L.L. David

48 papers receiving 1.5k citations

Peers

L.L. David
Comparison fields: 5 of 109
  • Clinical Biochemistry 200
  • Cell Biology 389
  • Sensory Systems 88
  • Molecular Biology 1.1k
  • Molecular Medicine 66
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Norihiro Azuma Japan
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Citations per year

Countries citing papers authored by L.L. David

Since Specialization
Citations

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

Fields of papers citing papers by L.L. David

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authors

The 25 scholars most cited alongside L.L. David, linked wherever they have co-authored with each other. Click a name or a connecting line to browse the papers they share.

Border = papers with L.L. David Line = papers co-authored together L.L. David links everyone, so they are left out of the graph.

All Works

20 of 20 papers shown

Showing the 20 most-cited of 48 papers — load more, or switch the sort, to bring in the rest.

#Work
1 2006247
2 2010100
3 201598
4 199395
5
Calcium-activated proteolysis in the lens nucleus during selenite cataractogenesis.
198487
6 199385
7
Cataract and the acceleration of calpain-induced beta-crystallin insolubilization occurring during normal maturation of rat lens.
199475
8 198764
9 198460
10 199758
11 199951
12 200048
13
Regional distribution of free calcium in selenite cataract: relation to calpain II.
198741
14 198240
15 201939
16
Amelioration of cataracts and proteolysis in cultured lenses by cysteine protease inhibitor E64.
199135
17 201033
18 199528
19 201526
20 198924

About L.L. David

L.L. David is a scholar working on Molecular Biology, Cell Biology, Physiology, Molecular Medicine and Endocrinology, having authored 48 papers that have together received 1.5k indexed citations. Recurring topics across this work include Connexins and lens biology (22 papers), Calpain Protease Function and Regulation (11 papers), Biochemical effects in animals (8 papers), Antibiotic Resistance in Bacteria (8 papers), Selenium in Biological Systems (4 papers), Infections and bacterial resistance (3 papers), Endodontics and Root Canal Treatments (2 papers) and Vibrio bacteria research studies (2 papers). The work is most often cited by research in Clinical Biochemistry (200 citations), Cell Biology (389 citations), Sensory Systems (88 citations), Molecular Biology (1.1k citations) and Molecular Medicine (66 citations). L.L. David has collaborated with scholars based in United States, France and Democratic Republic of the Congo. Frequent co-authors include Thomas R. Shearer, Miyuki Azuma, Phillip A. Wilmarth, M. Shih, Surendra Dasari, Stephen Tanner, Vineet Bafna, Pavel A. Pevzner, Michael A. Riviere and Srinivasa R. Nagalla. Their work appears in journals such as Investigative Ophthalmology & Visual Science, Experimental Eye Research, Current Eye Research, Research in Veterinary Science and Journal of Biological Chemistry.

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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