Robert J. Brooker

1.8k total citations
51 papers, 1.6k citations indexed

About

Robert J. Brooker is a scholar working on Genetics, Materials Chemistry and Molecular Biology. According to data from OpenAlex, Robert J. Brooker has authored 51 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Genetics, 22 papers in Materials Chemistry and 21 papers in Molecular Biology. Recurrent topics in Robert J. Brooker's work include Bacterial Genetics and Biotechnology (24 papers), Enzyme Structure and Function (22 papers) and Amino Acid Enzymes and Metabolism (21 papers). Robert J. Brooker is often cited by papers focused on Bacterial Genetics and Biotechnology (24 papers), Enzyme Structure and Function (22 papers) and Amino Acid Enzymes and Metabolism (21 papers). Robert J. Brooker collaborates with scholars based in United States, France and Switzerland. Robert J. Brooker's co-authors include Carolyn W. Slayman, T. Hastings Wilson, David S. Perlin, Kunihiro Kasamo, Jeremiah C. Collins, Steve Permuth, Nanette J. Pazdernik, Kenneth K. Kídd, Ralph A. W. Lehman and Raymond C. Heimbuch and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Robert J. Brooker

51 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert J. Brooker United States 25 926 616 373 361 218 51 1.6k
Tomoya Tsukazaki Japan 21 1.5k 1.6× 782 1.3× 188 0.5× 61 0.2× 151 0.7× 46 2.1k
Helen C. Pace United States 13 1.5k 1.6× 566 0.9× 255 0.7× 104 0.3× 185 0.8× 13 1.8k
D. Travis Gallagher United States 21 925 1.0× 117 0.2× 413 1.1× 142 0.4× 110 0.5× 56 1.3k
Mohindar S. Poonian United States 22 1.1k 1.2× 399 0.6× 165 0.4× 139 0.4× 113 0.5× 36 1.5k
Alan Boyd United Kingdom 30 1.8k 1.9× 806 1.3× 75 0.2× 54 0.1× 53 0.2× 72 2.6k
Xianqiang Li China 18 1.0k 1.1× 197 0.3× 106 0.3× 152 0.4× 114 0.5× 48 1.5k
C. Alexander Valencia United States 26 1.1k 1.2× 360 0.6× 200 0.5× 53 0.1× 93 0.4× 61 1.9k
Melanie J. Dobson Canada 29 2.8k 3.0× 528 0.9× 249 0.7× 76 0.2× 110 0.5× 55 3.5k
Lisa Henry United States 15 1.4k 1.5× 373 0.6× 117 0.3× 44 0.1× 49 0.2× 17 1.9k
Daniel L. Milligan United States 18 1.1k 1.2× 482 0.8× 135 0.4× 62 0.2× 104 0.5× 24 1.6k

Countries citing papers authored by Robert J. Brooker

Since Specialization
Citations

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

Fields of papers citing papers by Robert J. Brooker

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert J. Brooker

This figure shows the co-authorship network connecting the top 25 collaborators of Robert J. Brooker. A scholar is included among the top collaborators of Robert J. Brooker 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 J. Brooker. Robert J. Brooker 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, Yufang, et al.. (2011). A facile transport assay for H+coupled membrane transport using fluorescence probes. Analytical Methods. 4(1). 44–46. 5 indexed citations
2.
Johnson, Jerry & Robert J. Brooker. (2004). Control of H+/Lactose Coupling by Ionic Interactions in the Lactose Permease ofEscherichia coli. The Journal of Membrane Biology. 198(3). 135–146. 5 indexed citations
3.
Brooker, Robert J., et al.. (2004). Importance of Conserved Acidic Residues in MntH, the Nramp homolog of Escherichia coli. The Journal of Membrane Biology. 201(2). 97–107. 39 indexed citations
4.
Johnson, Jerry, et al.. (2001). A Triple Mutant, K319N/H322Q/E325Q, of the Lactose Permease Cotransports H+ with Thiodigalactoside. The Journal of Membrane Biology. 181(3). 215–224. 11 indexed citations
5.
Brooker, Robert J., et al.. (2001). A Face on Transmembrane Segment 8 of the Lactose Permease Is Important for Transport Activity. Biochemistry. 40(40). 12220–12229. 2 indexed citations
6.
Patzlaff, Jason S., Robert J. Brooker, & Bridgette A. Barry. (2000). A Reaction-induced Fourier Transform-Infrared Spectroscopic Study of the Lactose Permease. Journal of Biological Chemistry. 275(37). 28695–28700. 3 indexed citations
7.
Anderson, Ethan J., et al.. (2000). A Revised Model for the Structure and Function of the Lactose Permease. Journal of Biological Chemistry. 275(30). 23240–23246. 17 indexed citations
8.
Pazdernik, Nanette J., et al.. (2000). Roles of Charged Residues in the Conserved Motif, G-X-X-X-D/E-R/K-X-G-[X]-R/K-R/K, of the Lactose Permease of Escherichia coli. The Journal of Membrane Biology. 174(1). 31–40. 17 indexed citations
9.
10.
Pazdernik, Nanette J., et al.. (1997). An Analysis of Suppressor Mutations Suggests That the Two Halves of the Lactose Permease Function in a Symmetrical Manner. Journal of Biological Chemistry. 272(42). 26110–26116. 21 indexed citations
11.
Brooker, Robert J., et al.. (1996). Structural Topology of Transmembrane Helix 10 in the Lactose Permease of Escherichia coli. Journal of Biological Chemistry. 271(36). 21927–21932. 6 indexed citations
12.
Brooker, Robert J., et al.. (1996). Evidence That Transmembrane Segment 2 of the Lactose Permease Is Part of a Conformationally Sensitive Interface between the Two Halves of the Protein. Journal of Biological Chemistry. 271(3). 1400–1404. 43 indexed citations
13.
Brooker, Robert J., et al.. (1995). Structural features of the uniporter/symporter/antiporter superfamily. Protein Science. 4(3). 534–537. 85 indexed citations
14.
Brooker, Robert J., et al.. (1995). The Conserved Motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in Hydrophilic Loop 2/3 of the Lactose Permease. Journal of Biological Chemistry. 270(27). 16251–16257. 111 indexed citations
15.
Brooker, Robert J., et al.. (1993). Lactose permease mutants which transport (malto)-oligosaccharides. Journal of Bacteriology. 175(19). 6269–6275. 22 indexed citations
16.
Brooker, Robert J.. (1990). The lactose permease of Escherichia coli. Research in Microbiology. 141(3). 309–315. 57 indexed citations
17.
Brooker, Robert J.. (1990). Characterization of the double mutant, Val-177/Asn-322, of the lactose permease.. Journal of Biological Chemistry. 265(7). 4155–4160. 32 indexed citations
18.
Brooker, Robert J., et al.. (1989). Isolation and Characterization of Thiodigalactoside-resistant Mutants of the Lactose Permease Which Possess an Enhanced Recognition for Maltose. Journal of Biological Chemistry. 264(27). 15988–15992. 30 indexed citations
19.
Menick, Donald R., Jonathan A. Lee, Robert J. Brooker, T. Hastings Wilson, & H. Ronald Kaback. (1987). Role of cysteine residues in the lac permease of Escherichia coli. Biochemistry. 26(4). 1132–1136. 48 indexed citations
20.
Brooker, Robert J. & T. Hastings Wilson. (1985). Isolation, Characterization, and Nucleotide Sequences of Lactose Permease Mutants That Have Acquired the Ability to Transport Maltose. Annals of the New York Academy of Sciences. 456(1). 350–350. 4 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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