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Volumn 20, Issue 11, 2003, Pages 1940-1945

Aspartic Proteinase Phylogeny and the Origin of Pregnancy-Associated Glycoproteins

Author keywords

Aspartic proteinase; PAGs; Pregnancy associated glycoprotiens

Indexed keywords

ASPARTIC PROTEINASE; PEPSIN A; PEPSIN F; PREGNANCY ASSOCIATED PROTEIN; UNCLASSIFIED DRUG;

EID: 0242666273     PISSN: 07374038     EISSN: None     Source Type: Journal    
DOI: 10.1093/molbev/msg217     Document Type: Article
Times cited : (50)

References (31)
  • 2
    • 0027070658 scopus 로고
    • Cellular proteolysis: An overview
    • Barrett, A. J. 1992. Cellular proteolysis: an overview. Ann. N.Y. Acad. Sci. 674:1-15.
    • (1992) Ann. N.Y. Acad. Sci , vol.674 , pp. 1-15
    • Barrett, A.J.1
  • 4
    • 0034816573 scopus 로고    scopus 로고
    • An aspartic proteinase expressed in the yolk sac and neonatal stomach of the mouse
    • Chen, X., C. S. Rosenfeld, R. M. Roberts, and J. A. Green. 2001. An aspartic proteinase expressed in the yolk sac and neonatal stomach of the mouse. Biol. Reprod. 65:1092-1101.
    • (2001) Biol. Reprod. , vol.65 , pp. 1092-1101
    • Chen, X.1    Rosenfeld, C.S.2    Roberts, R.M.3    Green, J.A.4
  • 5
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies, D. R. 1990. The structure and function of the aspartic proteinases. Annu. Rev. Biophys. Chem. 19:189-215.
    • (1990) Annu. Rev. Biophys. Chem. , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 6
    • 0028278857 scopus 로고
    • X-ray analysis at 2.0 Å resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen
    • Dealwis, C. G., C. Frazao, M. Badasso et al. (12 co-authors). 1994. X-ray analysis at 2.0 Å resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen. J. Mol. Biol. 236:342-360.
    • (1994) J. Mol. Biol. , vol.236 , pp. 342-360
    • Dealwis, C.G.1    Frazao, C.2    Badasso, M.3
  • 7
    • 0026683982 scopus 로고
    • X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins
    • Dhanaraj, V., C. G. Dealwis, C. Frazao et al. (18 co-authors). 1992. X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins. Nature 357:466-472.
    • (1992) Nature , vol.357 , pp. 466-472
    • Dhanaraj, V.1    Dealwis, C.G.2    Frazao, C.3
  • 8
    • 0033767520 scopus 로고    scopus 로고
    • Caprinee pregnancy-associated glycoproteins (PAG): Their cloning, expression and evolutionary relationship to other PAG
    • Garbayo, J. M., J. A. Green, M. Mannekin, J.-F. Beckers, D. O. Kiesling, A. D. Ealy, and R. M. Roberts. 2000. Caprinee pregnancy-associated glycoproteins (PAG): their cloning, expression and evolutionary relationship to other PAG. Mol. Reprod. Dev. 57:311-322.
    • (2000) Mol. Reprod. Dev. , vol.57 , pp. 311-322
    • Garbayo, J.M.1    Green, J.A.2    Mannekin, M.3    Beckers, J.-F.4    Kiesling, D.O.5    Ealy, A.D.6    Roberts, R.M.7
  • 9
    • 0034030627 scopus 로고    scopus 로고
    • Pregnancy-associated glycoproteins exhibit spatially and temporally distinct expression patterns during pregnancy
    • Green, A. A., S. Xie, X. Quan, B. Bao, X. Gan, N. Mathialagan, J.-F. Beckers, and R. M. Roberts. 2000. Pregnancy-associated glycoproteins exhibit spatially and temporally distinct expression patterns during pregnancy. Biol. Reprod. 62:1624-1631.
    • (2000) Biol. Reprod. , vol.62 , pp. 1624-1631
    • Green, A.A.1    Xie, S.2    Quan, X.3    Bao, B.4    Gan, X.5    Mathialagan, N.6    Beckers, J.-F.7    Roberts, R.M.8
  • 10
    • 0030734575 scopus 로고    scopus 로고
    • A simple method for estimating the parameter of substitution rate variation among sites
    • Gu, X., and J. Zhang. 1997. A simple method for estimating the parameter of substitution rate variation among sites. Mol. Biol. Evol. 14:1106-1113.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 1106-1113
    • Gu, X.1    Zhang, J.2
  • 11
    • 0032834519 scopus 로고    scopus 로고
    • Isolation, purification, and characterization of pregnancy-specific protein B from elk and moose placenta
    • Huang, F., D. C. Cockrell, T. R. Stephenson, J. H. Noyes, and R. G. Sasser. 1999. Isolation, purification, and characterization of pregnancy-specific protein B from elk and moose placenta. Biol. Reprod. 61:1056-1061.
    • (1999) Biol. Reprod. , vol.61 , pp. 1056-1061
    • Huang, F.1    Cockrell, D.C.2    Stephenson, T.R.3    Noyes, J.H.4    Sasser, R.G.5
  • 13
    • 0023764283 scopus 로고
    • Pattern of nucleotide substitution at major histocompatibility complex class I loci reveals overdominant selection
    • Hughes, A. L., and M. Nei. 1988. Pattern of nucleotide substitution at major histocompatibility complex class I loci reveals overdominant selection. Nature 335:167-170.
    • (1988) Nature , vol.335 , pp. 167-170
    • Hughes, A.L.1    Nei, M.2
  • 14
    • 0034724185 scopus 로고    scopus 로고
    • Adaptive diversification within a large family of recently duplicated, placentally expressed genes
    • Hughes, A. L., J. A. Green, J. M. Garbayo, and R. M. Roberts. 2000. Adaptive diversification within a large family of recently duplicated, placentally expressed genes. Proc. Natl. Acad. Sci. USA 97:3319-3323.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3319-3323
