Enteropeptidase (Galician Wikipedia)

Analysis of information sources in references of the Wikipedia article "Enteropeptidase" in Galician language version.

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Global rank Galician rank

22nih.gov

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22doi.org

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1actachemscand.dk

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1sciencedirect.com

149^th place

162^nd place

1harvard.edu

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1huji.ac.il

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1archive.org

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actachemscand.dk

Yamashina I. (maio de 1956). "The action of enterokinase on trypsinogen" (PDF). Biochim Biophys Acta 20 (2): 433–4. PMID 13328891. doi:10.1016/0006-3002(56)90329-8.

archive.org

Haworth JC, Gourley B, Hadorn B, Sumida C (marzo de 1971). "Malabsorption and growth failure due to intestinal enterokinase deficiency". J. Pediatr. 78 (3): 481–90. PMID 4322674. doi:10.1016/s0022-3476(71)80231-7.

doi.org

dx.doi.org

Kunitz M (marzo de 1939). "Formation of trypsin from crystalline trypsinogen by means of enterokinase". J. Gen. Physiol. 22 (4): 429–46. PMC 2141988. PMID 19873112. doi:10.1085/jgp.22.4.429.
Light A, Janska H (14 de marzo de 1989). "Enterokinase (enteropeptidase) : comparative aspects". Trends Biochem. Sci. 14 (3): 110–2. PMID 2658218. doi:10.1016/0968-0004(89)90133-3.
Huang L, Ruan H, Gu W, Xu Z, Cen P, Fan L (2007). "Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli". Prep. Biochem. Biotechnol. 37 (3): 205–17. PMID 17516250. doi:10.1080/10826060701386695.
Rawlings ND, Barrett AJ (febreiro de 1993). "Evolutionary families of peptidases". Biochem. J. 290 (1): 205–18. PMC 1132403. PMID 8439290. doi:10.1042/bj2900205.
Lu D, Fütterer K, Korolev S, Zheng X, Tan K, Waksman G, Sadler JE (17 de setembro de 1999). "Crystal structure of enteropeptidase light chain complex with an analog of the trypsinogen activation peptide". J Mol Biol 292 (2): 361–73. PMID 10493881. doi:10.1006/jmbi.1999.3089.
Yamashina I. (maio de 1956). "The action of enterokinase on trypsinogen" (PDF). Biochim Biophys Acta 20 (2): 433–4. PMID 13328891. doi:10.1016/0006-3002(56)90329-8.
Zamolodchikova TS, Sokolova EA, Lu D, Sadler JE (28 de xaneiro de 2000). "Activation of recombinant proenteropeptidase by duodenase". FEBS Lett. 466 (2–3): 295–9. PMID 10682847. doi:10.1016/s0014-5793(00)01092-9.
Hooper JD, Clements JA, Quiqley JP, Antalis TM (12 de xaneiro de 2001). "Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes.". J Biol Chem 276 (2): 857–60. PMID 11060317. doi:10.1074/jbc.r000020200.
