John G. Conboy

13.6k total citations
73 papers, 3.9k citations indexed

About

John G. Conboy is a scholar working on Molecular Biology, Physiology and Pulmonary and Respiratory Medicine. According to data from OpenAlex, John G. Conboy has authored 73 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 50 papers in Molecular Biology, 40 papers in Physiology and 23 papers in Pulmonary and Respiratory Medicine. Recurrent topics in John G. Conboy's work include Erythrocyte Function and Pathophysiology (40 papers), RNA Research and Splicing (32 papers) and RNA modifications and cancer (25 papers). John G. Conboy is often cited by papers focused on Erythrocyte Function and Pathophysiology (40 papers), RNA Research and Splicing (32 papers) and RNA modifications and cancer (25 papers). John G. Conboy collaborates with scholars based in United States, Japan and China. John G. Conboy's co-authors include Narla Mohandas, Marilyn Parra, Yuet Wai Kan, Joel Anne Chasis, Sherry L. Gee, N Mohandas, Loren D. Walensky, Leah Rosenberg, Philippe Gascard and Solomon H. Snyder and has published in prestigious journals such as New England Journal of Medicine, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

John G. Conboy

73 papers receiving 3.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John G. Conboy United States 38 2.7k 1.4k 808 603 263 73 3.9k
Babette Gwynn United States 22 1.2k 0.4× 1.2k 0.9× 486 0.6× 197 0.3× 242 0.9× 36 2.5k
Tang K. Tang Taiwan 33 2.1k 0.8× 521 0.4× 1.7k 2.1× 349 0.6× 127 0.5× 81 3.2k
David Reczek United States 20 2.3k 0.9× 620 0.4× 1.6k 2.0× 362 0.6× 124 0.5× 25 4.1k
Sandy M. Price United States 22 2.4k 0.9× 371 0.3× 578 0.7× 446 0.7× 55 0.2× 28 3.8k
Shosei Kishida Japan 33 3.9k 1.5× 263 0.2× 1.2k 1.5× 109 0.2× 56 0.2× 67 4.7k
Isabel Correas Spain 30 1.4k 0.5× 985 0.7× 1.1k 1.3× 265 0.4× 75 0.3× 67 2.5k
Hiroaki Onda United States 22 2.2k 0.8× 1.3k 0.9× 338 0.4× 252 0.4× 46 0.2× 36 3.4k
Philippe Gascard United States 27 1.4k 0.5× 675 0.5× 542 0.7× 360 0.6× 80 0.3× 57 2.4k
Fuad Bahram Sweden 15 2.7k 1.0× 262 0.2× 601 0.7× 124 0.2× 141 0.5× 19 3.5k
Nicole Schreiber‐Agus United States 29 3.7k 1.4× 484 0.3× 533 0.7× 276 0.5× 134 0.5× 51 4.9k

Countries citing papers authored by John G. Conboy

Since Specialization
Citations

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

Fields of papers citing papers by John G. Conboy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John G. Conboy. 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 John G. Conboy. The network helps show where John G. Conboy may publish in the future.

