Sally S. Twining

4.5k total citations · 1 hit paper
89 papers, 3.8k citations indexed

About

Sally S. Twining is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Cancer Research. According to data from OpenAlex, Sally S. Twining has authored 89 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 29 papers in Radiology, Nuclear Medicine and Imaging and 28 papers in Cancer Research. Recurrent topics in Sally S. Twining's work include Protease and Inhibitor Mechanisms (28 papers), Corneal Surgery and Treatments (19 papers) and Blood Coagulation and Thrombosis Mechanisms (8 papers). Sally S. Twining is often cited by papers focused on Protease and Inhibitor Mechanisms (28 papers), Corneal Surgery and Treatments (19 papers) and Blood Coagulation and Thrombosis Mechanisms (8 papers). Sally S. Twining collaborates with scholars based in United States, United Kingdom and Philippines. Sally S. Twining's co-authors include M. Zouhair Atassi, Jianbo Yue, Chella S. David, Xiaoye Zhou, Patricia Wilson, Robert S. Feder, Lili Zhou, Luis A. Díaz, Zhi Liu and Robert M. Senior and has published in prestigious journals such as Cell, Journal of Biological Chemistry and Journal of Clinical Investigation.

In The Last Decade

Sally S. Twining

89 papers receiving 3.7k citations

Hit Papers

Fluorescein isothiocyanate-labeled casein assay for prote... 1984 2026 1998 2012 1984 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
Sally S. Twining United States 33 1.5k 1.1k 665 541 433 89 3.8k
Jonathan H. Lass United States 28 463 0.3× 1.1k 1.0× 149 0.2× 743 1.4× 1.0k 2.4× 65 3.0k
Eiichi Nakayama Japan 44 2.2k 1.5× 803 0.7× 295 0.4× 288 0.5× 147 0.3× 184 7.2k
M. Stangassinger Germany 30 1.1k 0.7× 270 0.2× 227 0.3× 108 0.2× 224 0.5× 100 4.0k
L Riddle United States 20 1.3k 0.8× 824 0.7× 141 0.2× 80 0.1× 630 1.5× 26 3.2k
Félix Elortza Spain 31 2.4k 1.5× 226 0.2× 520 0.8× 284 0.5× 89 0.2× 168 3.9k
Efrat Kessler Israel 36 2.0k 1.3× 129 0.1× 641 1.0× 109 0.2× 209 0.5× 88 3.7k
Victoria H. Freedman United States 23 1.5k 1.0× 374 0.3× 292 0.4× 127 0.2× 40 0.1× 40 4.2k
Richard G. DiScipio United States 35 1.1k 0.7× 279 0.2× 448 0.7× 301 0.6× 44 0.1× 69 4.1k
William R. Green United States 29 683 0.4× 330 0.3× 110 0.2× 136 0.3× 501 1.2× 110 3.0k
Angela Granelli‐Piperno United States 39 1.6k 1.1× 320 0.3× 952 1.4× 760 1.4× 45 0.1× 67 7.0k

Countries citing papers authored by Sally S. Twining

Since Specialization
Citations

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

Fields of papers citing papers by Sally S. Twining

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Sally S. Twining. 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 Sally S. Twining. The network helps show where Sally S. Twining may publish in the future.

