G F Ames

4.6k total citations
48 papers, 4.0k citations indexed

About

G F Ames is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, G F Ames has authored 48 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 28 papers in Genetics and 17 papers in Materials Chemistry. Recurrent topics in G F Ames's work include Bacterial Genetics and Biotechnology (26 papers), Enzyme Structure and Function (17 papers) and RNA and protein synthesis mechanisms (13 papers). G F Ames is often cited by papers focused on Bacterial Genetics and Biotechnology (26 papers), Enzyme Structure and Function (17 papers) and RNA and protein synthesis mechanisms (13 papers). G F Ames collaborates with scholars based in United States, South Korea and United Kingdom. G F Ames's co-authors include Kishiko Nikaido, Venkatakrishna Shyamala, Carol Mimura, Sydney Kustu, Catherine A. Prody, S H Kim, Chris Higgins, Feroza Ardeshir, Byung‐Ha Oh and Christopher F. Higgins and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

G F Ames

48 papers receiving 3.8k citations

Peers

G F Ames
Kishiko Nikaido United States
Robert J. Kadner United States
C R Raetz United States
Christopher F. Higgins United Kingdom
K. Brooks Low United States
Richard A. Zakour United States
B Bachmann Germany
W. Dean Rupp United States
G F Ames
Citations per year, relative to G F Ames G F Ames (= 1×) peers Giovanna Ferro‐Luzzi Ames

Countries citing papers authored by G F Ames

Since Specialization
Citations

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

Fields of papers citing papers by G F Ames

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by G F Ames. 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 G F Ames. The network helps show where G F Ames may publish in the future.

Co-authorship network of co-authors of G F Ames

This figure shows the co-authorship network connecting the top 25 collaborators of G F Ames. A scholar is included among the top collaborators of G F Ames 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 G F Ames. G F Ames 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.
Ames, G F. (1994). [18] Isolation and purification of periplasmic binding proteins. Methods in enzymology on CD-ROM/Methods in enzymology. 235. 234–241. 9 indexed citations
2.
Nikaido, Kishiko, et al.. (1994). The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies.. Journal of Biological Chemistry. 269(37). 23051–23058. 36 indexed citations
3.
Oh, Byung‐Ha, ChulHee Kang, S H Kim, et al.. (1994). The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins.. Journal of Biological Chemistry. 269(6). 4135–4143. 89 indexed citations
4.
Shyamala, Venkatakrishna & G F Ames. (1993). [32] Genome walking by single specific primer-polymerase chain reaction. Methods in enzymology on CD-ROM/Methods in enzymology. 217. 436–446. 49 indexed citations
5.
Ames, G F, et al.. (1992). Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family.. Journal of Biological Chemistry. 267(4). 2329–2336. 99 indexed citations
6.
Petronilli, Valeria & G F Ames. (1991). Binding protein-independent histidine permease mutants. Uncoupling of ATP hydrolysis from transmembrane signaling.. Journal of Biological Chemistry. 266(25). 16293–16296. 72 indexed citations
7.
Speiser, David M. & G F Ames. (1991). Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins. Journal of Bacteriology. 173(4). 1444–1451. 58 indexed citations
8.
Kang, ChulHee, et al.. (1991). Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-A resolution.. Journal of Biological Chemistry. 266(35). 23893–23899. 77 indexed citations
9.
Ames, G F. (1990). Energy coupling in periplasmic permeases: The histidine permease as a model system. Research in Microbiology. 141(3). 341–348. 17 indexed citations
10.
Mimura, Carol, et al.. (1990). The nucleotide-binding site of HisP, a membrane protein of the histidine permease. Identification of amino acid residues photoaffinity labeled by 8-azido-ATP.. Journal of Biological Chemistry. 265(32). 19535–19542. 29 indexed citations
11.
Ames, G F & Anil K. Joshi. (1990). Energy coupling in bacterial periplasmic permeases. Journal of Bacteriology. 172(8). 4133–4137. 75 indexed citations
12.
Ames, G F, et al.. (1989). Reconstitution of periplasmic transport in inside-out membrane vesicles. Journal of Biological Chemistry. 264(7). 3998–4002. 63 indexed citations
13.
Stern, Michael, Eric R. Prossnitz, & G F Ames. (1988). Role of the intercistronic region in post‐transcriptional control of gene expression in the histidine transport operon of Salmonella typhimurium: involvement of REP sequences. Molecular Microbiology. 2(1). 141–152. 60 indexed citations
14.
Prossnitz, Eric R., et al.. (1988). Formaldehyde and photoactivatable cross-linking of the periplasmic binding protein to a membrane component of the histidine transport system of Salmonella typhimurium.. Journal of Biological Chemistry. 263(34). 17917–17920. 72 indexed citations
15.
Ames, G F & Kishiko Nikaido. (1985). Nitrogen regulation in Salmonella typhimurium. Identification of an ntrC protein-binding site and definition of a consensus binding sequence.. The EMBO Journal. 4(2). 539–547. 107 indexed citations
16.
Hobson, A C, et al.. (1984). ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system.. Proceedings of the National Academy of Sciences. 81(23). 7333–7337. 127 indexed citations
17.
Ames, G F, Catherine A. Prody, & Sydney Kustu. (1984). Simple, rapid, and quantitative release of periplasmic proteins by chloroform. Journal of Bacteriology. 160(3). 1181–1183. 312 indexed citations
18.
Higgins, Chris & G F Ames. (1982). Regulatory regions of two transport operons under nitrogen control: nucleotide sequences.. Proceedings of the National Academy of Sciences. 79(4). 1083–1087. 45 indexed citations
19.
Gilson, Éric, Chris Higgins, Maurice Hofnung, G F Ames, & Hiroshi Nikaido. (1982). Extensive homology between membrane-associated components of histidine and maltose transport systems of Salmonella typhimurium and Escherichia coli.. Journal of Biological Chemistry. 257(17). 9915–9918. 56 indexed citations
20.
Ames, G F, et al.. (1979). In vivo methylation of prokaryotic elongation factor Tu.. Journal of Biological Chemistry. 254(20). 9947–9950. 34 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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