Robert A. Aldape

2.6k total citations · 1 hit paper
13 papers, 2.3k citations indexed

About

Robert A. Aldape is a scholar working on Molecular Biology, Immunology and Oncology. According to data from OpenAlex, Robert A. Aldape has authored 13 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 8 papers in Immunology and 6 papers in Oncology. Recurrent topics in Robert A. Aldape's work include Signaling Pathways in Disease (6 papers), Toxin Mechanisms and Immunotoxins (6 papers) and Peptidase Inhibition and Analysis (4 papers). Robert A. Aldape is often cited by papers focused on Signaling Pathways in Disease (6 papers), Toxin Mechanisms and Immunotoxins (6 papers) and Peptidase Inhibition and Analysis (4 papers). Robert A. Aldape collaborates with scholars based in United States, United Kingdom and Belgium. Robert A. Aldape's co-authors include David J. Livingston, Mark A. Murcko, John A. Thomson, Manuel A. Navia, Stephen P. Chambers, Scott A. Raybuck, Eunice E. Kim, James P. Griffith, Keith P. Wilson and Olga Futer and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Robert A. Aldape

13 papers receiving 2.2k 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.

Structure and mechanism of interleukin-lβ converting enzyme

1994 705 citations Keith P. Wilson, John A. Thomson et al. Nature profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Robert A. Aldape United States	12	1.7k	535	370	355	177	13	2.3k
Michael G. Mulkerrin United States	18	1.6k 1.0×	569 1.1×	315 0.9×	159 0.4×	101 0.6×	24	2.7k
T. R. Breitman United States	22	3.0k 1.8×	626 1.2×	396 1.1×	955 2.7×	228 1.3×	52	3.8k
Rodger A. Allen United States	26	1.2k 0.7×	1.0k 1.9×	219 0.6×	165 0.5×	221 1.2×	43	2.3k
William Scher United States	19	1.5k 0.9×	236 0.4×	323 0.9×	328 0.9×	197 1.1×	45	2.4k
Sandra S. Zinkel United States	20	2.2k 1.3×	424 0.8×	441 1.2×	177 0.5×	232 1.3×	34	2.8k
Barbara Wolff Austria	18	2.5k 1.5×	521 1.0×	442 1.2×	102 0.3×	293 1.7×	30	3.3k
Patricia M. Cameron United States	26	1.3k 0.8×	1.2k 2.3×	535 1.4×	172 0.5×	127 0.7×	36	2.8k
Jon D. Shuman United States	20	1.4k 0.9×	405 0.8×	311 0.8×	104 0.3×	185 1.0×	26	2.1k
Dale A. Cumming Canada	24	1.8k 1.1×	764 1.4×	286 0.8×	275 0.8×	333 1.9×	32	2.9k
Barbara J. Brandhuber United States	25	1.7k 1.0×	1.0k 1.9×	579 1.6×	130 0.4×	115 0.6×	37	3.0k

Countries citing papers authored by Robert A. Aldape

Since Specialization

Citations

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

Fields of papers citing papers by Robert A. Aldape

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert A. Aldape

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

All Works

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13 of 13 papers shown

Bellon, Steven F., Jonathan D. Parsons, Yunyi Wei, et al.. (2004). Crystal Structures of Escherichia coli Topoisomerase IV ParE Subunit (24 and 43 Kilodaltons): a Single Residue Dictates Differences in Novobiocin Potency against Topoisomerase IV and DNA Gyrase. Antimicrobial Agents and Chemotherapy. 48(5). 1856–1864. 124 indexed citations

Cameron, Andrew M., Frederick C. Nucifora, Eric T. Fung, et al.. (1997). FKBP12 Binds the Inositol 1,4,5-Trisphosphate Receptor at Leucine-Proline (1400–1401) and Anchors Calcineurin to this FK506-like Domain. Journal of Biological Chemistry. 272(44). 27582–27588. 184 indexed citations

DeCenzo, Maureen T., et al.. (1996). FK506-binding protein mutational analysis: defining the active-site residue contributions to catalysis and the stability of ligand complexes. Protein Engineering Design and Selection. 9(2). 173–180. 70 indexed citations

Gu, Yong, et al.. (1995). Cleavage of Poly(ADP-ribose) Polymerase by Interleukin-1β Converting Enzyme and Its Homologs TX and Nedd-2. Journal of Biological Chemistry. 270(32). 18715–18718. 145 indexed citations

Futer, Olga, Maureen T. DeCenzo, Robert A. Aldape, & David J. Livingston. (1995). FK506 Binding Protein Mutational Analysis. Journal of Biological Chemistry. 270(32). 18935–18940. 51 indexed citations

Faucheu, Chi, Anita Diu, A. W. Edith Chan, et al.. (1995). A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells.. The EMBO Journal. 14(9). 1914–1922. 285 indexed citations

Wilson, Keith P., John A. Thomson, Eunice E. Kim, et al.. (1994). Structure and mechanism of interleukin-lβ converting enzyme. Nature. 370(6487). 270–275. 705 indexed citations breakdown →

Connelly, Patrick R., Robert A. Aldape, Frank J. Bruzzese, et al.. (1994). Enthalpy of hydrogen bond formation in aprotein-ligand binding reaction.. Proceedings of the National Academy of Sciences. 91(5). 1964–1968. 111 indexed citations

Park, So‐Hyun, Robert A. Aldape, Olga Futer, Maureen T. DeCenzo, & David J. Livingston. (1992). PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism.. Journal of Biological Chemistry. 267(5). 3316–3324. 89 indexed citations

10.

Aldape, Robert A., et al.. (1992). Charged surface residues of FKBP12 participate in formation of the FKBP12-FK506-calcineurin complex.. Journal of Biological Chemistry. 267(23). 16029–16032. 116 indexed citations

11.

Hill, David E., Robert A. Aldape, & J. David Rozzell. (1990). Nucleotide sequence of a cyclodextrin glucosyltransferasse gene,cgtA, fromBacillus licheniformis. Nucleic Acids Research. 18(1). 199–199. 28 indexed citations

12.

Katan, Matilda, Ronald Kriz, Nicholas F. Totty, et al.. (1988). Primary Structure of PLC-154. Cold Spring Harbor Symposia on Quantitative Biology. 53(0). 921–926. 6 indexed citations

13.

Jenny, Richard J., Debra D. Pittman, J J Toole, et al.. (1987). Complete cDNA and derived amino acid sequence of human factor V.. Proceedings of the National Academy of Sciences. 84(14). 4846–4850. 338 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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