M.F. Utter

2.4k total citations
30 papers, 1.5k citations indexed

About

M.F. Utter is a scholar working on Molecular Biology, Cell Biology and Biochemistry. According to data from OpenAlex, M.F. Utter has authored 30 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 16 papers in Cell Biology and 9 papers in Biochemistry. Recurrent topics in M.F. Utter's work include Mitochondrial Function and Pathology (7 papers), Hemoglobin structure and function (7 papers) and Biotin and Related Studies (6 papers). M.F. Utter is often cited by papers focused on Mitochondrial Function and Pathology (7 papers), Hemoglobin structure and function (7 papers) and Biotin and Related Studies (6 papers). M.F. Utter collaborates with scholars based in United States, Australia and Tanzania. M.F. Utter's co-authors include K. Kurahashi, Marca Weinberg, Richard W. Hanson, Y Hod, Kiyoshi Kurahashi, R. J. Pennington, Fumihide Isohashi, Malcolm Watford, Irwin A. Rose and Barry Taylor and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

M.F. Utter

30 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M.F. Utter United States 22 882 413 361 283 210 30 1.5k
Harold L. Segal United States 23 873 1.0× 345 0.8× 263 0.7× 206 0.7× 246 1.2× 49 1.5k
Theodor Bücher Germany 20 1.3k 1.4× 236 0.6× 234 0.6× 216 0.8× 370 1.8× 44 2.0k
W. Seubert Germany 24 1.3k 1.5× 281 0.7× 335 0.9× 399 1.4× 389 1.9× 47 1.8k
Huei-Che Chang United States 8 634 0.7× 324 0.8× 274 0.8× 201 0.7× 280 1.3× 8 1.1k
Robert Y. Hsu United States 21 828 0.9× 247 0.6× 341 0.9× 129 0.5× 204 1.0× 38 1.3k
S. Ratner United States 24 738 0.8× 361 0.9× 550 1.5× 431 1.5× 374 1.8× 44 1.6k
Francis E. Stolzenbach United States 21 1.4k 1.5× 337 0.8× 221 0.6× 182 0.6× 189 0.9× 28 2.1k
M.A. Rosemeyer United Kingdom 17 619 0.7× 334 0.8× 280 0.8× 99 0.3× 238 1.1× 29 1.2k
Thomas P. Fondy United States 20 877 1.0× 353 0.9× 220 0.6× 166 0.6× 121 0.6× 49 1.4k
David P. Bloxham United Kingdom 19 1.1k 1.2× 273 0.7× 302 0.8× 153 0.5× 430 2.0× 68 1.9k

Countries citing papers authored by M.F. Utter

Since Specialization
Citations

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

Fields of papers citing papers by M.F. Utter

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M.F. Utter. 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 M.F. Utter. The network helps show where M.F. Utter may publish in the future.

