Marietta L. Harrison

4.4k total citations
70 papers, 3.8k citations indexed

About

Marietta L. Harrison is a scholar working on Molecular Biology, Immunology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Marietta L. Harrison has authored 70 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 24 papers in Immunology and 22 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Marietta L. Harrison's work include Monoclonal and Polyclonal Antibodies Research (22 papers), T-cell and B-cell Immunology (15 papers) and Glycosylation and Glycoproteins Research (14 papers). Marietta L. Harrison is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (22 papers), T-cell and B-cell Immunology (15 papers) and Glycosylation and Glycoproteins Research (14 papers). Marietta L. Harrison collaborates with scholars based in United States, China and United Kingdom. Marietta L. Harrison's co-authors include Robert L. Geahlen, Philip S. Low, Jill E. Hutchcroft, E G Krebs, Thomas F. Zioncheck, J E Casnellie, K E Hellström, Thomas M. Yankee, Lakhu Keshvara and Michael Furlong and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Immunology.

In The Last Decade

Marietta L. Harrison

69 papers receiving 3.7k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Marietta L. Harrison United States	32	2.0k	1.3k	756	658	468	70	3.8k
Gary L. Schieven United States	42	2.5k 1.3×	2.2k 1.7×	710 0.9×	281 0.4×	286 0.6×	94	5.5k
Joseph Fargnoli United States	34	2.3k 1.2×	826 0.6×	297 0.4×	306 0.5×	372 0.8×	56	3.9k
Anna Maria Brunati Italy	40	3.0k 1.5×	695 0.5×	282 0.4×	708 1.1×	630 1.3×	145	4.8k
James M. Trevillyan United States	34	2.4k 1.2×	1.7k 1.3×	405 0.5×	241 0.4×	189 0.4×	68	4.1k
Yoshito Ihara Japan	41	3.9k 2.0×	1.7k 1.3×	386 0.5×	539 0.8×	917 2.0×	132	5.3k
Andree Blaukat Germany	31	2.1k 1.1×	360 0.3×	275 0.4×	309 0.5×	334 0.7×	94	3.6k
Ronald L. Wange United States	34	1.9k 1.0×	2.9k 2.2×	597 0.8×	114 0.2×	230 0.5×	53	4.4k
Román Herrera United States	26	6.7k 3.4×	860 0.7×	521 0.7×	471 0.7×	812 1.7×	42	8.6k
Bruce Seligmann United States	30	1.4k 0.7×	977 0.7×	327 0.4×	279 0.4×	106 0.2×	66	2.7k
Tohru Kamata Japan	31	2.7k 1.3×	1.2k 0.9×	150 0.2×	656 1.0×	464 1.0×	74	4.6k

Countries citing papers authored by Marietta L. Harrison

Since Specialization

Citations

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

Fields of papers citing papers by Marietta L. Harrison

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Marietta L. Harrison. 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 Marietta L. Harrison. The network helps show where Marietta L. Harrison may publish in the future.

Co-authorship network of co-authors of Marietta L. Harrison

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

All Works

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20 of 20 papers shown

Chen, Chen, Lingli Deng, Siwei Wei, et al.. (2015). Exploring Metabolic Profile Differences between Colorectal Polyp Patients and Controls Using Seemingly Unrelated Regression. Journal of Proteome Research. 14(6). 2492–2499. 24 indexed citations

Paris, Leela L., Jacob A. Galán, Su Sien Ong, et al.. (2010). Regulation of Syk by Phosphorylation on Serine in the Linker Insert. Journal of Biological Chemistry. 285(51). 39844–39854. 25 indexed citations

Jennings, Benjamin C., et al.. (2008). 2-Bromopalmitate and 2-(2-hydroxy-5-nitro-benzylidene)-benzo[b]thiophen-3-one inhibit DHHC-mediated palmitoylation in vitro. Journal of Lipid Research. 50(2). 233–242. 168 indexed citations

Oh, Hyun-Ju, Elif Özkırımlı, Kavita Shah, Marietta L. Harrison, & Robert L. Geahlen. (2007). Generation of an Analog-sensitive Syk Tyrosine Kinase for the Study of Signaling Dynamics from the B Cell Antigen Receptor. Journal of Biological Chemistry. 282(46). 33760–33768. 21 indexed citations

