E. L. Hogan

3.3k total citations · 1 hit paper
65 papers, 2.7k citations indexed

About

E. L. Hogan is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, E. L. Hogan has authored 65 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 16 papers in Physiology and 15 papers in Cell Biology. Recurrent topics in E. L. Hogan's work include Calpain Protease Function and Regulation (12 papers), Glycosylation and Glycoproteins Research (11 papers) and Spinal Cord Injury Research (8 papers). E. L. Hogan is often cited by papers focused on Calpain Protease Function and Regulation (12 papers), Glycosylation and Glycoproteins Research (11 papers) and Spinal Cord Injury Research (8 papers). E. L. Hogan collaborates with scholars based in United States, Pakistan and Taiwan. E. L. Hogan's co-authors include Chung Y. Hsu, J. Douglas Balentine, H R Maricq, Naren L. Banik, Bruce Α. Freeman, Joseph S. Beckman, K. C. Joseph, Perry V. Halushka, Somsankar Dasgupta and Seymour Greenfield and has published in prestigious journals such as Journal of Biological Chemistry, Neurology and Stroke.

In The Last Decade

E. L. Hogan

65 papers receiving 2.7k citations

Hit Papers

A model of focal ischemic stroke in the rat: reproducible... 1986 2026 1999 2012 1986 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
E. L. Hogan United States 28 1.1k 654 542 473 459 65 2.7k
Bruce A. Citron United States 34 1.3k 1.2× 739 1.1× 378 0.7× 671 1.4× 536 1.2× 95 3.5k
Yuiko Morita‐Fujimura United States 26 1.8k 1.7× 514 0.8× 739 1.4× 611 1.3× 254 0.6× 39 3.3k
Tetsuya Nagayama United States 22 1.2k 1.1× 753 1.2× 400 0.7× 338 0.7× 198 0.4× 38 2.6k
Kensuke Murakami Japan 23 1.2k 1.1× 517 0.8× 713 1.3× 595 1.3× 206 0.4× 76 2.7k
Shunya Takizawa Japan 27 925 0.8× 385 0.6× 480 0.9× 427 0.9× 219 0.5× 143 2.9k
Teng‐Nan Lin Taiwan 28 1.4k 1.3× 583 0.9× 878 1.6× 307 0.6× 171 0.4× 62 3.0k
Raymond F. Regan United States 39 1.9k 1.7× 403 0.6× 349 0.6× 1.1k 2.4× 346 0.8× 80 3.4k
Armando P. Signore United States 22 1.2k 1.1× 478 0.7× 484 0.9× 341 0.7× 124 0.3× 25 2.5k
Raymond F. White United States 18 855 0.8× 331 0.5× 634 1.2× 274 0.6× 200 0.4× 28 2.2k
Masahiko Tsuji Japan 10 739 0.7× 547 0.8× 1.2k 2.1× 425 0.9× 146 0.3× 43 2.8k

Countries citing papers authored by E. L. Hogan

Since Specialization
Citations

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

Fields of papers citing papers by E. L. Hogan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of E. L. Hogan

