Ann Ginsburg

4.0k total citations
88 papers, 3.3k citations indexed

About

Ann Ginsburg is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Ann Ginsburg has authored 88 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 53 papers in Molecular Biology, 46 papers in Materials Chemistry and 32 papers in Biochemistry. Recurrent topics in Ann Ginsburg's work include Enzyme Structure and Function (46 papers), Amino Acid Enzymes and Metabolism (32 papers) and Protein Structure and Dynamics (19 papers). Ann Ginsburg is often cited by papers focused on Enzyme Structure and Function (46 papers), Amino Acid Enzymes and Metabolism (32 papers) and Protein Structure and Dynamics (19 papers). Ann Ginsburg collaborates with scholars based in United States, France and Italy. Ann Ginsburg's co-authors include John B. Hunt, Michael R. Maurizi, Bennett M. Shapiro, Sue H. Neece, H. K. Schachman, Earl R. Stadtman, S. Hennig, M. D. Denton, Jen Jen Yeh and Alan H. Mehler and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Annual Review of Biochemistry.

In The Last Decade

Ann Ginsburg

88 papers receiving 2.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ann Ginsburg United States 31 2.1k 1.2k 901 484 322 88 3.3k
Richard B. Honzatko United States 36 3.3k 1.5× 1.3k 1.2× 646 0.7× 438 0.9× 307 1.0× 109 4.7k
Florence Lederer France 33 3.3k 1.6× 653 0.6× 622 0.7× 582 1.2× 246 0.8× 145 4.2k
Guy Branlant France 36 3.0k 1.4× 886 0.8× 710 0.8× 478 1.0× 350 1.1× 121 3.7k
James K Stoops United States 30 2.4k 1.1× 517 0.4× 611 0.7× 419 0.9× 313 1.0× 67 3.4k
Jack F. Kirsch United States 41 4.1k 1.9× 1.7k 1.4× 1.2k 1.4× 287 0.6× 289 0.9× 145 5.8k
J. John Holbrook United Kingdom 40 3.7k 1.7× 1.9k 1.6× 873 1.0× 809 1.7× 349 1.1× 138 4.8k
Mary Ellen Jones United States 36 2.6k 1.2× 739 0.6× 689 0.8× 499 1.0× 659 2.0× 77 3.6k
S G Waley United Kingdom 40 2.8k 1.3× 756 0.7× 369 0.4× 428 0.9× 212 0.7× 109 5.0k
J. Ieuan Harris United Kingdom 39 3.4k 1.6× 1.1k 1.0× 429 0.5× 888 1.8× 494 1.5× 85 5.4k
Juris Ozols United States 40 2.3k 1.1× 230 0.2× 609 0.7× 698 1.4× 296 0.9× 95 4.2k

Countries citing papers authored by Ann Ginsburg

Since Specialization
Citations

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

Fields of papers citing papers by Ann Ginsburg

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ann Ginsburg. 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 Ann Ginsburg. The network helps show where Ann Ginsburg may publish in the future.

