Charles Grubmeyer

4.2k total citations · 1 hit paper
62 papers, 3.7k citations indexed

About

Charles Grubmeyer is a scholar working on Molecular Biology, Infectious Diseases and Materials Chemistry. According to data from OpenAlex, Charles Grubmeyer has authored 62 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 56 papers in Molecular Biology, 19 papers in Infectious Diseases and 19 papers in Materials Chemistry. Recurrent topics in Charles Grubmeyer's work include Biochemical and Molecular Research (39 papers), HIV/AIDS drug development and treatment (19 papers) and Enzyme Structure and Function (19 papers). Charles Grubmeyer is often cited by papers focused on Biochemical and Molecular Research (39 papers), HIV/AIDS drug development and treatment (19 papers) and Enzyme Structure and Function (19 papers). Charles Grubmeyer collaborates with scholars based in United States, Canada and Denmark. Charles Grubmeyer's co-authors include Harvey S. Penefsky, Richard L. Cross, James C. Sacchettini, Giovanna Scapin, Yiming Xu, Janina C. Eads, Vern L. Schramm, Carrie Baker Brachmann, Jef D. Boeke and Jeffrey S. Smith and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Charles Grubmeyer

62 papers receiving 3.5k citations

Hit Papers

A phylogenetically conserved NAD + -dependent protein dea... 2000 2026 2008 2017 2000 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Charles Grubmeyer United States 28 3.1k 740 704 496 438 62 3.7k
Abdellah Allali‐Hassani Canada 34 3.3k 1.0× 318 0.4× 103 0.1× 232 0.5× 195 0.4× 60 4.1k
Alexey Bochkarev Canada 28 2.2k 0.7× 487 0.7× 93 0.1× 260 0.5× 173 0.4× 42 3.1k
P. Loppnau Canada 28 2.1k 0.7× 192 0.3× 98 0.1× 102 0.2× 181 0.4× 54 2.7k
Robert W. Sprung United States 16 2.5k 0.8× 437 0.6× 51 0.1× 131 0.3× 608 1.4× 29 3.3k
Andrew D. Napper United States 22 1.3k 0.4× 369 0.5× 92 0.1× 42 0.1× 730 1.7× 53 2.4k
Brian H. Shilton Canada 28 1.6k 0.5× 141 0.2× 134 0.2× 196 0.4× 36 0.1× 64 2.5k
Ana P. C. Rodrigues United States 6 1.6k 0.5× 198 0.3× 157 0.2× 248 0.5× 41 0.1× 6 2.3k
Christie G. Brouillette United States 29 2.6k 0.8× 133 0.2× 129 0.2× 210 0.4× 25 0.1× 57 3.7k
F. Niesen United Kingdom 19 2.7k 0.9× 162 0.2× 199 0.3× 443 0.9× 18 0.0× 25 3.5k
H. Raghuraman India 24 1.7k 0.6× 177 0.2× 46 0.1× 122 0.2× 271 0.6× 42 2.7k

Countries citing papers authored by Charles Grubmeyer

Since Specialization
Citations

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

Fields of papers citing papers by Charles Grubmeyer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Charles Grubmeyer

