Table 2.
Top 15 co-citation analysis of cited reference on EP research.
| Rank | References | Title | Source | Affiliation | Country | Co-citations |
|---|---|---|---|---|---|---|
| 1 | Laemmli (44) | Cleavage of structural proteins during the assembly of the head of bacteriophage T4 | Nature | MRC Laboratory of Molecular Biology | UK | 118 |
| 2 | Kunitz (10) | Formation of trypsin from crystalline trypsinogen by means of enterokinase | J Gen Physiol | The Rockefeller Institute for Medical Research | USA | 88 |
| 3 | Maroux et al. (35) | Purification and specificity of porcine enterokinase | J Biol Chem | National de la Recherche scientifique | France | 88 |
| 4 | Hadorn et al. (19) | Intestinal enterokinase deficiency | Lancet | University of Berge | Switzerland | 85 |
| 5 | Bradford (45) | A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding | Anal Biochem | University of Georgia | Georgia | 79 |
| 6 | Lowry et al. (48) | Protein measurement with the Folin phenol reagent | J Biol Chem | Washington University School of Medicine | USA | 58 |
| 7 | Kitamoto et al. (16) | Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains | Proc Natl Acad Sci USA | Washington University School of Medicine | USA | 54 |
| 8 | LaVallie et al. (49) | Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase | J Biol Chem | Genetics Institute | UK | 53 |
| 9 | LaVallie et al. (46) | A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm | Genetics Institute | UK | 49 | |
| 10 | Nordstro (47) | Rat enterokinase-effect of ions and localizationin intestine | Biochimica ET Bioph ACTA |
University of Lund | Sweden | 49 |
| 11 | Liepnieks and Light (50) | The preparation and properties of bovine enterokinase | J Biol Chem | Purdue University | Indiana | 48 |
| 12 | Lu et al. (51) | Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain | J Biol Chem | Washington University | USA | 48 |
| 13 | Louvard et al. (52) | On the preparation and some properties of closed membrane vesicles from hog duodenal and jejunal brush border | Biochim Biophys Acta | National de la Recherche scientifique | France | 45 |
| 14 | Collins-racie et al. (53) | Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA | Biotechnology | Genetics Institute | USA | 45 |
| 15 | Lu et al. (54) | Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide | J Biol Chem | Washington University | USA | 45 |