Craig Freeman

4.6k total citations
73 papers, 3.8k citations indexed

About

Craig Freeman is a scholar working on Cell Biology, Molecular Biology and Physiology. According to data from OpenAlex, Craig Freeman has authored 73 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Cell Biology, 42 papers in Molecular Biology and 19 papers in Physiology. Recurrent topics in Craig Freeman's work include Proteoglycans and glycosaminoglycans research (42 papers), Glycosylation and Glycoproteins Research (26 papers) and Carbohydrate Chemistry and Synthesis (17 papers). Craig Freeman is often cited by papers focused on Proteoglycans and glycosaminoglycans research (42 papers), Glycosylation and Glycoproteins Research (26 papers) and Carbohydrate Chemistry and Synthesis (17 papers). Craig Freeman collaborates with scholars based in Australia, United States and United Kingdom. Craig Freeman's co-authors include Christopher R. Parish, John J. Hopwood, Mark D. Hulett, Kathryn J. Brown, Rohan T. Baker, Matthew Harris, William B. Cowden, Charmaine J. Simeonovic, Andrew Ziolkowski and Graham A.R. Johnston and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Clinical Investigation and Nature Medicine.

In The Last Decade

Craig Freeman

73 papers receiving 3.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Craig Freeman Australia 33 2.2k 2.1k 660 561 398 73 3.8k
Nancy Dahms United States 33 2.5k 1.1× 1.4k 0.7× 680 1.0× 1.3k 2.3× 107 0.3× 82 4.0k
Ehud Razin Israel 37 2.3k 1.0× 756 0.4× 226 0.3× 679 1.2× 186 0.5× 116 4.4k
Marco Maccarana Sweden 29 2.7k 1.2× 2.2k 1.0× 465 0.7× 183 0.3× 451 1.1× 56 3.7k
Gregory David United States 48 4.5k 2.0× 2.4k 1.1× 155 0.2× 626 1.1× 711 1.8× 107 7.0k
Tamotsu Kanzaki Japan 31 1.2k 0.5× 551 0.3× 356 0.5× 855 1.5× 141 0.4× 230 4.0k
Atsushi Irie Japan 33 1.9k 0.9× 424 0.2× 162 0.2× 275 0.5× 197 0.5× 89 3.7k
J J Cassiman Belgium 34 1.9k 0.9× 1.5k 0.7× 89 0.1× 198 0.4× 347 0.9× 66 3.4k
Elizabeth C. Arner United States 35 1.2k 0.5× 640 0.3× 150 0.2× 223 0.4× 389 1.0× 64 4.1k
Eun Sook Hwang South Korea 34 1.9k 0.8× 1.0k 0.5× 101 0.2× 495 0.9× 59 0.1× 106 4.3k
Evgenia Karousou Italy 28 1.6k 0.7× 1.6k 0.7× 195 0.3× 87 0.2× 98 0.2× 63 2.8k

Countries citing papers authored by Craig Freeman

Since Specialization
Citations

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

Fields of papers citing papers by Craig Freeman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Craig Freeman

