R Rosa

1.3k total citations
60 papers, 1.0k citations indexed

About

R Rosa is a scholar working on Physiology, Molecular Biology and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, R Rosa has authored 60 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Physiology, 21 papers in Molecular Biology and 11 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in R Rosa's work include Erythrocyte Function and Pathophysiology (34 papers), Neonatal Health and Biochemistry (11 papers) and Amino Acid Enzymes and Metabolism (9 papers). R Rosa is often cited by papers focused on Erythrocyte Function and Pathophysiology (34 papers), Neonatal Health and Biochemistry (11 papers) and Amino Acid Enzymes and Metabolism (9 papers). R Rosa collaborates with scholars based in France, United States and Spain. R Rosa's co-authors include J. Rosa, Marie‐Odette Préhu, Jean Rosa, Isabelle Max‐Audit, M. Calvin, Yves Beuzard, EF Jr Roth, V. Joulin, Martine Cohen‐Solal and Y. Blouquit and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Clinical Investigation.

In The Last Decade

R Rosa

60 papers receiving 982 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
R Rosa France 19 450 407 203 178 143 60 1.0k
Jean Rosa France 17 271 0.6× 390 1.0× 198 1.0× 280 1.6× 45 0.3× 52 909
Michael N. Blackburn United States 15 121 0.3× 326 0.8× 48 0.2× 52 0.3× 131 0.9× 18 707
N. Arous France 18 208 0.5× 264 0.6× 152 0.7× 430 2.4× 33 0.2× 60 933
Yu Fukuda United States 18 89 0.2× 601 1.5× 130 0.6× 135 0.8× 30 0.2× 28 1.1k
Joseph R. Shaeffer United States 19 176 0.4× 426 1.0× 107 0.5× 323 1.8× 24 0.2× 43 852
F.W. Verheijen Netherlands 19 413 0.9× 391 1.0× 140 0.7× 13 0.1× 31 0.2× 30 878
Richard L. Boriack United States 17 184 0.4× 536 1.3× 56 0.3× 43 0.2× 22 0.2× 32 828
E. A. Kvittingen Norway 19 124 0.3× 435 1.1× 78 0.4× 16 0.1× 40 0.3× 33 945
M.J. McDonald United States 13 260 0.6× 299 0.7× 195 1.0× 232 1.3× 25 0.2× 26 834
David Kakhniashvili United States 15 479 1.1× 419 1.0× 76 0.4× 121 0.7× 9 0.1× 40 1.0k

Countries citing papers authored by R Rosa

Since Specialization
Citations

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

Fields of papers citing papers by R Rosa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of R Rosa

This figure shows the co-authorship network connecting the top 25 collaborators of R Rosa. A scholar is included among the top collaborators of R Rosa 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 R Rosa. R Rosa 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.
Schneider, Arthur S., Beryl Westwood, Michel Cohen‐Solal, et al.. (1996). The 1591C Mutation in Triosephosphate Isomerase (TPI) Deficiency. Tightly Linked Polymorphisms and a Common Haplotype in All Known Families. Blood Cells Molecules and Diseases. 22(2). 115–125. 13 indexed citations
4.
Lemarchandel, Valérie, M. Calvin, N. Arous, et al.. (1993). Amino acid residues involved in the catalytic site of human erythrocyte bisphosphoglycerate mutase. European Journal of Biochemistry. 213(1). 493–500. 11 indexed citations
5.
Schaad, Olivier, et al.. (1992). Structural modeling of the human erythrocyte bisphosphoglycerate mutase. Biochimie. 74(6). 519–526. 5 indexed citations
6.
Cherfils, Jacqueline, et al.. (1991). Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase. Journal of Molecular Biology. 218(2). 269–270. 6 indexed citations
7.
Ojcius, David M., Philippe Leboulch, V. Joulin, et al.. (1990). Isolation and characterization of the gene encoding the muscle-specific isozyme of human phosphoglycerate mutase. Gene. 91(2). 225–232. 24 indexed citations
8.
Calvin, M., Y. Blouquit, M.C. Garel, et al.. (1990). Human bisphosphoglycerate mutase expressed in E coli: purification, characterization and structure studies. Biochimie. 72(5). 337–343. 9 indexed citations
11.
Préhu, Marie‐Odette, Claude Préhu, M. Calvin, & R Rosa. (1988). Rabbit M type phosphoglycermutase: comparative effects of two thiol reagents, antibody reaction and hybridization studies. Comparative Biochemistry and Physiology Part B Comparative Biochemistry. 89(2). 257–262. 3 indexed citations
12.
Rosa, R & M. Calvin. (1988). Comparative effects of two sulfhydryl reagents on the activities of a multifunctional red cell enzyme: Bisphosphoglycerate mutase. Biochemical and Biophysical Research Communications. 153(3). 945–951. 4 indexed citations
13.
Roth, EF Jr, et al.. (1988). The use of enzymopathic human red cells in the study of malarial parasite glucose metabolism. Blood. 71(5). 1408–1413. 2 indexed citations
14.
Max‐Audit, Isabelle, et al.. (1988). Pyruvate kinase synthesis and degradation by normal and pathologic cells during erythroid maturation. Blood. 72(3). 1039–1044. 13 indexed citations
15.
Max‐Audit, Isabelle, et al.. (1988). Pyruvate kinase synthesis and degradation by normal and pathologic cells during erythroid maturation. Blood. 72(3). 1039–1044. 13 indexed citations
16.
Barichard, F., V. Joulin, Isabelle Henry, et al.. (1987). Chromosomal assignment of the human 2,3-bisphosphoglycerate mutase gene (BPGM) to region 7q34→7q22. Human Genetics. 77(3). 283–285. 14 indexed citations
17.
Rosa, R, et al.. (1984). Evidence for the presence of a hybrid of phosphoglyceromutase/bisphosphoglyceromutase in the red cells: Partial characterization of the hybrid. Biochemical and Biophysical Research Communications. 120(3). 715–720. 10 indexed citations
18.
Galactéros, Frederic, et al.. (1984). [Diphosphoglyceromutase deficiency: new cases associated with erythrocytosis].. PubMed. 26(2). 69–74. 18 indexed citations
19.
Rosa, R, et al.. (1983). Partial characterization of the inactive mutant form of human red cell bisphosphoglyceromutase and comparison with an alkylated form. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 742(1). 243–249. 17 indexed citations
20.
Rosa, R, Isabelle Max‐Audit, V. Izraël, et al.. (1981). Hereditary pyruvate kinase abnormalities associated with erythrocytosis. American Journal of Hematology. 10(1). 47–55. 13 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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