Enteropeptidas (Swedish Wikipedia)

Analysis of information sources in references of the Wikipedia article "Enteropeptidas" in Swedish language version.

refsWebsite

Global rank Swedish rank

22nih.gov

4^th place

17^th place

22doi.org

2^nd place

14^th place

1actachemscand.dk

low place

1sciencedirect.com

149^th place

211^th place

1harvard.edu

18^th place

162^nd place

1huji.ac.il

3,903^rd place

4,652^nd place

actachemscand.dk (Global: low place; Swedish: low place)

Yamashina I. (May 1956). ”The action of enterokinase on trypsinogen”. Biochim Biophys Acta 20 (2): sid. 433–4. doi:10.1016/0006-3002(56)90329-8. PMID 13328891. http://actachemscand.dk/pdf/acta_vol_10_p0739-0743.pdf.

doi.org (Global: 2^nd place; Swedish: 14^th place)

dx.doi.org

Kunitz M (March 1939). ”Formation of trypsin from crystalline trypsinogen by means of enterokinase”. J. Gen. Physiol. 22 (4): sid. 429–46. doi:10.1085/jgp.22.4.429. PMID 19873112.
”Enterokinase (enteropeptidase) : comparative aspects”. Trends Biochem. Sci. 14 (3): sid. 110–2. March 14, 1989. doi:10.1016/0968-0004(89)90133-3. PMID 2658218.
”Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli”. Prep. Biochem. Biotechnol. 37 (3): sid. 205–17. 2007. doi:10.1080/10826060701386695. PMID 17516250.
”Evolutionary families of peptidases”. Biochem. J. 290 (1): sid. 205–18. February 1993. doi:10.1042/bj2900205. PMID 8439290.
”Crystal structure of enteropeptidase light chain complex with an analog of the trypsinogen activation peptide”. J Mol Biol 292 (2): sid. 361–73. Sep 17, 1999. doi:10.1006/jmbi.1999.3089. PMID 10493881.
Yamashina I. (May 1956). ”The action of enterokinase on trypsinogen”. Biochim Biophys Acta 20 (2): sid. 433–4. doi:10.1016/0006-3002(56)90329-8. PMID 13328891. http://actachemscand.dk/pdf/acta_vol_10_p0739-0743.pdf.
”Activation of recombinant proenteropeptidase by duodenase”. FEBS Lett. 466 (2–3): sid. 295–9. Jan 28, 2000. doi:10.1016/s0014-5793(00)01092-9. PMID 10682847.
”Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes.”. J Biol Chem 276 (2): sid. 857–60. Jan 12, 2001. doi:10.1074/jbc.r000020200. PMID 11060317.
”Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains”. Proc Natl Acad Sci USA 91 (16): sid. 7588–92. August 2, 1994. doi:10.1073/pnas.91.16.7588. PMID 8052624. Bibcode: 1994PNAS...91.7588K.
”Bovine enterokinase. Purification, specificity and some molecular properties”. Biochemistry 16 (15): sid. 3354–60. July 26, 1977. doi:10.1021/bi00634a011. PMID 889800.
”The preparation and properties of bovine enterokinase”. J Biol Chem 254 (5): sid. 1677–83. March 10, 1979. doi:10.1016/S0021-9258(17)37826-2. PMID 762166.
”Incorporation of bovine enterokinase in reconstituted soybean phospholipid vesicles”. J Biol Chem 258 (5): sid. 3069–74. March 10, 1983. doi:10.1016/S0021-9258(18)32831-X. PMID 6338012.
”Bovine proenteroptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain”. J Biol Chem 272 (50): sid. 31293–300. December 12, 1997. doi:10.1074/jbc.272.50.31293. PMID 9395456.
”The preparation and properties of the catalytic subunit of bovine enterokinase”. J Biol Chem 259 (21): sid. 13195–8. November 10, 1984. doi:10.1016/S0021-9258(18)90676-9. PMID 6386810.
”Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase”. J Biol Chem 268 (31): sid. 23311–7. November 5, 1993. doi:10.1016/S0021-9258(19)49464-7. PMID 8226855.
”On the catalytic and binding sites of porcine enteropeptidase”. Biochim Biophys Acta 452 (2): sid. 488–96. December 8, 1976. doi:10.1016/0005-2744(76)90199-6. PMID 12810.
Terpe K (2003). ”Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems”. Appl Microbiol Biotechnol 60 (5): sid. 523–33. doi:10.1007/s00253-002-1158-6. PMID 12536251. http://wolfson.huji.ac.il/expression/local/tag-protein-fusions.pdf.
”Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound”. J Gen Physiol 19 (6): sid. 991–1007. Jul 20, 1936. doi:10.1085/jgp.19.6.991. PMID 19872978.
”Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency”. Am. J. Hum. Genet. 70 (1): sid. 20–5. January 2002. doi:10.1086/338456. PMID 11719902.
”Intestinal enterokinase deficiency”. Lancet 1 (7599): sid. 812–3. April 19, 1969. doi:10.1016/s0140-6736(69)92071-6. PMID 4180366.
”Malabsorption and growth failure due to intestinal enterokinase deficiency”. J. Pediatr. 78 (3): sid. 481–90. March 1971. doi:10.1016/s0022-3476(71)80231-7. PMID 4322674.
”Production of active recombinant human chymase from a construct containing the enterokinase cleavage site of trypsinogen in place of the native propeptide sequence”. Biol Chem Hoppe-Seyler 376 (11): sid. 681–84. Nov 1995. doi:10.1515/bchm3.1995.376.11.681. PMID 8962677.