Kitamoto Y, Yuan X, Wu Q, McCourt DW, Sadler JE (2 de agosto de 1994). "Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains". Proc Natl Acad Sci USA 91 (16): 7588–92. Bibcode:1994PNAS...91.7588K. PMC 44447. PMID 8052624. doi:10.1073/pnas.91.16.7588.
Anderson LE, Walsh KA, Neurath H (26 de xullo de 1977). "Bovine enterokinase. Purification, specificity and some molecular properties". Biochemistry 16 (15): 3354–60. PMID 889800. doi:10.1021/bi00634a011.
Liepnieks JJ, Light A (10 de marzo de 1979). "The preparation and properties of bovine enterokinase". J Biol Chem 254 (5): 1677–83. PMID 762166. doi:10.1016/S0021-9258(17)37826-2.
Fonseca P, Light A (10 de marzo de 1983). "Incorporation of bovine enterokinase in reconstituted soybean phospholipid vesicles". J Biol Chem 258 (5): 3069–74. PMID 6338012. doi:10.1016/S0021-9258(18)32831-X.
Lu D, Yuan X, Zheng X, Sadler JE (12 de decembro de 1997). "Bovine proenteroptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain". J Biol Chem 272 (50): 31293–300. PMID 9395456. doi:10.1074/jbc.272.50.31293.
Light A, Fonseca P (10 de novembro de 1984). "The preparation and properties of the catalytic subunit of bovine enterokinase". J Biol Chem 259 (21): 13195–8. PMID 6386810. doi:10.1016/S0021-9258(18)90676-9.
LaVallie ER, Rehemtulla A, Racie LA, DiBlasio EA, Ferenz C, Grant KL, Light A, McCoy JM (5 de novembro de 1993). "Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase". J Biol Chem 268 (31): 23311–7. PMID 8226855. doi:10.1016/S0021-9258(19)49464-7.
Baratti J, Maroux S (8 de decembro de 1976). "On the catalytic and binding sites of porcine enteropeptidase". Biochim Biophys Acta 452 (2): 488–96. PMID 12810. doi:10.1016/0005-2744(76)90199-6.
Terpe K (2003). "Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems" (PDF). Appl Microbiol Biotechnol 60 (5): 523–33. PMID 12536251. doi:10.1007/s00253-002-1158-6.
Kunitz M, Northrop JH (20 de xullo de 1936). "Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound". J Gen Physiol 19 (6): 991–1007. PMC 2141477. PMID 19872978. doi:10.1085/jgp.19.6.991.
Holzinger A, Maier EM, Bück C, Mayerhofer PU, Kappler M, Haworth JC, Moroz SP, Hadorn HB, Sadler JE, Roscher AA (xaneiro de 2002). "Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency". Am. J. Hum. Genet. 70 (1): 20–5. PMC 384888. PMID 11719902. doi:10.1086/338456.
Hadorn B, Tarlow MJ, Lloyd JK, Wolff OH (19 de abril de 1969). "Intestinal enterokinase deficiency". Lancet 1 (7599): 812–3. PMID 4180366. doi:10.1016/s0140-6736(69)92071-6.
Haworth JC, Gourley B, Hadorn B, Sumida C (marzo de 1971). "Malabsorption and growth failure due to intestinal enterokinase deficiency". J. Pediatr. 78 (3): 481–90. PMID 4322674. doi:10.1016/s0022-3476(71)80231-7.
Wang ZM, Rubin H, Schechter NM (novembro de 1995). "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): 681–84. PMID 8962677. doi:10.1515/bchm3.1995.376.11.681.

