Gerald M. Carlson

2.0k total citations
72 papers, 1.6k citations indexed

About

Gerald M. Carlson is a scholar working on Molecular Biology, Materials Chemistry and Rheumatology. According to data from OpenAlex, Gerald M. Carlson has authored 72 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 58 papers in Molecular Biology, 25 papers in Materials Chemistry and 12 papers in Rheumatology. Recurrent topics in Gerald M. Carlson's work include Enzyme Structure and Function (25 papers), Protein Kinase Regulation and GTPase Signaling (17 papers) and Glycosylation and Glycoproteins Research (13 papers). Gerald M. Carlson is often cited by papers focused on Enzyme Structure and Function (25 papers), Protein Kinase Regulation and GTPase Signaling (17 papers) and Glycosylation and Glycoproteins Research (13 papers). Gerald M. Carlson collaborates with scholars based in United States, United Kingdom and France. Gerald M. Carlson's co-authors include Sidney Cohen, William J. Snape, Owen W. Nadeau, Giovanna Colombo, Henry A. Lardy, Marita M. King, Donald J. Graves, Todd Holyoak, Peter J. Bechtel and Mona Trempe Norcum and has published in prestigious journals such as Journal of Biological Chemistry, Gastroenterology and Journal of Molecular Biology.

In The Last Decade

Gerald M. Carlson

72 papers receiving 1.6k citations

Peers

Gerald M. Carlson
Ronald E. Chance United States
J. W. Black United Kingdom
Stefania Hanau Italy
Michael E. Parsons United Kingdom
Annie Hiniker United States
Jason Brown United States
Thomas Weiser Germany
Albano C. Méli France
Gregor Schütze Germany
Ann Barbier United States
Ronald E. Chance United States
Gerald M. Carlson
Citations per year, relative to Gerald M. Carlson Gerald M. Carlson (= 1×) peers Ronald E. Chance

Countries citing papers authored by Gerald M. Carlson

Since Specialization
Citations

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

Fields of papers citing papers by Gerald M. Carlson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Gerald M. Carlson

This figure shows the co-authorship network connecting the top 25 collaborators of Gerald M. Carlson. A scholar is included among the top collaborators of Gerald M. Carlson 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 Gerald M. Carlson. Gerald M. Carlson 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.
2.
Carlson, Gerald M., Gerald A. Dienel, & Roger Colbran. (2018). Introduction to the Thematic Minireview Series: Brain glycogen metabolism. Journal of Biological Chemistry. 293(19). 7087–7088. 6 indexed citations
3.
Carlson, Gerald M., et al.. (2016). The regulatory α and β subunits of phosphorylase kinase directly interact with its substrate, glycogen phosphorylase. Biochemical and Biophysical Research Communications. 482(2). 221–225. 5 indexed citations
4.
Artigues, Antonio, Owen W. Nadeau, María T. Villar, et al.. (2016). Protein Structural Analysis via Mass Spectrometry-Based Proteomics. Advances in experimental medicine and biology. 919. 397–431. 25 indexed citations
5.
Liu, Weiya, et al.. (2013). Physicochemical changes in phosphorylase kinase induced by its cationic activator Mg2+. Protein Science. 22(4). 444–454. 4 indexed citations
6.
Lane, Laura A., Owen W. Nadeau, Gerald M. Carlson, & Carol V. Robinson. (2012). Mass Spectrometry Reveals Differences in Stability and Subunit Interactions between Activated and Nonactivated Conformers of the (αβγδ)4 Phosphorylase Kinase Complex. Molecular & Cellular Proteomics. 11(12). 1768–1776. 11 indexed citations
7.
Nadeau, Owen W. & Gerald M. Carlson. (2011). A Review of Methods Used for Identifying Structural Changes in a Large Protein Complex. Methods in molecular biology. 796. 117–132. 5 indexed citations
8.
Artigues, Antonio, et al.. (2008). Structural Evidence for Co-Evolution of the Regulation of Contraction and Energy Production in Skeletal Muscle. Journal of Molecular Biology. 377(3). 623–629. 14 indexed citations
9.
Liu, Weiya, et al.. (2008). Physicochemical changes in phosphorylase kinase associated with its activation. Protein Science. 17(12). 2111–2119. 9 indexed citations
10.
Middaugh, C. Russell, et al.. (2007). Electrostatic changes in phosphorylase kinase induced by its obligatory allosteric activator Ca2+. Protein Science. 16(3). 517–527. 18 indexed citations
11.
Nadeau, Owen W., David W. Anderson, Qing Yang, et al.. (2006). Evidence for the Location of the Allosteric Activation Switch in the Multisubunit Phosphorylase Kinase Complex from Mass Spectrometric Identification of Chemically Crosslinked Peptides. Journal of Molecular Biology. 365(5). 1429–1445. 22 indexed citations
12.
MacDonald, Brian A., et al.. (2005). Ca2+‐induced structural changes in phosphorylase kinase detected by small‐angle X‐ray scattering. Protein Science. 14(4). 1039–1048. 19 indexed citations
13.
Nadeau, Owen W., Edward P. Gogol, & Gerald M. Carlson. (2005). Cryoelectron microscopy reveals new features in the three‐dimensional structure of phosphorylase kinase. Protein Science. 14(4). 914–920. 15 indexed citations
14.
Rice, Nancy A., Owen W. Nadeau, Qing Yang, & Gerald M. Carlson. (2002). The Calmodulin-binding Domain of the Catalytic γ Subunit of Phosphorylase Kinase Interacts with Its Inhibitory α Subunit. Journal of Biological Chemistry. 277(17). 14681–14687. 24 indexed citations
15.
Carlson, Gerald M., et al.. (1998). Evaluation of Phosphoenolpyruvate as a Phosphoryl Group Donor for Phosphoproteins in Skeletal Muscle. Archives of Biochemistry and Biophysics. 357(2). 285–292. 2 indexed citations
16.
Nadeau, Owen W., David B. Sacks, & Gerald M. Carlson. (1997). The Structural Effects of Endogenous and Exogenous Ca2+/Calmodulin on Phosphorylase Kinase. Journal of Biological Chemistry. 272(42). 26202–26209. 19 indexed citations
17.
Marion, Tony N., David M. Tillman, Mona Trempe Norcum, et al.. (1994). An Epitope Proximal to the Carboxyl Terminus of the α-Subunit is Located near the Lobe Tips of the Phosphorylase Kinase Hexadecamer. Journal of Molecular Biology. 235(3). 974–982. 43 indexed citations
18.
Paudel, Hemant K., et al.. (1993). The model calmodulin-binding peptide melittin inhibits phosphorylase kinase by interacting with its catalytic center. Biochemistry. 32(44). 11865–11872. 11 indexed citations
19.
Carlson, Gerald M., et al.. (1991). Kinetic characterization of the calmodulin-activated catalytic subunit of phosphorylase kinase. Biochemistry. 30(42). 10274–10279. 14 indexed citations
20.

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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