J. Kister

2.1k total citations
107 papers, 1.7k citations indexed

About

J. Kister is a scholar working on Cell Biology, Genetics and Physiology. According to data from OpenAlex, J. Kister has authored 107 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 94 papers in Cell Biology, 63 papers in Genetics and 57 papers in Physiology. Recurrent topics in J. Kister's work include Hemoglobin structure and function (94 papers), Hemoglobinopathies and Related Disorders (63 papers) and Erythrocyte Function and Pathophysiology (55 papers). J. Kister is often cited by papers focused on Hemoglobin structure and function (94 papers), Hemoglobinopathies and Related Disorders (63 papers) and Erythrocyte Function and Pathophysiology (55 papers). J. Kister collaborates with scholars based in France, United States and Greece. J. Kister's co-authors include Claire Poyart, B. Bohn, Henri Wajcman, M.C. Marden, Stuart J. Edelstein, Frédéric Galactéros, M. F. Perutz, G. Fermi, J. Pagnier and Michael C. Marden and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Blood.

In The Last Decade

J. Kister

107 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J. Kister France 21 1.1k 849 569 541 393 107 1.7k
R Benesch United States 18 1.0k 0.9× 432 0.5× 433 0.8× 500 0.9× 494 1.3× 29 1.4k
Clara Fronticelli United States 26 2.0k 1.7× 598 0.7× 1.2k 2.2× 741 1.4× 806 2.1× 95 2.5k
P.H. Rogers United States 24 1.1k 1.0× 345 0.4× 942 1.7× 628 1.2× 388 1.0× 33 1.9k
L. Rossi-Bernardi Italy 24 1.2k 1.1× 295 0.3× 812 1.4× 603 1.1× 450 1.1× 55 1.8k
Robert M. Bookchin United States 33 945 0.8× 1.9k 2.2× 998 1.8× 1.8k 3.3× 723 1.8× 72 3.3k
Suzanna Kwong United States 18 517 0.4× 416 0.5× 265 0.5× 283 0.5× 194 0.5× 32 818
Winston F. Moo-Penn United States 18 569 0.5× 528 0.6× 326 0.6× 244 0.5× 247 0.6× 59 956
B. Bohn France 16 659 0.6× 257 0.3× 343 0.6× 286 0.5× 207 0.5× 38 835
Itiro Tyuma Japan 21 1.1k 1.0× 221 0.3× 590 1.0× 590 1.1× 386 1.0× 46 1.4k
M.C. Garel France 16 303 0.3× 390 0.5× 263 0.5× 283 0.5× 128 0.3× 28 738

