M. Shih
- Cell Biology top 2%
- Calpain Protease Function and Regulation 16
- Hemoglobin structure and function 2
- Clinical Biochemistry top 2%
- Molecular Biology top 10%
- Connexins and lens biology 21
- Heat shock proteins research 8
- Physiology top 10%
- Biochemical effects in animals 7
- Erythrocyte Function and Pathophysiology 2
- Ophthalmology top 5%
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- Meat and Animal Product Quality 3
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- Hemoglobinopathies and Related Disorders 2
M. Shih
24 papers receiving 1.1k citations
Peers
Comparison fields: 5 of 78
- Cell Biology 482
- Clinical Biochemistry 166
- Molecular Biology 1.0k
- Physiology 270
- Ophthalmology 67
Countries citing papers authored by M. Shih
This map shows the geographic impact of M. Shih'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 M. Shih with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites M. Shih more than expected).
Fields of papers citing papers by M. Shih
This network shows the impact of papers produced by M. Shih. 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 M. Shih. The network helps show where M. Shih may publish in the future.
Co-authorship network
The 25 scholars most cited alongside M. Shih, linked wherever they have co-authored with each other. Click a name or a connecting line to browse the papers they share.
All Works
| # | Work | ||
|---|---|---|---|
| 1 | 2005 | 23 | |
| 2 | 2004 | 5 | |
| 3 | Different Expression Patterns for Human Css1 and Css2 During Lens Maturation | 2003 | 1 |
| 4 | 2003 | 18 | |
| 5 | 2002 | 47 | |
| 6 | 2001 | 98 | |
| 7 | 2001 | 29 | |
| 8 | Influence of specific regions in Lp82 calpain on protein stability, activity, and localization within lens. | 2000 | 29 |
| 9 | 1999 | 28 | |
| 10 | 1999 | 37 | |
| 11 | 1998 | 39 | |
| 12 | 1998 | 35 | |
| 13 | 1998 | 224 | |
| 14 | 1997 | 172 | |
| 15 | 1997 | 10 | |
| 16 | 1996 | 22 | |
| 17 | 1996 | 6 | |
| 18 | 1995 | 28 | |
| 19 | 1990 | 76 | |
| 20 | 1987 | 16 |
About M. Shih
M. Shih is a scholar working on Cell Biology, Physiology, Molecular Biology, Animal Science and Zoology and Periodontics, having authored 24 papers that have together received 1.2k indexed citations. Recurring topics across this work include Connexins and lens biology (21 papers), Calpain Protease Function and Regulation (16 papers), Heat shock proteins research (8 papers), Biochemical effects in animals (7 papers), Meat and Animal Product Quality (3 papers), Erythrocyte Function and Pathophysiology (2 papers), Hemoglobinopathies and Related Disorders (2 papers) and Hemoglobin structure and function (2 papers). The work is most often cited by research in Cell Biology (482 citations), Clinical Biochemistry (166 citations), Molecular Biology (1.0k citations), Physiology (270 citations) and Ophthalmology (67 citations). M. Shih has collaborated with scholars based in United States, Japan and France. Frequent co-authors include Thomas R. Shearer, Kirsten J. Lampi, Larry L. David, Chiho Fukiage, Hong Ma, Jean B. Smith, David L. Smith, L.L. David, Larry L. David and Miyuki Azuma. Their work appears in journals such as Experimental Eye Research, Current Eye Research, Journal of Biological Chemistry, Molecular & Cellular Proteomics and Investigative Ophthalmology & Visual Science.
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.