Zelda B. Rose

1.3k total citations
26 papers, 1.1k citations indexed

About

Zelda B. Rose is a scholar working on Molecular Biology, Physiology and Biochemistry. According to data from OpenAlex, Zelda B. Rose has authored 26 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 9 papers in Physiology and 9 papers in Biochemistry. Recurrent topics in Zelda B. Rose's work include Amino Acid Enzymes and Metabolism (9 papers), Erythrocyte Function and Pathophysiology (8 papers) and Cancer, Hypoxia, and Metabolism (7 papers). Zelda B. Rose is often cited by papers focused on Amino Acid Enzymes and Metabolism (9 papers), Erythrocyte Function and Pathophysiology (8 papers) and Cancer, Hypoxia, and Metabolism (7 papers). Zelda B. Rose collaborates with scholars based in United States. Zelda B. Rose's co-authors include Naotaka Hamasaki, Robert G. Whalen, Raj K. Gupta, W.D. Yushok, Pratima Gupta, E. Racker, Syamalima Dube, John Salon, G.S. Kaklij and Raj K. Gupta and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Analytical Biochemistry.

In The Last Decade

Zelda B. Rose

26 papers receiving 989 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Zelda B. Rose United States 17 506 383 356 207 192 26 1.1k
Z.B. Rose United States 12 336 0.7× 199 0.5× 187 0.5× 121 0.6× 103 0.5× 12 728
Edward L. O'Connell United States 18 860 1.7× 411 1.1× 233 0.7× 299 1.4× 289 1.5× 27 1.5k
Jessie V.B. Warms United States 17 789 1.6× 406 1.1× 244 0.7× 185 0.9× 84 0.4× 19 1.3k
David P. Kosow United States 20 512 1.0× 121 0.3× 252 0.7× 134 0.6× 94 0.5× 31 969
Haruhisa Yoshikawa Japan 19 676 1.3× 701 1.8× 307 0.9× 61 0.3× 39 0.2× 72 1.6k
Lorenzo Minchiotti Italy 25 1.3k 2.6× 248 0.6× 294 0.8× 135 0.7× 93 0.5× 84 1.7k
Thomas H. Zytkovicz United States 11 604 1.2× 176 0.5× 91 0.3× 107 0.5× 47 0.2× 19 1.2k
Masazumi Takeshita Japan 17 408 0.8× 186 0.5× 124 0.3× 121 0.6× 37 0.2× 50 843
Stephen J. Hoffman United States 14 413 0.8× 161 0.4× 433 1.2× 44 0.2× 26 0.1× 20 863
Yosuke Yoneyama Japan 21 701 1.4× 269 0.7× 529 1.5× 26 0.1× 21 0.1× 78 1.3k

Countries citing papers authored by Zelda B. Rose

Since Specialization
Citations

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

Fields of papers citing papers by Zelda B. Rose

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Zelda B. Rose. 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 Zelda B. Rose. The network helps show where Zelda B. Rose may publish in the future.

Co-authorship network of co-authors of Zelda B. Rose

This figure shows the co-authorship network connecting the top 25 collaborators of Zelda B. Rose. A scholar is included among the top collaborators of Zelda B. Rose 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 Zelda B. Rose. Zelda B. Rose 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.
Rose, Zelda B.. (1986). The glucose biphosphate family of enzymes. Trends in Biochemical Sciences. 11(6). 253–255. 9 indexed citations
2.
Rose, Zelda B., et al.. (1986). The enzymic synthesis of ribose-1,5-bisphosphate: Studies of its role in metabolism. Archives of Biochemistry and Biophysics. 250(2). 513–518. 10 indexed citations
3.
Carter, Joyce G., et al.. (1985). Distribution of Glucose‐ 1,6‐Bisphosphate and IMP‐Activated Glucose Bisphosphatase in Brain and Retina. Journal of Neurochemistry. 44(6). 1741–1746. 10 indexed citations
4.
Rose, Zelda B. & G.S. Kaklij. (1984). The effects of anions on phosphoglycerate mutase. Biochemical and Biophysical Research Communications. 121(3). 834–841. 6 indexed citations
5.
Rose, Zelda B., et al.. (1984). Macro-structural organization of phosphoglycerate mutase. Biochemical and Biophysical Research Communications. 121(3). 826–833. 6 indexed citations
6.
Gupta, Raj K., Pratima Gupta, W.D. Yushok, & Zelda B. Rose. (1983). Measurement of the dissociation constant of MgATP at physiological nucleotide levels by a combination of 31P NMR and optical absorbance spectroscopy. Biochemical and Biophysical Research Communications. 117(1). 210–216. 86 indexed citations
7.
Rose, Zelda B., et al.. (1983). Role of inosine 5'-phosphate in activating glucose bisphosphatase. Biochemistry. 22(6). 1356–1361. 18 indexed citations
8.
Rose, Zelda B.. (1982). [4] Intermediates in the phosphoglycerate mutase and bisphosphoglycerate synthase reactions. Methods in enzymology on CD-ROM/Methods in enzymology. 87. 42–51. 11 indexed citations
9.
Rose, Zelda B.. (1981). Phosphoglycolate phosphatase from human red blood cells. Archives of Biochemistry and Biophysics. 208(2). 602–609. 18 indexed citations
10.
Rose, Zelda B.. (1980). The Enzymology of 2, 3‐Bisphosphoglycerate. Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects. 51. 211–253. 61 indexed citations
11.
Rose, Zelda B., et al.. (1979). A reappaisal of 31P NMR studies indicating enzyme complexation in red blood cells. Biochemical and Biophysical Research Communications. 91(2). 651–657. 6 indexed citations
12.
Rose, Zelda B.. (1976). A procedure for decreasing the level of 2,3-bisphosphoglycerate in red cells invitro. Biochemical and Biophysical Research Communications. 73(4). 1011–1017. 30 indexed citations
13.
Rose, Zelda B. & Syamalima Dube. (1976). The purification and kinetic properties of bisphosphoglycerate synthase from horse red blood cells. Archives of Biochemistry and Biophysics. 177(1). 284–292. 31 indexed citations
14.
Hamasaki, Naotaka & Zelda B. Rose. (1974). The Binding of Phosphorylated Red Cell Metabolites to Human Hemoglobin A. Journal of Biological Chemistry. 249(24). 7896–7901. 76 indexed citations
15.
Rose, Zelda B. & Robert G. Whalen. (1973). The Phosphorylation of Diphosphoglycerate Mutase. Journal of Biological Chemistry. 248(5). 1513–1519. 52 indexed citations
16.
Rose, Zelda B.. (1971). The phosphorylation of yeast phosphoglycerate mutase. Archives of Biochemistry and Biophysics. 146(1). 359–360. 43 indexed citations
17.
Rose, Zelda B.. (1970). Evidence for a phosphohistidine protein intermediate in the phosphoglycerate mutase reaction. Archives of Biochemistry and Biophysics. 140(2). 508–513. 86 indexed citations
18.
Rose, Zelda B.. (1966). The Stereochemistry of the Nicotinamide Adenine Dinucleotide-specific Isocitric Dehydrogenase Reaction. Journal of Biological Chemistry. 241(10). 2311–2313. 9 indexed citations
19.
Rose, Zelda B. & E. Racker. (1962). Formaldehyde Dehydrogenase from Bakers' Yeast. Journal of Biological Chemistry. 237(10). 3279–3281. 41 indexed citations
20.
Rose, Zelda B.. (1960). Studies on the Mechanism of Action of Isocitric Dehydrogenase. Journal of Biological Chemistry. 235(4). 928–933. 67 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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