2006). Protein Engineering of the Colony-stimulating Factor-1 Receptor Kinase Domain for Structural Studies. Journal of Biological Chemistry. 282(6). 4085–4093. 10 indexed citations
5.
Schubert, Carsten J., Céline Schalk‐Hihi, Geoffrey T. Struble, et al.. (2006). Crystal Structure of the Tyrosine Kinase Domain of Colony-stimulating Factor-1 Receptor (cFMS) in Complex with Two Inhibitors. Journal of Biological Chemistry. 282(6). 4094–4101. 56 indexed citations
6.
Kervinen, Jukka, Hongchang Ma, Shariff Bayoumy, et al.. (2006). Effect of construct design on MAPKAP kinase-2 activity, thermodynamic stability and ligand-binding affinity. Archives of Biochemistry and Biophysics. 449(1-2). 47–56. 15 indexed citations
7.
Bayburt, Timothy H., et al.. (2006). Functional reconstitution of β2-adrenergic receptors utilizing self-assembling Nanodisc technology. BioTechniques. 40(5). 601–612. 168 indexed citations
8.
Pantoliano, Michael W., Eugene C. Petrella, Victor S. Lobanov, et al.. (2001). High-Density Miniaturized Thermal Shift Assays as a General Strategy for Drug Discovery. SLAS DISCOVERY. 6(6). 429–440. 704 indexed citations breakdown →
9.
Pantoliano, Michael W., Eugene C. Petrella, Victor S. Lobanov, et al.. (2001). High-Density Miniaturized Thermal Shift Assays as a General Strategy for Drug Discovery. 6(6). 429–440. 22 indexed citations
10.
Springer, Barry A., et al.. (1995). ChemInform Abstract: Mechanisms of Ligand Recognition in Myoglobin.. ChemInform. 26(5).
11.
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
12.
Thompson, L D, Michael W. Pantoliano, & Barry A. Springer. (1994). Energetic Characterization of the Basic Fibroblast Growth Factor-Heparin Interaction: Identification of the Heparin Binding Domain. Biochemistry. 33(13). 3831–3840. 256 indexed citations
13.
Braunstein, David, K. R. Chu, Karen D. Egeberg, et al.. (1993). Ligand binding to heme proteins: III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin. Biophysical Journal. 65(6). 2447–2454. 87 indexed citations
14.
Phillips, G.N., Robert M. Arduini, Barry A. Springer, & Stephen G. Sligar. (1990). Crystal structure of myoglobin form a synthetic gene. Proteins Structure Function and Bioinformatics. 7(4). 358–365. 96 indexed citations
15.
Egeberg, Karen D., Barry A. Springer, Susan A. Martinis, et al.. (1990). Alteration of sperm whale myoglobin heme axial ligation by site-directed mutagenesis. Biochemistry. 29(42). 9783–9791. 105 indexed citations
16.
Bellelli, Andrea, Giovanni Antonini, Maurizio Brunori, Barry A. Springer, & Stephen G. Sligar. (1990). Transient spectroscopy of the reaction of cyanide with ferrous myoglobin. Effect of distal side residues.. Journal of Biological Chemistry. 265(31). 18898–18901. 90 indexed citations
17.
Egeberg, Karen D., Barry A. Springer, Stephen G. Sligar, et al.. (1990). The role of Val68(E11) in ligand binding to sperm whale myoglobin. Site-directed mutagenesis of a synthetic gene.. Journal of Biological Chemistry. 265(20). 11788–11795. 97 indexed citations
18.
Morikis, Dimitrios, P. M. Champion, Barry A. Springer, & Stephen G. Sligar. (1989). Resonance Raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement. Biochemistry. 28(11). 4791–4800. 181 indexed citations
19.
Springer, Barry A.. (1989). Ligand discrimination and inhibition of heme iron autooxidation by myoglobin: Site-directed mutagenesis of a synthetic gene. 1 indexed citations
20.
Olson, John S., Antony J. Mathews, Ronald J. Rohlfs, et al.. (1988). The role of the distal histidine in myoglobin and haemoglobin. Nature. 336(6196). 265–266. 246 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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