This figure shows the co-authorship network connecting the top 25 collaborators of Charles Grubmeyer. A scholar is included among the top collaborators of Charles Grubmeyer 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 Grubmeyer. Charles Grubmeyer 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.
Hansen, Michael Riis, Eric W. Barr, Kaj Frank Jensen, et al.. (2013). Catalytic site interactions in yeast OMP synthase. Archives of Biochemistry and Biophysics. 542. 28–38. 7 indexed citations
2.
Schramm, Vern L. & Charles Grubmeyer. (2004). Phosphoribosyltransferase Mechanisms and Roles in Nucleic Acid Metabolism. Progress in nucleic acid research and molecular biology. 78. 261–304. 37 indexed citations
3.
Schramm, Vern L., Steven C. Almo, Wuxian Shi, et al.. (1999). The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor.. Nature Structural Biology. 6(6). 588–593. 139 indexed citations
4.
Schramm, Vern L., Peter C. Tyler, Richard H. Furneaux, et al.. (1999). Transition-state analogs as inhibitors of human and malarial hypoxanthine-guanine phosphoribosyltransferases.. Nature Structural Biology. 6(6). 582–587. 89 indexed citations
5.
Sharma, Vivek, Charles Grubmeyer, & James C. Sacchettini. (1998). Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target. Structure. 6(12). 1587–1599. 63 indexed citations
6.
Eads, Janina C., et al.. (1997). A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase. Structure. 5(1). 47–58. 74 indexed citations
7.
Scapin, Giovanna, et al.. (1995). Structure and Function of Salmonella typhimurium Orotate Phosphoribosyltransferase: Protein Complementation Reveals Shared Active Sites. Biochemistry. 34(34). 10764–10770. 27 indexed citations
8.
Scapin, Giovanna, et al.. (1995). The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and .alpha.-D-5-Phosphoribosyl-1-Pyrophosphate. Biochemistry. 34(34). 10744–10754. 73 indexed citations
9.
Scapin, Giovanna, et al.. (1995). Locations and Functional Roles of Conserved Lysine Residues in Salmonella typhimurium Orotate Phosphoribosyltransferase. Biochemistry. 34(34). 10755–10763. 34 indexed citations
10.
Scapin, Giovanna, Charles Grubmeyer, & James C. Sacchettini. (1994). Crystal Structure of Orotate Phosphoribosyltransferase. Biochemistry. 33(6). 1287–1294. 94 indexed citations
11.
Eads, Janina C., Giovanna Scapin, Yiming Xu, Charles Grubmeyer, & James C. Sacchettini. (1994). The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 78(2). 325–334. 170 indexed citations
12.
Scapin, Giovanna, et al.. (1993). Primary Structure and Crystallization of Orotate Phosphoribosyltransferase from Salmonella typhimurium. Journal of Molecular Biology. 230(4). 1304–1308. 18 indexed citations
13.
Grubmeyer, Charles, et al.. (1993). The Role of Divalent Magnesium in Activating the Reaction Catalyzed by Orotate Phosphoribosyltransferase. Archives of Biochemistry and Biophysics. 303(2). 321–325. 19 indexed citations
14.
Vinitsky, Alexander, et al.. (1990). Kinetic mechanism of orotate phosphoribosyltransferase from Salmonella typhimurium. Biochemistry. 29(46). 10480–10487. 50 indexed citations
15.
Grubmeyer, Charles. (1990). A Paradigm for Aldehyde Oxidation: Histidinol Dehydrogenase. Advances in experimental medicine and biology. 284. 105–112. 2 indexed citations
16.
Grubmeyer, Charles, et al.. (1989). Salmonella typhimurium histidinol dehydrogenase: complete reaction stereochemistry and active site mapping. Biochemistry. 28(20). 8174–8180. 17 indexed citations
17.
Grubmeyer, Charles, et al.. (1987). Kinetic mechanism of histidinol dehydrogenase: histidinol binding and exchange reactions. Biochemistry. 26(12). 3369–3373. 13 indexed citations
18.
Grubmeyer, Charles & Mary S. Spencer. (1980). ATPase Activity of Pea Cotyledon Submitochondrial Particles. PLANT PHYSIOLOGY. 65(2). 281–285. 15 indexed citations
19.
Grubmeyer, Charles, et al.. (1979). Oxidative Phosphorylation in Pea Cotyledon Submitochondrial Particles. PLANT PHYSIOLOGY. 64(5). 757–762. 8 indexed citations
20.
Grubmeyer, Charles & Mary S. Spencer. (1978). Oligomycin-sensitive ATPase of Submitochondrial Particles from Corn. PLANT PHYSIOLOGY. 61(4). 567–569. 11 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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