harvard.edu

adsabs.harvard.edu

Kitamoto Y, Yuan X, Wu Q, McCourt DW, Sadler JE (2 de agosto de 1994). "Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains". Proc Natl Acad Sci USA 91 (16): 7588–92. Bibcode:1994PNAS...91.7588K. PMC 44447. PMID 8052624. doi:10.1073/pnas.91.16.7588.

huji.ac.il

wolfson.huji.ac.il

Terpe K (2003). "Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems" (PDF). Appl Microbiol Biotechnol 60 (5): 523–33. PMID 12536251. doi:10.1007/s00253-002-1158-6.

nih.gov

ncbi.nlm.nih.gov

Kunitz M (marzo de 1939). "Formation of trypsin from crystalline trypsinogen by means of enterokinase". J. Gen. Physiol. 22 (4): 429–46. PMC 2141988. PMID 19873112. doi:10.1085/jgp.22.4.429.
Light A, Janska H (14 de marzo de 1989). "Enterokinase (enteropeptidase) : comparative aspects". Trends Biochem. Sci. 14 (3): 110–2. PMID 2658218. doi:10.1016/0968-0004(89)90133-3.
Huang L, Ruan H, Gu W, Xu Z, Cen P, Fan L (2007). "Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli". Prep. Biochem. Biotechnol. 37 (3): 205–17. PMID 17516250. doi:10.1080/10826060701386695.
Rawlings ND, Barrett AJ (febreiro de 1993). "Evolutionary families of peptidases". Biochem. J. 290 (1): 205–18. PMC 1132403. PMID 8439290. doi:10.1042/bj2900205.
Lu D, Fütterer K, Korolev S, Zheng X, Tan K, Waksman G, Sadler JE (17 de setembro de 1999). "Crystal structure of enteropeptidase light chain complex with an analog of the trypsinogen activation peptide". J Mol Biol 292 (2): 361–73. PMID 10493881. doi:10.1006/jmbi.1999.3089.
Yamashina I. (maio de 1956). "The action of enterokinase on trypsinogen" (PDF). Biochim Biophys Acta 20 (2): 433–4. PMID 13328891. doi:10.1016/0006-3002(56)90329-8.
Zamolodchikova TS, Sokolova EA, Lu D, Sadler JE (28 de xaneiro de 2000). "Activation of recombinant proenteropeptidase by duodenase". FEBS Lett. 466 (2–3): 295–9. PMID 10682847. doi:10.1016/s0014-5793(00)01092-9.
Hooper JD, Clements JA, Quiqley JP, Antalis TM (12 de xaneiro de 2001). "Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes.". J Biol Chem 276 (2): 857–60. PMID 11060317. doi:10.1074/jbc.r000020200.
Kitamoto Y, Yuan X, Wu Q, McCourt DW, Sadler JE (2 de agosto de 1994). "Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains". Proc Natl Acad Sci USA 91 (16): 7588–92. Bibcode:1994PNAS...91.7588K. PMC 44447. PMID 8052624. doi:10.1073/pnas.91.16.7588.
Anderson LE, Walsh KA, Neurath H (26 de xullo de 1977). "Bovine enterokinase. Purification, specificity and some molecular properties". Biochemistry 16 (15): 3354–60. PMID 889800. doi:10.1021/bi00634a011.
Liepnieks JJ, Light A (10 de marzo de 1979). "The preparation and properties of bovine enterokinase". J Biol Chem 254 (5): 1677–83. PMID 762166. doi:10.1016/S0021-9258(17)37826-2.
Fonseca P, Light A (10 de marzo de 1983). "Incorporation of bovine enterokinase in reconstituted soybean phospholipid vesicles". J Biol Chem 258 (5): 3069–74. PMID 6338012. doi:10.1016/S0021-9258(18)32831-X.
Lu D, Yuan X, Zheng X, Sadler JE (12 de decembro de 1997). "Bovine proenteroptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain". J Biol Chem 272 (50): 31293–300. PMID 9395456. doi:10.1074/jbc.272.50.31293.
Light A, Fonseca P (10 de novembro de 1984). "The preparation and properties of the catalytic subunit of bovine enterokinase". J Biol Chem 259 (21): 13195–8. PMID 6386810. doi:10.1016/S0021-9258(18)90676-9.
LaVallie ER, Rehemtulla A, Racie LA, DiBlasio EA, Ferenz C, Grant KL, Light A, McCoy JM (5 de novembro de 1993). "Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase". J Biol Chem 268 (31): 23311–7. PMID 8226855. doi:10.1016/S0021-9258(19)49464-7.
Baratti J, Maroux S (8 de decembro de 1976). "On the catalytic and binding sites of porcine enteropeptidase". Biochim Biophys Acta 452 (2): 488–96. PMID 12810. doi:10.1016/0005-2744(76)90199-6.
Terpe K (2003). "Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems" (PDF). Appl Microbiol Biotechnol 60 (5): 523–33. PMID 12536251. doi:10.1007/s00253-002-1158-6.
Kunitz M, Northrop JH (20 de xullo de 1936). "Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound". J Gen Physiol 19 (6): 991–1007. PMC 2141477. PMID 19872978. doi:10.1085/jgp.19.6.991.
Holzinger A, Maier EM, Bück C, Mayerhofer PU, Kappler M, Haworth JC, Moroz SP, Hadorn HB, Sadler JE, Roscher AA (xaneiro de 2002). "Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency". Am. J. Hum. Genet. 70 (1): 20–5. PMC 384888. PMID 11719902. doi:10.1086/338456.
Hadorn B, Tarlow MJ, Lloyd JK, Wolff OH (19 de abril de 1969). "Intestinal enterokinase deficiency". Lancet 1 (7599): 812–3. PMID 4180366. doi:10.1016/s0140-6736(69)92071-6.
Haworth JC, Gourley B, Hadorn B, Sumida C (marzo de 1971). "Malabsorption and growth failure due to intestinal enterokinase deficiency". J. Pediatr. 78 (3): 481–90. PMID 4322674. doi:10.1016/s0022-3476(71)80231-7.
Wang ZM, Rubin H, Schechter NM (novembro de 1995). "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): 681–84. PMID 8962677. doi:10.1515/bchm3.1995.376.11.681.

sciencedirect.com

Rawlings, Neil D.; Salvesen, Guy (2013). Handbook of Proteolytic Enzymes (3ª ed.). ISBN 978-0-12-382219-2. Consultado o 20 de febreiro de 2014.