Countries citing papers authored by J. Kister

Since Specialization
Citations

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

Fields of papers citing papers by J. Kister

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J. Kister

This figure shows the co-authorship network connecting the top 25 collaborators of J. Kister. A scholar is included among the top collaborators of J. Kister 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 J. Kister. J. Kister 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.
Kister, J. & Henri Wajcman. (2003). Oxygen Equilibrium Measurements of Human Red Blood Cells. Humana Press eBooks. 82. 49–64. 7 indexed citations
2.
Préhu, Claude, et al.. (2003). A new Unstable α2‐Globin Gene Variant: Hb Chartres [α33(B14)Phe→Ser]. Hemoglobin. 27(2). 111–115. 7 indexed citations
3.
Groff, Paolo, Barbara Golińska, Ai Miyazaki, et al.. (2000). Hb Ernz Iβ123(Hl)Thr→Asn] and Hb Renert Iβ133(H1l)Val →Ala]: Two new Neutral Variants Revealed by Reversed Phase High Performance Liquid Chromatography Analysis. Hemoglobin. 24(4). 287–297. 20 indexed citations
4.
Wajcman, Henri, Joan Henthorn, J. Kister, et al.. (2000). Two new Variants with the Same Substitution at Position β122: Hb Bushey [β122(GHS)Phe→Leu] and Hb Casablanca [β65(E9)Lys→Met;β122(GHS)Phe→Leu]. Hemoglobin. 24(2). 125–132. 5 indexed citations
5.
Wajcman, Henri, J. Riou, Danièlle Promé, J. Kister, & Frédéric Galactéros. (1999). Hb Brie Comte Robert [β36(C2)Pro→Ala]: A New Hemoglobin Variant with High Oxygen Affinity and Marked Hydrophobic Properties. Hemoglobin. 23(3). 281–286. 3 indexed citations
6.
Badens, Catherine, Danielle Lena‐Russo, Alain Francina, et al.. (1999). Hb Toulon [α77(EF6)Pro→His]: a New Variant Due to a Mutation in the α2 Gene Found During Measurement of Glycated Hemoglobin. Hemoglobin. 23(4). 367–371. 6 indexed citations
7.
8.
Boyiri, Telih, et al.. (1995). Bisaldehyde Allosteric Effectors as Molecular Ratchets and Probes. Biochemistry. 34(46). 15021–15036. 29 indexed citations
9.
Samain, D., et al.. (1995). Conception et développement d'une nouvelle génération de transporteur d'oxygène. Transfusion Clinique et Biologique. 2(6). 449–452. 1 indexed citations
10.
Poyart, Claire, Michael C. Marden, & J. Kister. (1994). [24] Bezafibrate derivatives as potent effectors of hemoglobin. Methods in enzymology on CD-ROM/Methods in enzymology. 232. 496–513. 20 indexed citations
11.
Baudin, V., M.-T. Bihoreau, J. Kister, et al.. (1994). Functional Properties of β(NA1)Val-Deleted, (NA2)His→Met Hemoglobin Synthesized inEscherichia Coli.. Artificial Cells Blood Substitutes and Biotechnology. 22(3). 739–745. 2 indexed citations
12.
Wajcman, Henri, J. Kister, Danièlle Promé, Frédéric Galactéros, & Florinda Gilsanz. (1993). Hb Villaverde [β 89 (F5) Ser → Thr]: the structural modification of an intrasubunit contact is responsible for a high oxygen affinity. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1225(1). 89–94. 3 indexed citations
13.
Wajcman, Henri, J. Kister, Danièlle Promé, et al.. (1993). Hb Saint Nazaire (β103[G5]Phe→Ile): A new example of polycythemia due to a hemoglobin variant with increased oxygen affinity. American Journal of Hematology. 44(1). 16–21. 15 indexed citations
14.
Wajcman, Henri, J. Kister, M.C. Marden, et al.. (1992). Homoglobin Rouen (α-140 (HC2) Tyr→His): alteration of the α-chain C-terminal region and moderate increase in oxygen affinity. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1180(1). 53–57. 10 indexed citations
15.
Poyart, Claire, Olivier Schaad, J. Kister, et al.. (1990). Hemoglobin Saint Mandé [β102 (G4) Asn→Tyr]. European Journal of Biochemistry. 194(2). 343–348. 7 indexed citations
16.
Lalezari, I., Parviz Lalezari, Claire Poyart, et al.. (1990). New effectors of human hemoglobin: structure and function. Biochemistry. 29(6). 1515–1523. 109 indexed citations
17.
Marden, M.C., J. Kister, Claire Poyart, & Stuart J. Edelstein. (1989). Analysis of hemoglobin oxygen equilibrium curves are unique solutions possible?. Journal of Molecular Biology. 208(2). 341–345. 19 indexed citations
18.
Kister, J., et al.. (1989). Analysis of oxygen binding byXenopus laevis hemoglobin: implications for the Root effect. Respiration Physiology. 76(2). 191–203. 2 indexed citations
19.
Marden, M.C., J. Kister, B. Bohn, & Claire Poyart. (1988). T-state hemoglobin with four ligands bound. Biochemistry. 27(5). 1659–1664. 82 indexed citations
20.
Bardakdjian, J., J. Kister, M.C. Marden, et al.. (1988). HB J-Cordoba [α2Aβ295 (FG2)LYS →MET] A New HB Variant Found in Argentina. Hemoglobin. 12(1). 1–11. 8 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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