Eric T. Baldwin

4.1k total citations · 1 hit paper
38 papers, 2.9k citations indexed

About

Eric T. Baldwin is a scholar working on Molecular Biology, Materials Chemistry and Infectious Diseases. According to data from OpenAlex, Eric T. Baldwin has authored 38 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 10 papers in Materials Chemistry and 7 papers in Infectious Diseases. Recurrent topics in Eric T. Baldwin's work include Enzyme Structure and Function (9 papers), Protein Structure and Dynamics (7 papers) and HIV/AIDS drug development and treatment (7 papers). Eric T. Baldwin is often cited by papers focused on Enzyme Structure and Function (9 papers), Protein Structure and Dynamics (7 papers) and HIV/AIDS drug development and treatment (7 papers). Eric T. Baldwin collaborates with scholars based in United States, Japan and Malaysia. Eric T. Baldwin's co-authors include Irene T. Weber, Alexander Wlodawer, Bangalore K. Sathyanarayana, John W. Erickson, Stephen B. H. Kent, Jens Schneider, Linda Selk, Leigh Clawson, Mariusz Jaskólski and Maria Miller and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Eric T. Baldwin

38 papers receiving 2.8k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 Protease

1989 937 citations Eric T. Baldwin, Irene T. Weber et al. profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Eric T. Baldwin United States	22	1.6k	927	869	437	383	38	2.9k
Alla Gustchina United States	37	1.7k 1.1×	684 0.7×	694 0.8×	380 0.9×	234 0.6×	94	3.2k
Bangalore K. Sathyanarayana United States	11	1.2k 0.8×	898 1.0×	804 0.9×	216 0.5×	358 0.9×	17	2.2k
Brian M. McKeever United States	24	1.4k 0.9×	731 0.8×	617 0.7×	227 0.5×	615 1.6×	46	2.5k
Youwei Yan United States	22	1.1k 0.7×	625 0.7×	521 0.6×	412 0.9×	366 1.0×	34	2.4k
Lenora J. Davis United States	18	2.1k 1.3×	1.0k 1.1×	988 1.1×	767 1.8×	238 0.6×	24	3.7k
Krzysztof Appelt United States	30	2.2k 1.4×	722 0.8×	518 0.6×	594 1.4×	733 1.9×	85	3.9k
Sergei Gulnik United States	25	1.1k 0.7×	1.1k 1.2×	1.0k 1.2×	203 0.5×	315 0.8×	49	2.5k
Maxwell D. Cummings United States	26	1.6k 1.0×	681 0.7×	263 0.3×	457 1.0×	577 1.5×	52	2.9k
Linda Selk United States	7	933 0.6×	935 1.0×	812 0.9×	149 0.3×	298 0.8×	8	1.7k
Paul L. Darke United States	34	1.4k 0.9×	1.3k 1.4×	1.1k 1.2×	206 0.5×	756 2.0×	63	2.8k

Countries citing papers authored by Eric T. Baldwin

Since Specialization

Citations

This map shows the geographic impact of Eric T. Baldwin'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 Eric T. Baldwin with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Eric T. Baldwin more than expected).

Fields of papers citing papers by Eric T. Baldwin

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eric T. Baldwin. 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 Eric T. Baldwin. The network helps show where Eric T. Baldwin may publish in the future.

Co-authorship network of co-authors of Eric T. Baldwin

This figure shows the co-authorship network connecting the top 25 collaborators of Eric T. Baldwin. A scholar is included among the top collaborators of Eric T. Baldwin 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 Eric T. Baldwin. Eric T. Baldwin is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Baldwin, Eric T., Matthias Götte, Egor P. Tchesnokov, et al.. (2022). Human endogenous retrovirus-K (HERV-K) reverse transcriptase (RT) structure and biochemistry reveals remarkable similarities to HIV-1 RT and opportunities for HERV-K–specific inhibition. Proceedings of the National Academy of Sciences. 119(27). e2200260119–e2200260119. 27 indexed citations

Matsushima, Kouji, Eric T. Baldwin, & Naofumi Mukaida. (2015). Interleukin-8 and MCAF: Novel Leukocyte Recruitment and Activating Cytokines. Chemical immunology/Fortschritte der Allergielehre/Progress in allergy/Chemical immunology and allergy. 51. 236–265. 42 indexed citations