Co-authorship network of co-authors of Ann Ginsburg

This figure shows the co-authorship network connecting the top 25 collaborators of Ann Ginsburg. A scholar is included among the top collaborators of Ann Ginsburg 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 Ann Ginsburg. Ann Ginsburg 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.
Fodor, Elfrieda & Ann Ginsburg. (2006). Specific DNA binding by the homeodomain Nkx2.5(C56S): Detection of impaired DNA or unfolded protein by isothermal titration calorimetry. Proteins Structure Function and Bioinformatics. 64(1). 13–18. 2 indexed citations
2.
Piszczek, Grzegorz, Jan Różycki, Satyendra Kumar Singh, Ann Ginsburg, & Michael R. Maurizi. (2005). The Molecular Chaperone, ClpA, Has a Single High Affinity Peptide Binding Site per Hexamer. Journal of Biological Chemistry. 280(13). 12221–12230. 27 indexed citations
3.
Remmert, Kirsten, et al.. (2004). CARMIL Is a Bona Fide Capping Protein Interactant. Journal of Biological Chemistry. 279(4). 3068–3077. 29 indexed citations
4.
Dimitrova, Mariana N., Alan Peterkofsky, & Ann Ginsburg. (2003). Opposing effects of phosphoenolpyruvate and pyruvate with Mg2+ on the conformational stability and dimerization of phosphotransferase enzyme I from Escherichia coli. Protein Science. 12(9). 2047–2056. 13 indexed citations
5.
Ginsburg, Ann & Alan Peterkofsky. (2002). Enzyme I: The Gateway to the Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System. Archives of Biochemistry and Biophysics. 397(2). 273–278. 32 indexed citations
6.
Kwon, Ki‐Sun, et al.. (1999). Molecular Cloning and Characterization of a Mitochondrial Selenocysteine-containing Thioredoxin Reductase from Rat Liver. Journal of Biological Chemistry. 274(8). 4722–4734. 226 indexed citations
7.
Nosworthy, Neil J., Alan Peterkofsky, Simone König, et al.. (1998). Phosphorylation Destabilizes the Amino-Terminal Domain of Enzyme I of the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System. Biochemistry. 37(19). 6718–6726. 31 indexed citations
8.
Žółkiewski, Michal, Maria Jolanta Rędowicz, Edward D. Korn, & Ann Ginsburg. (1996). Thermal unfolding of Acanthamoeba myosin II and skeletal muscle myosin. Biophysical Chemistry. 59(3). 365–371. 9 indexed citations
9.
Žółkiewski, Michal, Neil J. Nosworthy, & Ann Ginsburg. (1995). Urea‐induced dissociation and unfolding of dodecameric glutamine synthetase from escherichia coli: Calorimetric and spectral studies. Protein Science. 4(8). 1544–1552. 9 indexed citations
10.
Maurizi, Michael R., Harold B. Pinkofsky, & Ann Ginsburg. (1987). ADP, chloride ion, and metal ion binding to bovine brain glutamine synthetase. Biochemistry. 26(16). 5023–5031. 24 indexed citations
11.
Ginsburg, Ann, et al.. (1987). Thermodynamics of active-site ligand binding to Escherichia coli glutamine synthetase. Biochemistry. 26(19). 5989–5996. 12 indexed citations
12.
Levine, Rodney L. & Ann Ginsburg. (1985). Modulation by molecular interactions. Academic Press eBooks. 3 indexed citations
13.
Maurizi, Michael R. & Ann Ginsburg. (1982). Active site ligand stabilization of quaternary structures of glutamine synthetase from Escherichia coli.. Journal of Biological Chemistry. 257(12). 7246–7251. 31 indexed citations
14.
Shrake, Andrew, Ann Ginsburg, Frederick C. Wedler, & Yuichi Sugiyama. (1982). On the binding of L-S- and L-R-diastereoisomers of the substrate analog L-methionine sulfoximine to glutamine synthetase from Escherichia coli.. Journal of Biological Chemistry. 257(14). 8238–8243. 15 indexed citations
15.
Whitley, Edward & Ann Ginsburg. (1978). A spectral probe near the subunit catalytic site of glutamine synthetase from Escherichia coli. Reduced pyridoxal 5'-phosphate.enzyme complexes.. Journal of Biological Chemistry. 253(19). 7017–7025. 8 indexed citations
16.
Zopf, David A., Ann Ginsburg, & Victor Ginsburg. (1975). Goat Antibody Directed Against a Human Leb Blood Group Hapten, Lacto-N-Difucohexaose I. The Journal of Immunology. 115(6). 1525–1529. 21 indexed citations
17.
Stadtman, Earl R., Ann Ginsburg, J.E. Ciardi, et al.. (1970). Multiple molecular forms of glutamine synthetase produced by enzyme catalyzed adenylylation and deadenylylation reactions. Advances in Enzyme Regulation. 8. 99–118. 170 indexed citations
18.
Ross, Philip D. & Ann Ginsburg. (1969). Calorimetric study of the binding of two feedback inhibitors to the glutamine synthetase from Escherichia coli. Biochemistry. 8(12). 4690–4695. 15 indexed citations
19.
Ginsburg, Ann & William R. Carroll. (1965). Some Specific Ion Effects on the Conformation and Thermal Stability of Ribonuclease*. Biochemistry. 4(10). 2159–2174. 100 indexed citations
20.
Ginsburg, Ann & H. K. Schachman. (1960). Studies on the Enzymatic Breakdown of Proteins. Journal of Biological Chemistry. 235(1). 115–123. 16 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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