Aspartilna proteaza (Serbian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Aspartilna proteaza" in Serbian language version.

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9nih.gov

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doi.org

Baldwin E. T.; Bhat T. N.; Gulnik S; et al. (1993). „Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design”. Proc. Natl. Acad. Sci. U.S.A. 90 (14): 6796—800. PMC 47019 . PMID 8393577. doi:10.1073/pnas.90.14.6796.
Szecsi PB (1992). „The aspartic proteases”. Scand. J. Clin. Lab. In vest. Suppl. 210: 5—22. PMID 1455179. doi:10.3109/00365519209104650.
Taylor R K; LaPointe CF (2000). „The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases”. J. Biol. Chem. 275 (2): 1502—10. PMID 10625704. doi:10.1074/jbc.275.2.1502.
Jarrell KF, Ng SY, Chaban B (2006). „Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications”. J. Mol. Microbiol. Bio technol. 11 (3): 167—91. PMID 16983194. doi:10.1159/000094053.
Jarrell KF, Bardy SL (2003). „Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae”. Mol. Microbiol. 50 (4): 1339—1347. PMID 14622420. doi:10.1046/j.1365-2958.2003.03758.x.
Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR (1987). „Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action”. Proc. Natl. Acad. Sci. U.S.A. 84 (20): 7009—13. PMC 299218 . PMID 3313384. doi:10.1073/pnas.84.20.7009.
Brik A, Wong CH (2003). „HIV-1 protease: mechanism and drug discovery”. Org. Biomol. Chem. 1 (1): 5—14. PMID 12929379. doi:10.1039/b208248a.
Hartsuck JA, Koelsch G, Remington SJ (1992). „The high-resolution crystal structure of porcine pepsinogen”. Proteins. 13 (1): 1—25. PMID 1594574. doi:10.1002/prot.340130102.
Sielecki AR, Fujinaga M, Read RJ, James MN (1991). „Refined structure of porcine pepsinogen at 1.8 A resolution”. J. Mol. Biol. 219 (4): 671—92. PMID 2056534. doi:10.1016/0022-2836(91)90664-R.

nih.gov

ncbi.nlm.nih.gov

Baldwin E. T.; Bhat T. N.; Gulnik S; et al. (1993). „Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design”. Proc. Natl. Acad. Sci. U.S.A. 90 (14): 6796—800. PMC 47019 . PMID 8393577. doi:10.1073/pnas.90.14.6796.
Szecsi PB (1992). „The aspartic proteases”. Scand. J. Clin. Lab. In vest. Suppl. 210: 5—22. PMID 1455179. doi:10.3109/00365519209104650.
Taylor R K; LaPointe CF (2000). „The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases”. J. Biol. Chem. 275 (2): 1502—10. PMID 10625704. doi:10.1074/jbc.275.2.1502.
Jarrell KF, Ng SY, Chaban B (2006). „Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications”. J. Mol. Microbiol. Bio technol. 11 (3): 167—91. PMID 16983194. doi:10.1159/000094053.
Jarrell KF, Bardy SL (2003). „Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae”. Mol. Microbiol. 50 (4): 1339—1347. PMID 14622420. doi:10.1046/j.1365-2958.2003.03758.x.
Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR (1987). „Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action”. Proc. Natl. Acad. Sci. U.S.A. 84 (20): 7009—13. PMC 299218 . PMID 3313384. doi:10.1073/pnas.84.20.7009.
Brik A, Wong CH (2003). „HIV-1 protease: mechanism and drug discovery”. Org. Biomol. Chem. 1 (1): 5—14. PMID 12929379. doi:10.1039/b208248a.
Hartsuck JA, Koelsch G, Remington SJ (1992). „The high-resolution crystal structure of porcine pepsinogen”. Proteins. 13 (1): 1—25. PMID 1594574. doi:10.1002/prot.340130102.
Sielecki AR, Fujinaga M, Read RJ, James MN (1991). „Refined structure of porcine pepsinogen at 1.8 A resolution”. J. Mol. Biol. 219 (4): 671—92. PMID 2056534. doi:10.1016/0022-2836(91)90664-R.