József Batke

617 total citations
36 papers, 507 citations indexed

About

József Batke is a scholar working on Molecular Biology, Materials Chemistry and Clinical Biochemistry. According to data from OpenAlex, József Batke has authored 36 papers receiving a total of 507 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 13 papers in Materials Chemistry and 12 papers in Clinical Biochemistry. Recurrent topics in József Batke's work include Enzyme Structure and Function (13 papers), Metabolism and Genetic Disorders (12 papers) and Hemoglobin structure and function (9 papers). József Batke is often cited by papers focused on Enzyme Structure and Function (13 papers), Metabolism and Genetic Disorders (12 papers) and Hemoglobin structure and function (9 papers). József Batke collaborates with scholars based in Hungary, Argentina and Egypt. József Batke's co-authors include Judit Ovádi, Péter Tompa, Tamás Keleti, Mária Vas, T Keleti, Ferenc A. Bartha, Jörg Bär, G Asbóth, Bernard Schmitt and René Cohen and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Analytical Biochemistry.

In The Last Decade

József Batke

36 papers receiving 482 citations

Peers

József Batke
Constance D. Anderson United States
Blanche P. Meriwether United States
F. Seydoux France
Jane Harting Park United States
Elizabeth Heyde Australia
John S. Easterby United Kingdom
H A Lardy United States
George R. Drysdale United States
Constance D. Anderson United States
József Batke
Citations per year, relative to József Batke József Batke (= 1×) peers Constance D. Anderson

Countries citing papers authored by József Batke

Since Specialization
Citations

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

Fields of papers citing papers by József Batke

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of József Batke

This figure shows the co-authorship network connecting the top 25 collaborators of József Batke. A scholar is included among the top collaborators of József Batke 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 József Batke. József Batke 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.
Tompa, Péter, Éva Schád, Andrea Baki, et al.. (1995). An Ultrasensitive, Continuous Fluorometric Assay for Calpain Activity. Analytical Biochemistry. 228(2). 287–293. 19 indexed citations
2.
Batke, József & J. Gaál. (1993). Suicide inhibition of monoamine oxidases A and B by (−)-deprenyl. Biochemical Pharmacology. 46(4). 597–602. 3 indexed citations
3.
Batke, József, et al.. (1992). A possible in vivo mechanism of intermediate transfer by glycolytic enzyme complexes: Steady state fluorescence anisotropy analysis of an enzyme complex formation. Archives of Biochemistry and Biophysics. 296(2). 654–659. 1 indexed citations
4.
Nazaryan, Karen, et al.. (1992). Interaction of rabbit muscle enolase and 3-phosphoglycerate mutase studied by ELISA and by batch gel filtration. Archives of Biochemistry and Biophysics. 296(2). 650–653. 10 indexed citations
5.
Batke, József. (1991). Channelling by loose enzyme complexes in situ is likely, though physiological significance is open for speculation. Journal of Theoretical Biology. 152(1). 41–46. 6 indexed citations
6.
Vas, Mária & József Batke. (1990). Kinetic misinterpretation of a coupled enzyme reaction can lead to the assumption of an enzyme—enzyme interaction. European Journal of Biochemistry. 191(3). 679–683. 6 indexed citations
7.
Tompa, Péter & József Batke. (1990). Fructose-1,6-bisphosphate aldolase preferentially associates to glyceraldehyde-3-phosphate dehydrogenase in a mixture of cytosolic proteins as revealed by fluorescence energy transfer measurements.. PubMed. 20(3). 487–94. 2 indexed citations
8.
Keleti, Tamás, Judit Ovádi, & József Batke. (1989). Kinetic and physico-chemical analysis of enzyme complexes and their possible role in the control of metabolism. Progress in Biophysics and Molecular Biology. 53(2). 105–152. 48 indexed citations
9.
Batke, József. (1989). Remarks on the supramolecular organization of the glycolytic system in vivo. FEBS Letters. 251(1-2). 13–16. 16 indexed citations
10.
Batke, József. (1989). Channeling of glycolytic intermediates by temporary, stationary bi-enzyme complexes is probable in vivo. Trends in Biochemical Sciences. 14(12). 481–482. 18 indexed citations
11.
Batke, József, et al.. (1988). Complex of brain d-phosphoglycerate mutase and γ enolase and its reactivation by d-glycerate 2,3-bisphosphate. Archives of Biochemistry and Biophysics. 264(2). 510–518. 15 indexed citations
12.
Tompa, Péter, József Batke, & Judit Ovádi. (1987). How to determine the efficiency of intermediate transfer in an interacting enzyme system?. FEBS Letters. 214(2). 244–248. 17 indexed citations
13.
Bartha, Ferenc A., et al.. (1983). Change in the reactivity of the active‐site serine OH of butyrylcholinesterase caused by a new reversible inhibitor. European Journal of Biochemistry. 135(1). 157–162. 3 indexed citations
14.
Ovádi, Judit, et al.. (1983). Interaction of the Dissociable Glycerol‐3‐phosphate Dehydrogenase and Fructose‐1,6‐bisphosphate Aldolase. European Journal of Biochemistry. 133(2). 433–437. 22 indexed citations
16.
Ovádi, Judit, József Batke, Ferenc A. Bartha, & T Keleti. (1979). Effect of association-dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenase. Archives of Biochemistry and Biophysics. 193(1). 28–33. 23 indexed citations
17.
Keleti, T, József Batke, Judit Ovádi, Veronika Jancsik, & Ferenc A. Bartha. (1977). Macromolecular interactions in enzyme regulation. Advances in Enzyme Regulation. 15. 233–265. 33 indexed citations
18.
Keleti, T, Judit Ovádi, & József Batke. (1976). Catalysts and enzymes. Journal of Molecular Catalysis. 1(3). 173–200. 4 indexed citations
19.
Ovádi, Judit, et al.. (1971). Functional Non‐Identity of Subunits and Isolation of Active Dimers of d‐Glyceraldehyde‐3‐phosphate Dehydrogenase. European Journal of Biochemistry. 22(3). 430–438. 37 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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