Charles M. Grisham

1.6k total citations
58 papers, 1.2k citations indexed

About

Charles M. Grisham is a scholar working on Molecular Biology, Spectroscopy and Nuclear and High Energy Physics. According to data from OpenAlex, Charles M. Grisham has authored 58 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 23 papers in Spectroscopy and 13 papers in Nuclear and High Energy Physics. Recurrent topics in Charles M. Grisham's work include Advanced NMR Techniques and Applications (18 papers), Ion Transport and Channel Regulation (13 papers) and NMR spectroscopy and applications (13 papers). Charles M. Grisham is often cited by papers focused on Advanced NMR Techniques and Applications (18 papers), Ion Transport and Channel Regulation (13 papers) and NMR spectroscopy and applications (13 papers). Charles M. Grisham collaborates with scholars based in United States, Denmark and Israel. Charles M. Grisham's co-authors include Ronald E. Barnett, Albert S. Mildvan, Reginald H. Garrett, John M. Stewart, Mary Lou Gantzer, James E. Mahaney, William Hutton, Lindsay B. Wheeler, Charles Clark and Raj K. Gupta and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Charles M. Grisham

58 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Charles M. Grisham United States 20 779 250 111 102 88 58 1.2k
Peter Bigler Switzerland 22 604 0.8× 267 1.1× 123 1.1× 50 0.5× 60 0.7× 85 1.9k
C.M. Gary-Bobo France 21 895 1.1× 188 0.8× 38 0.3× 242 2.4× 47 0.5× 48 1.4k
Ronald E. Barnett United States 16 696 0.9× 108 0.4× 58 0.5× 117 1.1× 50 0.6× 27 1.0k
J.C. Hsia Canada 20 743 1.0× 158 0.6× 75 0.7× 115 1.1× 55 0.6× 68 1.1k
Wieland Willker Germany 15 638 0.8× 333 1.3× 88 0.8× 90 0.9× 82 0.9× 27 1.6k
Christoph Grathwohl United Kingdom 12 1.0k 1.3× 305 1.2× 195 1.8× 56 0.5× 96 1.1× 12 1.3k
Max A. Keniry Australia 26 1.4k 1.8× 391 1.6× 234 2.1× 74 0.7× 111 1.3× 69 2.0k
Gad Yagil Israel 19 1.2k 1.5× 164 0.7× 116 1.0× 146 1.4× 77 0.9× 46 1.9k
Jean‐Marc Lhoste France 18 604 0.8× 144 0.6× 235 2.1× 36 0.4× 40 0.5× 46 1.0k
Teresa J. T. Pinheiro United Kingdom 28 1.6k 2.0× 230 0.9× 208 1.9× 256 2.5× 75 0.9× 52 2.0k