This figure shows the co-authorship network connecting the top 25 collaborators of E. L. Hogan. A scholar is included among the top collaborators of E. L. Hogan 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 E. L. Hogan. E. L. Hogan 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.
Banik, Naren L., Donald C. Shields, Swapan K. Ray, et al.. (1998). Role of calpain in spinal cord injury: effects of calpain and free radical inhibitors.. PubMed. 844. 131–7. 57 indexed citations
2.
Banik, Naren L., Donald C. Shields, Swapan K. Ray, et al.. (1998). Role of Calpain in Spinal Cord Injury: Effects of Calpain and Free Radical Inhibitorsa. Annals of the New York Academy of Sciences. 844(1). 131–137. 54 indexed citations
3.
Hogan, E. L., et al.. (1998). Activation of JNK/SAPK in Primary Glial Cultures: II. Differential Activation of Kinase Isoforms Corresponds to Their Differential Expression. Neurochemical Research. 23(2). 219–225. 26 indexed citations
4.
Matzelle, Denise, et al.. (1998). New inhibitors of calpain prevent degradation of cytoskeletal and myelin proteins in spinal cord in vitro. Journal of Neuroscience Research. 51(2). 218–222. 39 indexed citations
5.
Goust, J M, et al.. (1995). Calpain secreted by activated human lymphoid cells degrades myelin. Journal of Neuroscience Research. 42(2). 259–265. 42 indexed citations
6.
Salyan, Mary Ellen K., S.J. Steele, Reiji Kannagi, et al.. (1994). A Revised Structure for the Disialosyl Globo-Series Gangliosides of Human Erythrocytes and Chicken Skeletal Muscle. Archives of Biochemistry and Biophysics. 312(1). 125–134. 12 indexed citations
7.
Banik, Naren L., et al.. (1994). Peptide bond specificity of calpain: Proteolysis of human myelin basic protein. Journal of Neuroscience Research. 37(4). 489–496. 40 indexed citations
8.
Dasgupta, Somsankar, et al.. (1994). Branched Monosialo Gangliosides of the Lacto-Series Isolated from Bovine Erythrocytes: Characterization of a Novel Ganglioside, NeuGc-Isooctaosylceramide. Archives of Biochemistry and Biophysics. 310(2). 373–384. 13 indexed citations
9.
Xu, Jian, et al.. (1992). Protective Effect of Methylprednisolone on Vascular Injury in Rat Spinal Cord Injury. Journal of Neurotrauma. 9(3). 245–253. 35 indexed citations
10.
Banik, Naren L., et al.. (1991). Calcium‐activated neutral proteinase (CANP; calpain) activity in Schwann cells: Immunofluorescence localization and compartmentation of μ‐ and mCANP. Journal of Neuroscience Research. 29(3). 346–354. 20 indexed citations
11.
Xu, Jian, et al.. (1991). A Sensitive Fluorometric Method for Measurement of Vascular Permeability in Spinal Cord Injury. Journal of Neurotrauma. 8(2). 149–156. 7 indexed citations
12.
Banik, Naren L., Arun K. Chakrabarti, & E. L. Hogan. (1990). Purification of an endogenous 68 kD inhibitor of calcium‐activated neutral proteinase (CANP) from bovine brain: Immunoblot identification and characterization. Journal of Neuroscience Research. 25(1). 119–124. 14 indexed citations
13.
Hsu, Chung Y., et al.. (1988). Temporal profile of thromboxane-prostacyclin imbalance in experimental spinal cord injury. Journal of the Neurological Sciences. 83(1). 55–62. 25 indexed citations
14.
Konat�, G., et al.. (1988). Expression of myelin protein genes in quaking mouse brain. Journal of Neuroscience Research. 20(1). 19–22. 18 indexed citations
15.
Chakrabarti, Arun K., et al.. (1988). Calcium‐activated neutral proteinase in rat brain myelin and subcellular fractions. Journal of Neuroscience Research. 20(3). 351–358. 50 indexed citations
16.
Lee, William A., et al.. (1987). Therapeutic Model for Experimental Spinal Cord Injury in the Rat: I. Mortality and Motor Deficit. PubMed. 4(3). 149–159. 46 indexed citations
17.
Konat�, G., et al.. (1987). Increased turnover of myelin proteolipid protein in quaking mouse brain. Metabolic Brain Disease. 2(2). 113–116. 3 indexed citations
18.
Konat�, G., et al.. (1986). Synthesis and acylation of myelin proteolipid protein in quaking mouse brain. Metabolic Brain Disease. 1(4). 241–247. 6 indexed citations
19.
Hogan, E. L., et al.. (1984). Glycosphingolipid biosynthesis during myogenesis in vitro a comparative study. The Society for Neuroscience Abstracts. 10(2). 1180. 2 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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