Zheng, Yanan, V. Balakrishnan, Gregery T. Buzzard, et al.. (2005). Modeling and analysis of early events in T-lymphocyte antigen-activated intracellular-signaling pathways. Journal of Computational and Applied Mathematics. 184(1). 320–341. 7 indexed citations

Hu, Xiangxiang, et al.. (2002). The oxygen-substituted palmitic acid analogue, 13-oxypalmitic acid, inhibits Lck localization to lipid rafts and T cell signaling. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1589(2). 140–150. 30 indexed citations

Geahlen, Robert L., et al.. (2002). The Lck SH3 Domain Negatively Regulates Localization to Lipid Rafts through an Interaction with c-Cbl. Journal of Biological Chemistry. 277(7). 5683–5691. 43 indexed citations

Yankee, Thomas M., et al.. (2002). Regulation of Signaling in B Cells through the Phosphorylation of Syk on Linker Region Tyrosines. Journal of Biological Chemistry. 277(35). 31703–31714. 76 indexed citations

Ma, Haiyan, et al.. (2001). Visualization of Syk-Antigen Receptor Interactions Using Green Fluorescent Protein: Differential Roles for Syk and Lyn in the Regulation of Receptor Capping and Internalization. The Journal of Immunology. 166(3). 1507–1516. 92 indexed citations

10.

Hong, Julie, et al.. (1999). The engagement of β1 integrins on promonocytic cells promotes phosphorylation of Syk and formation of a protein complex containing Lyn and β1 integrin. European Journal of Immunology. 29(5). 1426–1434. 1 indexed citations

11.

Oberlies, Nicholas H., et al.. (1997). The Annonaceous acetogenin bullatacin is cytotoxic against multidrug-resistant human mammary adenocarcinoma cells. Cancer Letters. 115(1). 73–79. 131 indexed citations

12.

Furlong, Michael, et al.. (1997). Identification of the major sites of autophosphorylation of the murine protein-tyrosine kinase Syk. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1355(2). 177–190. 106 indexed citations

13.

Geahlen, Robert L., et al.. (1996). The Protein-tyrosine Kinase Lck Associates with and Is Phosphorylated by Cdc2. Journal of Biological Chemistry. 271(44). 27517–27523. 22 indexed citations

14.

Furlong, Michael, et al.. (1996). Syk, Activated by Cross-linking the B-cell Antigen Receptor, Localizes to the Cytosol Where It Interacts with and Phosphorylates α-Tubulin on Tyrosine. Journal of Biological Chemistry. 271(9). 4755–4762. 133 indexed citations

15.

Burg, Debra L., et al.. (1994). Interactions of Lyn with the antigen receptor during B cell activation.. Journal of Biological Chemistry. 269(45). 28136–28142. 54 indexed citations

16.

Nadler, Monica J. S., et al.. (1993). Treatment of T cells with 2-hydroxymyristic acid inhibits the myristoylation and alters the stability of p56lck. Biochemistry. 32(35). 9250–9255. 48 indexed citations

17.

Harrison, Marietta L., et al.. (1992). Resealing of Protein Tyrosine Kinase Substrates into Human Erythrocytes by Rapid Freezing and Thawing in Liquid Nitrogen. Advances in experimental medicine and biology. 326. 111–117. 2 indexed citations

18.

Smith, Jean B., et al.. (1991). Identification of tyrosine 67 in bovine brain myelin basic protein as a specific phosphorylation site for thymus p56lck. Biochemical and Biophysical Research Communications. 178(3). 1393–1399. 15 indexed citations

19.

Geahlen, Robert L., et al.. (1986). Detection of protein kinase activity in sodium dodecyl sulfate-polyacrylamide gels. Analytical Biochemistry. 153(1). 151–158. 77 indexed citations

20.

Casnellie, J E, Marietta L. Harrison, Linda J. Pike, K E Hellström, & E G Krebs. (1982). Phosphorylation of synthetic peptides by a tyrosine protein kinase from the particulate fraction of a lymphoma cell line.. Proceedings of the National Academy of Sciences. 79(2). 282–286. 183 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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