Co-authorship network of co-authors of John G. Conboy

This figure shows the co-authorship network connecting the top 25 collaborators of John G. Conboy. A scholar is included among the top collaborators of John G. Conboy 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 John G. Conboy. John G. Conboy 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.
Huang, Yu‐Shan, Paul D. Kingsley, Xiuli An, et al.. (2017). Circulating primitive erythroblasts establish a functional, protein 4.1R-dependent cytoskeletal network prior to enucleating. Scientific Reports. 7(1). 5164–5164. 10 indexed citations
2.
Pimentel, Harold, Marilyn Parra, Sherry L. Gee, et al.. (2014). A dynamic alternative splicing program regulates gene expression during terminal erythropoiesis. Nucleic Acids Research. 42(6). 4031–4042. 70 indexed citations
3.
Lovci, Michael, Dana Ghanem, Justin D. Arnold, et al.. (2013). Rbfox proteins regulate alternative mRNA splicing through evolutionarily conserved RNA bridges. Nature Structural & Molecular Biology. 20(12). 1434–1442. 257 indexed citations
4.
Parra, Marilyn, Thomas L. Gallagher, Sharon L. Amacher, Narla Mohandas, & John G. Conboy. (2012). Deep Intron Elements Mediate Nested Splicing Events at Consecutive AG Dinucleotides To Regulate Alternative 3′ Splice Site Choice in Vertebrate 4.1 Genes. Molecular and Cellular Biology. 32(11). 2044–2053. 15 indexed citations
5.
Gallagher, Thomas L., Joshua A. Arribere, Cameron R. T. Exner, et al.. (2011). Rbfox-regulated alternative splicing is critical for zebrafish cardiac and skeletal muscle functions. Developmental Biology. 359(2). 251–261. 76 indexed citations
6.
Parra, Marilyn, Sherry L. Gee, Narla Mohandas, & John G. Conboy. (2010). Efficient in Vivo Manipulation of Alternative Pre-mRNA Splicing Events Using Antisense Morpholinos in Mice. Journal of Biological Chemistry. 286(8). 6033–6039. 21 indexed citations
7.
Das, Debopriya, Tyson A. Clark, Anthony Schweitzer, et al.. (2007). A correlation with exon expression approach to identify cis-regulatory elements for tissue-specific alternative splicing. Nucleic Acids Research. 35(14). 4845–4857. 69 indexed citations
8.
Parra, Marilyn, et al.. (2007). Intrasplicing coordinates alternative first exons with alternative splicing in the protein 4.1R gene. The EMBO Journal. 27(1). 122–131. 27 indexed citations
9.
Chen, Weiguo, Robert Lersch, Sherry L. Gee, et al.. (2006). Fox-2 Splicing Factor Binds to a Conserved Intron Motif to Promote Inclusion of Protein \n4.1R Alternative Exon 16. eScholarship (California Digital Library). 94 indexed citations
11.
Blot‐Chabaud, Marcel, Françoise Cluzeaud, Michael Patterson, et al.. (2003). Distinct distribution of specific members of protein 4.1 gene family in the mouse nephron. Kidney International. 63(4). 1321–1337. 48 indexed citations
12.
Parra, Marilyn, Philippe Gascard, Loren D. Walensky, et al.. (2000). Molecular and Functional Characterization of Protein 4.1B, a Novel Member of the Protein 4.1 Family with High Level, Focal Expression in Brain. Journal of Biological Chemistry. 275(5). 3247–3255. 114 indexed citations
13.
Gascard, Philippe, Wataru Nunomura, Gloria Lee, et al.. (1999). Deciphering the Nuclear Import Pathway for the Cytoskeletal Red Cell Protein 4.1R. Molecular Biology of the Cell. 10(6). 1783–1798. 39 indexed citations
14.
Conboy, John G.. (1999). The Role of Alternative Pre‐mRNA Splicing in Regulating the Structure and Function of Skeletal Protein 4.1. Proceedings of The Society for Experimental Biology and Medicine. 220(2). 73–78. 38 indexed citations
15.
Parra, Mireya, Philippe Gascard, Loren D. Walensky, et al.. (1998). Cloning and Characterization of 4.1G (EPB41L2), a New Member of the Skeletal Protein 4.1 (EPB41) Gene Family. Genomics. 49(2). 298–306. 97 indexed citations
16.
Schischmanoff, Pierre Olivier, R Winardi, Dennis E. Discher, et al.. (1995). Defining of the Minimal Domain of Protein 4.1 Involved in Spectrin-Actin Binding. Journal of Biological Chemistry. 270(36). 21243–21250. 57 indexed citations
17.
Gee, Sherry L. & John G. Conboy. (1994). Mouse erythroid cells express multiple putative RNA helicase genes exhibiting high sequence conservation from yeast to mammals. Gene. 140(2). 171–177. 40 indexed citations
18.
Conboy, John G.. (1993). Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells.. PubMed. 30(1). 58–73. 101 indexed citations
19.
Conboy, John G., Joel Anne Chasis, R Winardi, et al.. (1993). An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells.. Journal of Clinical Investigation. 91(1). 77–82. 35 indexed citations
20.
Mohandas, Narla, R Winardi, Chi-Sing Leung, et al.. (1992). Molecular basis for membrane rigidity of hereditary ovalocytosis. A novel mechanism involving the cytoplasmic domain of band 3.. Journal of Clinical Investigation. 89(2). 686–692. 113 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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