Joseph A. Beavo

546 total citations
10 papers, 456 citations indexed

About

Joseph A. Beavo is a scholar working on Molecular Biology, Pharmacology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Joseph A. Beavo has authored 10 papers receiving a total of 456 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 2 papers in Pharmacology and 2 papers in Cellular and Molecular Neuroscience. Recurrent topics in Joseph A. Beavo's work include Phosphodiesterase function and regulation (8 papers), Enzyme function and inhibition (3 papers) and Chemical Synthesis and Analysis (2 papers). Joseph A. Beavo is often cited by papers focused on Phosphodiesterase function and regulation (8 papers), Enzyme function and inhibition (3 papers) and Chemical Synthesis and Analysis (2 papers). Joseph A. Beavo collaborates with scholars based in United States. Joseph A. Beavo's co-authors include J. Kelley Bentley, Harry Charbonneau, Lauren P. Baker, Soren Impey, Guy C.‐K. Chan, Allan Z. Zhao, Wei Jia, William K. Sonnenburg, Kenneth A. Walsh and Jerlyn Beltman and has published in prestigious journals such as Neuron, Biochemistry and Biochemical and Biophysical Research Communications.

In The Last Decade

Joseph A. Beavo

10 papers receiving 448 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Joseph A. Beavo United States 8 299 148 114 71 47 10 456
Michelle C. Catlin United States 4 372 1.2× 226 1.5× 96 0.8× 21 0.3× 80 1.7× 6 572
Chris Mathes United States 13 441 1.5× 241 1.6× 84 0.7× 24 0.3× 93 2.0× 22 586
Mylène Robert France 8 581 1.9× 198 1.3× 45 0.4× 19 0.3× 67 1.4× 8 624
Haruo Takemura Japan 12 356 1.2× 164 1.1× 75 0.7× 50 0.7× 98 2.1× 26 501
Xiao Wen Fu United States 13 304 1.0× 81 0.5× 43 0.4× 15 0.2× 100 2.1× 18 506
Laura A. Price United States 10 419 1.4× 211 1.4× 33 0.3× 23 0.3× 17 0.4× 13 629
Bernd Nilius Belgium 9 341 1.1× 188 1.3× 175 1.5× 55 0.8× 93 2.0× 12 520
Steven C. Prinster United States 6 388 1.3× 281 1.9× 24 0.2× 70 1.0× 88 1.9× 7 528
H. Scheer Italy 12 462 1.5× 227 1.5× 90 0.8× 10 0.1× 28 0.6× 18 628
I. Wessler Germany 6 252 0.8× 121 0.8× 45 0.4× 16 0.2× 80 1.7× 9 420

Countries citing papers authored by Joseph A. Beavo

Since Specialization
Citations

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

Fields of papers citing papers by Joseph A. Beavo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Joseph A. Beavo. 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 Joseph A. Beavo. The network helps show where Joseph A. Beavo may publish in the future.

Co-authorship network of co-authors of Joseph A. Beavo

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph A. Beavo. A scholar is included among the top collaborators of Joseph A. Beavo 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 Joseph A. Beavo. Joseph A. Beavo is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

10 of 10 papers shown
1.
Beavo, Joseph A., et al.. (2000). [40] Purification and assay of bovine type 6 photoreceptor phosphodiesterase and its subunits. Methods in enzymology on CD-ROM/Methods in enzymology. 315. 597–616. 4 indexed citations
2.
Jia, Wei, Allan Z. Zhao, Guy C.‐K. Chan, et al.. (1998). Phosphorylation and Inhibition of Olfactory Adenylyl Cyclase by CaM Kinase II in Neurons. Neuron. 21(3). 495–504. 155 indexed citations
3.
Hamilton, Susan E., Rabi K. Prusti, J. Kelley Bentley, Joseph A. Beavo, & James B. Hurley. (1993). Affinities of bovine photoreceptor cGMP phosphodiesterases for rod and cone inhibitory subunits. FEBS Letters. 318(2). 157–161. 30 indexed citations
4.
Beltman, Jerlyn, William K. Sonnenburg, & Joseph A. Beavo. (1993). The role of protein phosphorylation in the regulation of cyclic nucleotide phosphodiesterases. Molecular and Cellular Biochemistry. 127-128(1). 239–253. 38 indexed citations
5.
Bentley, J. Kelley & Joseph A. Beavo. (1992). Regulation and function of cyclic nucleotides. Current Opinion in Cell Biology. 4(2). 233–240. 69 indexed citations
6.
Charbonneau, Harry, Santosh Kumar, Jeffrey P. Novack, et al.. (1991). Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain. Biochemistry. 30(32). 7931–7940. 68 indexed citations
7.
Trong, Hai Le, Norbert Beier, William K. Sonnenburg, et al.. (1990). Amino acid sequence of the cyclic GMP stimulated cyclic nucleotide phosphodiesterase from bovine heart. Biochemistry. 29(44). 10280–10288. 49 indexed citations
8.
Novack, Jeffrey P., Harry Charbonneau, Donald Blumenthal, Kenneth A. Walsh, & Joseph A. Beavo. (1989). The Domain Structure of the Calmodulin-Dependent Phosphodiesterase Isozymes. Advances in experimental medicine and biology. 255. 387–395. 3 indexed citations
9.
Hansen, R. Scott, Harry Charbonneau, & Joseph A. Beavo. (1988). [51] Purification of calmodulin-stimulated cyclic nucleotide phosphodiesterase by monoclonal antibody affinity chromatography. Methods in enzymology on CD-ROM/Methods in enzymology. 159. 543–557. 17 indexed citations
10.
Blumenthal, Donald, Harry Charbonneau, Thomas R. Hinds, et al.. (1988). Synthetic peptides based on the calmodulin-binding domain of myosin light chain kinase inhibit activation of other calmodulin-dependent enzymes. Biochemical and Biophysical Research Communications. 156(2). 860–865. 23 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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