Co-authorship network of co-authors of M.F. Utter

This figure shows the co-authorship network connecting the top 25 collaborators of M.F. Utter. A scholar is included among the top collaborators of M.F. Utter 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 M.F. Utter. M.F. Utter 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.
Freytag, Svend O. & M.F. Utter. (1983). Regulation of the synthesis and degradation of pyruvate carboxylase in 3T3-L1 cells.. Journal of Biological Chemistry. 258(10). 6307–6312. 30 indexed citations
2.
Hod, Y, M.F. Utter, & Richard W. Hanson. (1982). The mitochondrial and cytosolic forms of avian phosphoenolpyruvate carboxykinase (GTP) are encoded by different messenger RNAs.. Journal of Biological Chemistry. 257(22). 13787–13794. 31 indexed citations
3.
Goss, James A., et al.. (1981). Characterization of the subunit structure of pyruvate carboxylase from Pseudomonas citronellolis.. Journal of Biological Chemistry. 256(22). 11819–11825. 20 indexed citations
4.
Markovitz, Paul J., et al.. (1981). Comparative inhibition of mitochondrial and cytosolic phosphoenolpyruvate carboxykinases by stereospecific substrate analogues.. Proceedings of the National Academy of Sciences. 78(11). 6680–6683. 11 indexed citations
5.
Weinberg, Marca & M.F. Utter. (1980). Effect of streptozotocin-induced diabetes mellitus on the turnover of rat liver pyruvate carboxylase and pyruvate dehydrogenase. Biochemical Journal. 188(3). 601–608. 50 indexed citations
6.
Beegen, H., et al.. (1979). A re-examination of the electron microscopic appearance of pyruvate carboxylase from chicken liver.. Journal of Biological Chemistry. 254(5). 1740–1747. 12 indexed citations
7.
Chuang, David & M.F. Utter. (1979). Structural and regulatory properties of pyruvate kinase from Pseudomonas citronellolis.. Journal of Biological Chemistry. 254(17). 8434–8441. 16 indexed citations
8.
Weinberg, Marca & M.F. Utter. (1979). Effect of thyroid hormone on the turnover of rat liver pyruvate carboxylase and pyruvate dehydrogenase.. Journal of Biological Chemistry. 254(19). 9492–9499. 66 indexed citations
9.
Taylor, Barry, William H. Frey, R E Barden, M.C. Scrutton, & M.F. Utter. (1978). The use of the ultracentrifuge to determine the catalytically competent forms of enzymes with more than one oligomeric structure. Multiple reacting forms of pyruvate carboxylase from chicken and rat liver.. Journal of Biological Chemistry. 253(9). 3062–3069. 13 indexed citations
10.
O’Brien, Ricky, David Chuang, Barry Taylor, & M.F. Utter. (1977). Novel enzymic machinery for the metabolism of oxalacetate, phosphoenolpyruvate, and pyruvate in Pseudomonas citronellolis.. Journal of Biological Chemistry. 252(4). 1257–1263. 41 indexed citations
11.
Barritt, Greg J., et al.. (1976). regulation of pyruvate carboxylase activity in gluconeogenic tissues. 3 indexed citations
12.
Utter, M.F., et al.. (1975). Decarboxylation of oxalacetate to pyruvate by purified avian liver phosphoenolpyruvate carboxykinase. Journal of Biological Chemistry. 250(23). 9099–9105. 64 indexed citations
13.
Utter, M.F., et al.. (1969). Pyruvate carboxylase. XIII. Reversible inactivation by cold. Biochemistry. 8(12). 5136–5148. 89 indexed citations
14.
Kurahashi, K., R. J. Pennington, & M.F. Utter. (1957). NUCLEOTIDE SPECIFICITY OF OXALACETIC CARBOXYLASE. Journal of Biological Chemistry. 226(2). 1059–1075. 48 indexed citations
15.
Vennesland, Birgit, et al.. (1956). THE MECHANISM OF THE REVERSIBLE CARBOXYLATION OF PHOSPHOENOLPYRUVATE. Journal of Biological Chemistry. 223(1). 551–557. 41 indexed citations
16.
Utter, M.F., K. Kurahashi, & Irwin A. Rose. (1954). SOME PROPERTIES OF OXALACETIC CARBOXYLASE. Journal of Biological Chemistry. 207(2). 803–819. 66 indexed citations
17.
Utter, M.F. & K. Kurahashi. (1954). PURIFICATION OF OXALACETIC CARBOXYLASE FROM CHICKEN LIVER. Journal of Biological Chemistry. 207(2). 787–802. 157 indexed citations
18.
Utter, M.F. & Kiyoshi Kurahashi. (1953). MECHANISM OF ACTION OF OXALACETIC CARBOXYLASE FROM LIVER1. Journal of the American Chemical Society. 75(3). 758–758. 58 indexed citations
19.
Utter, M.F.. (1952). Carbon dioxide fixation and photosynthesis. Archives of Biochemistry and Biophysics. 38(1). 473–474. 11 indexed citations
20.
Utter, M.F.. (1951). INTERRELATIONSHIPS OF OXALACETIC AND l-MALIC ACIDS IN CARBON DIOXIDE FIXATION. Journal of Biological Chemistry. 188(2). 847–863. 35 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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