harvard.edu (Global: 18^th place; Swedish: 162^nd place)

adsabs.harvard.edu

”Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains”. Proc Natl Acad Sci USA 91 (16): sid. 7588–92. August 2, 1994. doi:10.1073/pnas.91.16.7588. PMID 8052624. Bibcode: 1994PNAS...91.7588K.

huji.ac.il (Global: 3,903^rd place; Swedish: 4,652^nd place)

wolfson.huji.ac.il

Terpe K (2003). ”Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems”. Appl Microbiol Biotechnol 60 (5): sid. 523–33. doi:10.1007/s00253-002-1158-6. PMID 12536251. http://wolfson.huji.ac.il/expression/local/tag-protein-fusions.pdf.

nih.gov (Global: 4^th place; Swedish: 17^th place)

ncbi.nlm.nih.gov

Kunitz M (March 1939). ”Formation of trypsin from crystalline trypsinogen by means of enterokinase”. J. Gen. Physiol. 22 (4): sid. 429–46. doi:10.1085/jgp.22.4.429. PMID 19873112.
”Enterokinase (enteropeptidase) : comparative aspects”. Trends Biochem. Sci. 14 (3): sid. 110–2. March 14, 1989. doi:10.1016/0968-0004(89)90133-3. PMID 2658218.
”Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli”. Prep. Biochem. Biotechnol. 37 (3): sid. 205–17. 2007. doi:10.1080/10826060701386695. PMID 17516250.
”Evolutionary families of peptidases”. Biochem. J. 290 (1): sid. 205–18. February 1993. doi:10.1042/bj2900205. PMID 8439290.
”Crystal structure of enteropeptidase light chain complex with an analog of the trypsinogen activation peptide”. J Mol Biol 292 (2): sid. 361–73. Sep 17, 1999. doi:10.1006/jmbi.1999.3089. PMID 10493881.
Yamashina I. (May 1956). ”The action of enterokinase on trypsinogen”. Biochim Biophys Acta 20 (2): sid. 433–4. doi:10.1016/0006-3002(56)90329-8. PMID 13328891. http://actachemscand.dk/pdf/acta_vol_10_p0739-0743.pdf.
”Activation of recombinant proenteropeptidase by duodenase”. FEBS Lett. 466 (2–3): sid. 295–9. Jan 28, 2000. doi:10.1016/s0014-5793(00)01092-9. PMID 10682847.
”Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes.”. J Biol Chem 276 (2): sid. 857–60. Jan 12, 2001. doi:10.1074/jbc.r000020200. PMID 11060317.
”Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains”. Proc Natl Acad Sci USA 91 (16): sid. 7588–92. August 2, 1994. doi:10.1073/pnas.91.16.7588. PMID 8052624. Bibcode: 1994PNAS...91.7588K.
”Bovine enterokinase. Purification, specificity and some molecular properties”. Biochemistry 16 (15): sid. 3354–60. July 26, 1977. doi:10.1021/bi00634a011. PMID 889800.
”The preparation and properties of bovine enterokinase”. J Biol Chem 254 (5): sid. 1677–83. March 10, 1979. doi:10.1016/S0021-9258(17)37826-2. PMID 762166.