Co-authorship network of co-authors of Sally S. Twining

This figure shows the co-authorship network connecting the top 25 collaborators of Sally S. Twining. A scholar is included among the top collaborators of Sally S. Twining 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 Sally S. Twining. Sally S. Twining 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.
Twining, Sally S. & Debra J. Warejcka. (2012). Thrombin Increases Human Corneal Fibroblast Expression Of The Chemokines, CXCL1, CCL2, IL-6, IL-8, CXCL10 And CCL13. Investigative Ophthalmology & Visual Science. 53(14). 1088–1088. 1 indexed citations
3.
Barnes, Jarrod W., et al.. (2012). Latency-associated Peptide of Transforming Growth Factor-β1 Is Not Subject to Physiological Mannose Phosphorylation. Journal of Biological Chemistry. 287(10). 7526–7534. 9 indexed citations
4.
Narayan, Malathi, Shama P. Mirza, & Sally S. Twining. (2011). Identification of phosphorylation sites on extracellular corneal epithelial cell maspin. PROTEOMICS. 11(8). 1382–1390. 10 indexed citations
5.
Bernstein, Audrey M., et al.. (2007). Urokinase Receptor Cleavage: A Crucial Step in Fibroblast to Myofibroblast Differentiation. Investigative Ophthalmology & Visual Science. 48(13). 1498–1498. 1 indexed citations
6.
Bernstein, Audrey M., et al.. (2007). Urokinase Receptor Cleavage: A Crucial Step in Fibroblast-to-Myofibroblast Differentiation. Molecular Biology of the Cell. 18(7). 2716–2727. 76 indexed citations
7.
Twining, Sally S., et al.. (2005). The Fibrinolysis Inhibitor α2-Antiplasmin in the Human Cornea. Current Eye Research. 30(12). 1097–1103. 4 indexed citations
8.
Rogers, Christian, et al.. (2004). The effects of sub-solar levels of UV-A and UV-B on rabbit corneal and lens epithelial cells. Experimental Eye Research. 78(5). 1007–1014. 55 indexed citations
9.
Twining, Sally S., Igor Y. Goryshin, Archna Bhasin, & William S. Reznikoff. (2001). Functional Characterization of Arginine 30, Lysine 40, and Arginine 62 in Tn5 Transposase. Journal of Biological Chemistry. 276(25). 23135–23143. 15 indexed citations
10.
Liu, Zhi, Xiaoye Zhou, Steven D. Shapiro, et al.. (2000). The Serpin α1-Proteinase Inhibitor Is a Critical Substrate for Gelatinase B/MMP-9 In Vivo. Cell. 102(5). 647–655. 307 indexed citations
11.
Liu, Zhi, Steven D. Shapiro, Xiaoye Zhou, et al.. (2000). A critical role for neutrophil elastase in experimental bullous pemphigoid. Journal of Clinical Investigation. 105(1). 113–123. 151 indexed citations
12.
McGill, Craig, et al.. (2000). Blood Glucose Laboratory for First-year Medical Students. Journal of the American Dietetic Association. 100(5). 570–572. 1 indexed citations
13.
Bošković, Goran & Sally S. Twining. (1998). Local control of α1-proteinase inhibitor levels: regulation of α1-proteinase inhibitor in the human cornea by growth factors and cytokines. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1403(1). 37–46. 37 indexed citations
14.
Li, Yuhong, Lili Zhou, Sally S. Twining, Joel Sugar, & Jianbo Yue. (1998). Involvement of Sp1 Elements in the Promoter Activity of the α1-Proteinase Inhibitor Gene. Journal of Biological Chemistry. 273(16). 9959–9965. 33 indexed citations
15.
Twining, Sally S., et al.. (1997). Vitamin A Deficiency Alters Rat Neutrophil Function ,. Journal of Nutrition. 127(4). 558–565. 58 indexed citations
16.
Twining, Sally S., et al.. (1996). Retinol Is Sequestered in the Bone Marrow of Vitamin A-Deficient Rats. Journal of Nutrition. 126(6). 1618–1626. 13 indexed citations
17.
Twining, Sally S., et al.. (1996). Neutrophil cathepsin G is specifically decreased under vitamin A deficiency. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1317(2). 112–118. 11 indexed citations
18.
Twining, Sally S., et al.. (1994). Alpha 2-macroglobulin is present in and synthesized by the cornea.. PubMed. 35(8). 3226–33. 28 indexed citations
19.
Twining, Sally S.. (1994). Regulation of Proteolytic Activity in Tissues. Critical Reviews in Biochemistry and Molecular Biology. 29(5). 315–383. 80 indexed citations
20.
Twining, Sally S., et al.. (1989). Localization and quantification of a-1-proteinase inhibitor in the human cornea. Current Eye Research. 8(4). 389–395. 10 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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