This figure shows the co-authorship network connecting the top 25 collaborators of Craig Freeman. A scholar is included among the top collaborators of Craig Freeman 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 Craig Freeman. Craig Freeman 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.
Simeonovic, Charmaine J., Lora Starrs, Debra Brown, et al.. (2018). Loss of intra-islet heparan sulfate is a highly sensitive marker of type 1 diabetes progression in humans. PLoS ONE. 13(2). e0191360–e0191360. 29 indexed citations
2.
Boyle, Michelle J., Mark A. Skidmore, Benjamin K. Dickerman, et al.. (2017). Identification of Heparin Modifications and Polysaccharide Inhibitors of Plasmodium falciparum Merozoite Invasion That Have Potential for Novel Drug Development. Antimicrobial Agents and Chemotherapy. 61(11). 22 indexed citations
3.
Mak, Jcw, et al.. (2015). S-maltoheptaose targets syndecan-bound effectors to reduce smoking-related neutrophilic inflammation. Scientific Reports. 5(1). 12945–12945. 7 indexed citations
4.
Cui, Hao, Craig Freeman, Glenn A. Jacobson, & David H. Small. (2013). Proteoglycans in the central nervous system: Role in development, neural repair, and Alzheimer's disease. IUBMB Life. 65(2). 108–120. 72 indexed citations
5.
Yuan, Ling, Jie Hu, Yan Luo, et al.. (2012). Upregulation of heparanase in high-glucose-treated endothelial cells promotes endothelial cell migration and proliferation and correlates with Akt and extracellular-signal-regulated kinase phosphorylation.. PubMed. 18. 1684–95. 23 indexed citations
6.
Ziolkowski, Andrew, et al.. (2011). Heparan sulfate and heparanase play key roles in mouse β cell survival and autoimmune diabetes. Journal of Clinical Investigation. 122(1). 132–141. 124 indexed citations
7.
Garg, Hari G., Lunyin Yu, Craig Freeman, et al.. (2010). Effect of carboxyl-reduced heparin on the growth inhibition of bovine pulmonary artery smooth muscle cells. Carbohydrate Research. 345(9). 1084–1087. 7 indexed citations
8.
Garg, Hari G., Lunyin Yu, Craig Freeman, et al.. (2008). Significance of the 2-O-sulfo group of l-iduronic acid residues in heparin on the growth inhibition of bovine pulmonary artery smooth muscle cells. Carbohydrate Research. 343(14). 2406–2410. 8 indexed citations
9.
Ellyard, Julia I., et al.. (2007). Eotaxin Selectively Binds Heparin. Journal of Biological Chemistry. 282(20). 15238–15247. 67 indexed citations
10.
Warren, Hilary S., Allison Jones, Craig Freeman, Jayaram Bettadapura, & Christopher R. Parish. (2005). Evidence That the Cellular Ligand for the Human NK Cell Activation Receptor NKp30 Is Not a Heparan Sulfate Glycosaminoglycan. The Journal of Immunology. 175(1). 207–212. 35 indexed citations
11.
Joyce, Johanna A., Craig Freeman, Nicole Meyer-Morse, Christopher R. Parish, & Douglas Hanahan. (2005). A functional heparan sulfate mimetic implicates both heparanase and heparan sulfate in tumor angiogenesis and invasion in a mouse model of multistage cancer. Oncogene. 24(25). 4037–4051. 135 indexed citations
12.
Freeman, Craig, Ligong Liu, Martin G. Banwell, et al.. (2005). Use of Sulfated Linked Cyclitols as Heparan Sulfate Mimetics to Probe the Heparin/Heparan Sulfate Binding Specificity of Proteins. Journal of Biological Chemistry. 280(10). 8842–8849. 50 indexed citations
13.
McColl, Bradley, Megan E. Baldwin, Sally Roufail, et al.. (2003). Plasmin Activates the Lymphangiogenic Growth Factors VEGF-C and VEGF-D. The Journal of Experimental Medicine. 198(6). 863–868. 164 indexed citations
14.
Hulett, Mark D., J. Hornby, Stephen Ohms, et al.. (2000). Identification of Active-Site Residues of the Pro-Metastatic Endoglycosidase Heparanase. Biochemistry. 39(51). 15659–15667. 132 indexed citations
15.
Parish, Christopher R., et al.. (1999). Identification of sulfated oligosaccharide-based inhibitors of tumor growth and metastasis using novel in vitro assays for angiogenesis and heparanase activity.. PubMed. 59(14). 3433–41. 352 indexed citations
16.
Scott, Hamish S., Xiao-Hui Guo, Craig Freeman, et al.. (1995). Cloning of the sulphamidase gene and identification of mutations in Sanfilippo A syndrome. Nature Genetics. 11(4). 465–467. 118 indexed citations
17.
Freeman, Craig & John J. Hopwood. (1992). Lysosomal Degradation of Heparin and Heparan Sulphate. Advances in experimental medicine and biology. 313. 121–134. 30 indexed citations
18.
Brooks, Doug A., G. S. Harper, G J Gibson, et al.. (1992). Hurler syndrome: A patient with abnormally high levels of α-l-iduronidase protein. Biochemical Medicine and Metabolic Biology. 47(3). 211–220. 19 indexed citations
19.
Bielicki, Julie, et al.. (1990). Human liver iduronate-2-sulphatase. Purification, characterization and catalytic properties. Biochemical Journal. 271(1). 75–86. 52 indexed citations
20.
Turner, John V., A. David Ward, & Craig Freeman. (1978). The mutagenic screening of fourteen imidazo compounds using a modified ames' test. Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis. 57(2). 135–139. 6 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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