”Incorporation of bovine enterokinase in reconstituted soybean phospholipid vesicles”. J Biol Chem 258 (5): sid. 3069–74. March 10, 1983. doi:10.1016/S0021-9258(18)32831-X. PMID 6338012.
”Bovine proenteroptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain”. J Biol Chem 272 (50): sid. 31293–300. December 12, 1997. doi:10.1074/jbc.272.50.31293. PMID 9395456.
”The preparation and properties of the catalytic subunit of bovine enterokinase”. J Biol Chem 259 (21): sid. 13195–8. November 10, 1984. doi:10.1016/S0021-9258(18)90676-9. PMID 6386810.
”Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase”. J Biol Chem 268 (31): sid. 23311–7. November 5, 1993. doi:10.1016/S0021-9258(19)49464-7. PMID 8226855.
”On the catalytic and binding sites of porcine enteropeptidase”. Biochim Biophys Acta 452 (2): sid. 488–96. December 8, 1976. doi:10.1016/0005-2744(76)90199-6. PMID 12810.
Terpe K (2003). ”Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems”. Appl Microbiol Biotechnol 60 (5): sid. 523–33. doi:10.1007/s00253-002-1158-6. PMID 12536251. http://wolfson.huji.ac.il/expression/local/tag-protein-fusions.pdf.
”Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound”. J Gen Physiol 19 (6): sid. 991–1007. Jul 20, 1936. doi:10.1085/jgp.19.6.991. PMID 19872978.
”Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency”. Am. J. Hum. Genet. 70 (1): sid. 20–5. January 2002. doi:10.1086/338456. PMID 11719902.
”Intestinal enterokinase deficiency”. Lancet 1 (7599): sid. 812–3. April 19, 1969. doi:10.1016/s0140-6736(69)92071-6. PMID 4180366.
”Malabsorption and growth failure due to intestinal enterokinase deficiency”. J. Pediatr. 78 (3): sid. 481–90. March 1971. doi:10.1016/s0022-3476(71)80231-7. PMID 4322674.
”Production of active recombinant human chymase from a construct containing the enterokinase cleavage site of trypsinogen in place of the native propeptide sequence”. Biol Chem Hoppe-Seyler 376 (11): sid. 681–84. Nov 1995. doi:10.1515/bchm3.1995.376.11.681. PMID 8962677.

sciencedirect.com (Global: 149^th place; Swedish: 211^th place)

Rawlings, Neil D.; Salvesen, Guy (2013). Handbook of Proteolytic Enzymes (3rd). ISBN 978-0-12-382219-2. http://www.sciencedirect.com/science/book/9780123822192. Läst 20 februari 2014.

Enteropeptidas (Swedish Wikipedia)

actachemscand.dk (Global: low place; Swedish: low place)

doi.org (Global: 2nd place; Swedish: 14th place)

dx.doi.org

harvard.edu (Global: 18th place; Swedish: 162nd place)