Sivaprakasam, Prasanna, Xiaojun Han, Rita L. Civiello, et al.. (2015). Discovery of new acylaminopyridines as GSK-3 inhibitors by a structure guided in-depth exploration of chemical space around a pyrrolopyridinone core. Bioorganic & Medicinal Chemistry Letters. 25(9). 1856–1863. 100 indexed citations

Klei, Herbert E., Nigel W. Moriarty, Nathaniel Echols, et al.. (2013). Ligand placement based on prior structures: the guided ligand-replacement method. Acta Crystallographica Section D Biological Crystallography. 70(1). 134–143. 10 indexed citations

Liu, Shenping, Jeanne S. Chang, Heinz Fischer, et al.. (2011). Affinity purification of a chimeric nicotinic acetylcholine receptor in the agonist and antagonist bound states. Protein Expression and Purification. 79(1). 102–110. 2 indexed citations

Liu, Shenping, John D. Knafels, Jeanne S. Chang, et al.. (2006). Crystal Structure of the Herpes Simplex Virus 1 DNA Polymerase. Journal of Biological Chemistry. 281(26). 18193–18200. 139 indexed citations

Baldwin, Eric T., Melissa S. Harris, Anthony W. Yem, et al.. (2002). Crystal Structure of Type II Peptide Deformylase from Staphylococcus aureus. Journal of Biological Chemistry. 277(34). 31163–31171. 39 indexed citations

Sarver, Ronald W., Joseph M. Rogers, Brian J. Stockman, et al.. (2002). Physical methods to determine the binding mode of putative ligands for hepatitis C virus NS3 helicase. Analytical Biochemistry. 309(2). 186–195. 9 indexed citations

Harris, Melissa S., John T. Herberg, J. I. CIALDELLA, et al.. (2001). Crystallization and preliminary X-ray analysis of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) fromStaphylococcus aureus. Acta Crystallographica Section D Biological Crystallography. 57(7). 1032–1035. 7 indexed citations

10.

Baldwin, Eric T., Ronald W. Sarver, G. L. Bryant, et al.. (1998). Cation binding to the integrin CD11b I domain and activation model assessment. Structure. 6(7). 923–935. 61 indexed citations

11.

Tomasselli, Alfredo G., Robert Garlick, Joseph W. Leone, et al.. (1998). Recombinant Human Cytomegalovirus Protease with a C-Terminal (His)6Extension: Purification, Autocatalytic Release of the Mature Enzyme, and Biochemical Characterization. Protein Expression and Purification. 14(3). 343–352. 3 indexed citations

12.

Finzel, B.C., Eric T. Baldwin, G. L. Bryant, et al.. (1998). Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity. Protein Science. 7(10). 2118–2126. 60 indexed citations

13.

Baldwin, Eric T., Talapady N. Bhat, Sergei Gulnik, et al.. (1995). Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine. Structure. 3(6). 581–590. 127 indexed citations

14.

Bhat, Talapady N., et al.. (1995). X-Ray Structure of a Tethered Dimer for HIV-1 Protease. Advances in experimental medicine and biology. 362. 439–444. 3 indexed citations

15.

Erickson, John W., Eric T. Baldwin, Talapady N. Bhat, & Sergei Gulnik. (1995). Structure of Human Cathepsin D: Comparison of Inhibitor Binding and Subdomain Displacement with other Aspartic Proteases. Advances in experimental medicine and biology. 362. 181–192. 6 indexed citations

16.

Baldwin, Eric T., et al.. (1995). Structural basis of drug resistance for the V82A mutant of HIV-1 proteinase. Nature Structural & Molecular Biology. 2(3). 244–249. 79 indexed citations

17.

Bhat, Talapady N., et al.. (1994). Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor. Nature Structural Biology. 1(8). 552–556. 27 indexed citations

18.

Hosur, M.V., Talapady N. Bhat, Dale J. Kempf, et al.. (1994). Influence of stereochemistry on activity and binding modes for C2 symmetry-based diol inhibitors of HIV-1 protease. Journal of the American Chemical Society. 116(3). 847–855. 112 indexed citations

19.

Gulnik, Sergei, Eric T. Baldwin, Nadya I. Tarasova, & John W. Erickson. (1992). Human liver cathepsin D. Journal of Molecular Biology. 227(1). 265–270. 24 indexed citations

20.

Baldwin, Eric T., Irene T. Weber, Robert Charles, et al.. (1991). Crystal structure of interleukin 8: symbiosis of NMR and crystallography.. Proceedings of the National Academy of Sciences. 88(2). 502–506. 300 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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