Countries citing papers authored by Charles M. Grisham

Since Specialization
Citations

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

Fields of papers citing papers by Charles M. Grisham

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Charles M. Grisham

This figure shows the co-authorship network connecting the top 25 collaborators of Charles M. Grisham. A scholar is included among the top collaborators of Charles M. Grisham 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 Charles M. Grisham. Charles M. Grisham 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.
Wheeler, Lindsay B., et al.. (2016). Computational Methods in General Chemistry: Perceptions of Programming, Prior Experience, and Student Outcomes. Journal of College Science Teaching. 45(3). 83–91. 1 indexed citations
2.
Ayers, Edward L. & Charles M. Grisham. (2003). Why IT Has Not Paid Off as We Hoped (Yet). 38(6). 40. 13 indexed citations
3.
Gray, Mary C., et al.. (2001). Structural Consequences of Divalent Metal Binding by the Adenylyl Cyclase Toxin of Bordetella pertussis. Archives of Biochemistry and Biophysics. 395(2). 169–176. 24 indexed citations
4.
Goger, Michael, Ivan S. Login, Erik Fernández, & Charles M. Grisham. (1994). 31P NMR investigation of energy metabolism in perifused MMQ cells. Magnetic Resonance in Medicine. 32(5). 584–591. 3 indexed citations
5.
Grisham, Charles M.. (1994). Biochemistry, 5Th Edition. 4 indexed citations
6.
Mahaney, James E. & Charles M. Grisham. (1992). Effects of ouabain on the rotational dynamics of renal sodium-potassium ATPase studied by saturation-transfer EPR. Biochemistry. 31(7). 2025–2034. 3 indexed citations
7.
Kuntzweiler, Theresa A. & Charles M. Grisham. (1992). Inactivation and phosphorylation of sarcoplasmic reticulum Ca2+-ATPase by Mg · ATP analogues Rh(III)-ATP and Co(III)-ATP. Archives of Biochemistry and Biophysics. 295(1). 188–197. 1 indexed citations
8.
Maurer, Muriel C., Julianne J. Sando, & Charles M. Grisham. (1992). High-affinity calcium and substrate-binding sites on protein kinase C .alpha. as determined by nuclear magnetic resonance spectroscopy. Biochemistry. 31(33). 7714–7721. 13 indexed citations
9.
Mahaney, James E., Christopher Weis, Charles M. Grisham, & Howard Kutchai. (1991). Antibodies against the 53 kDa glycoprotein inhibit the rotational dynamics of both the 53 kDa glycoprotein and the Ca2+-ATPase in the sarcoplasmic reticulum membrane. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1064(1). 55–68. 5 indexed citations
10.
Mahaney, James E., et al.. (1990). Saturation transfer EPR measurements of the rotational motion of a strongly immobilized ouabain spin label on renal Na, K‐ATPase. FEBS Letters. 260(2). 160–164. 48 indexed citations
11.
Stewart, John M., et al.. (1989). Nuclear Overhauser effect studies of the conformation of Co(NH3)4ATP bound to kidney sodium-potassium ATPase. Biochemistry. 28(11). 4695–4701. 17 indexed citations
12.
Grisham, Charles M., et al.. (1988). NMR relaxation measurements detect four intermediate states of ATPase and transport cycle of sarcoplasmic reticulum Ca2+-ATPase. Biochemical and Biophysical Research Communications. 155(1). 236–242. 6 indexed citations
13.
Andersen, Jens Peter, et al.. (1986). Occluded calcium sites in soluble sarcoplasmic reticulum Ca2+-ATPase.. Journal of Biological Chemistry. 261(4). 1495–1498. 15 indexed citations
14.
Brewer, Greg, et al.. (1984). The crystal and molecular structure of [Co(NH3)5PO4]·3H2O, a Na+-K+ ATPase probe. Inorganica Chimica Acta. 89(2). 105–111. 3 indexed citations
15.
Grisham, Charles M.. (1981). Characterization of ATP binding sites of sheep kidney medulla (Na+ + K+)-ATPase using CrATP. Journal of Inorganic Biochemistry. 14(1). 45–57. 19 indexed citations
17.
Grisham, Charles M. & William Hutton. (1978). Lithium-7 NMR as a probe of monovalent cation sites at the active site of (Na+ + K+)-ATPase from kidney. Biochemical and Biophysical Research Communications. 81(4). 1406–1411. 20 indexed citations
18.
Grisham, Charles M., Raj K. Gupta, Ronald E. Barnett, & Albert S. Mildvan. (1974). Thallium-205 Nuclear Relaxation and Kinetic Studies of Sodium and Potassium Ion-activated Adenosine Triphosphatase. Journal of Biological Chemistry. 249(21). 6738–6744. 52 indexed citations
19.
Grisham, Charles M. & Ronald E. Barnett. (1973). Role of lipid-phase transitions in the regulation of the (sodium + potassium ion)-dependent adenosinetriphosphatase. Biochemistry. 12(14). 2635–2637. 211 indexed citations
20.
Grisham, Charles M.. (1972). The interrelationship of membrane and protein structure in the functioning of the (Na+ + K+)-activated ATPase. Biochimica et Biophysica Acta. 266(3). 613–624. 62 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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