    • Hughes, A.L.1    Green, J.A.2    Garbayo, J.M.3    Roberts, R.M.4
  • 15
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones, D. T., W. R. Taylor, and J. M. Thomton. 1992. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8:275-282.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thomton, J.M.3
  • 16
    • 0019296687 scopus 로고
    • A simple method for estimating evolutionary rates of base substitutions through comparative studies of nucleotide sequences
    • Kimura, M. 1980. A simple method for estimating evolutionary rates of base substitutions through comparative studies of nucleotide sequences. J. Mol. Evol. 16:111-120.
    • (1980) J. Mol. Evol. , vol.16 , pp. 111-120
    • Kimura, M.1
  • 17
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar, S., K. Tamura, I. B. Jakobsen, and M. Nei. 2001. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17:1244-1245.
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 18
    • 0022005270 scopus 로고
    • A new method for estimating synonymous and nonsynonymous rates of nucleotide substitution considering the relative likelihood of nucleotide and codon changes
    • Li, W.-H., C.-I. Wu, and C.-C. Luo. 1985. A new method for estimating synonymous and nonsynonymous rates of nucleotide substitution considering the relative likelihood of nucleotide and codon changes. Mol. Biol. Evol. 2:150-174.
    • (1985) Mol. Biol. Evol. , vol.2 , pp. 150-174
    • Li, W.-H.1    Wu, C.-I.2    Luo, C.-C.3
  • 19
    • 0025935211 scopus 로고
    • X-ray analyses of aspartic proteinases IV: Structure and refinement at 2.2 Å resolution of bovine chymosin
    • Newman, M., M. Saffro, C. Frazao, G. Khan, A. Zdanov, I. J. Tickle, T. L. Blundell, and N. Andreeva. 1991. X-ray analyses of aspartic proteinases IV: structure and refinement at 2.2 Å resolution of bovine chymosin. J. Mol. Biol. 221:1295-1309.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1295-1309
    • Newman, M.1    Saffro, M.2    Frazao, C.3    Khan, G.4    Zdanov, A.5    Tickle, I.J.6    Blundell, T.L.7    Andreeva, N.8
  • 20
    • 0028338820 scopus 로고
    • Estimation of the number of amino acid substitutions per site when the substitution rate varies among sites
    • Ota, T., and M. Nei. 1994. Estimation of the number of amino acid substitutions per site when the substitution rate varies among sites. J. Mol. Evol. 38:642-643.
    • (1994) J. Mol. Evol. , vol.38 , pp. 642-643
    • Ota, T.1    Nei, M.2
  • 21
    • 0026660413 scopus 로고
    • A simple method for estimating and testing minimum-evolution trees
    • Rzhetsky, A., and M. Nei. 1992. A simple method for estimating and testing minimum-evolution trees. Mol. Biol. Evol. 9:945-967.
    • (1992) Mol. Biol. Evol. , vol.9 , pp. 945-967
    • Rzhetsky, A.1    Nei, M.2
  • 22
    • 0025354599 scopus 로고
    • Molecular and crystal structures of monolithic porcine pepsin refined at 1.8 Å resolution
    • Sielecki, A. R., A. A. Fedorov, A. Boodhoo, N. S. Andreeva, and M. N. G. James. 1990. Molecular and crystal structures of monolithic porcine pepsin refined at 1.8 Å resolution. J. Mol. Biol. 214:143-170.
    • (1990) J. Mol. Biol. , vol.214 , pp. 143-170
    • Sielecki, A.R.1    Fedorov, A.A.2    Boodhoo, A.3    Andreeva, N.S.4    James, M.N.G.5
  • 23
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies
    • Strimmer, K., and A. von Haeseler. 1996. Quartet puzzling: a quartet maximum likelihood method for reconstructing tree topologies. Mol. Biol. Evol. 13:964-969.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 964-969
    • Strimmer, K.1    Von Haeseler, A.2
  • 25
    • 0029060733 scopus 로고
    • Porcine pregnancy-associated glycoproteins: New members of the aspartic proteinase gene family expressed in trophectoderm
    • Szafranska, B., S. Xie, J. Green, and R. M. Roberts. 1995. Porcine pregnancy-associated glycoproteins: new members of the aspartic proteinase gene family expressed in trophectoderm. Biol. Reprod. 5:21-28.
    • (1995) Biol. Reprod. , vol.5 , pp. 21-28
    • Szafranska, B.1    Xie, S.2    Green, J.3    Roberts, R.M.4
  • 26
    • 0017843307 scopus 로고
    • Structural evidence for gene duplication in the evolution of the acid proteases
    • Tang, J., M. N. James, I. N. Hsu, J. A. Jenkins, and T. L. Blundell. 1978. Structural evidence for gene duplication in the evolution of the acid proteases. Nature 271:618-621.
    • (1978) Nature , vol.271 , pp. 618-621
    • Tang, J.1    James, M.N.2    Hsu, I.N.3    Jenkins, J.A.4    Blundell, T.L.5
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and D. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, D.J.3
  • 28
    • 0030679766 scopus 로고    scopus 로고
    • The diversity and evolutionary relationships of the pregnancy-associated glycoproteins, an aspartic proteinase subfamily consisting of many trophoblast-expressed genes
    • Xie, S., J. Green, J. B. Bixby, B. Szafranska, J. C. DeMartini, S. Hecht, and R. M. Roberts. 1997. The diversity and evolutionary relationships of the pregnancy-associated glycoproteins, an aspartic proteinase subfamily consisting of many trophoblast-expressed genes. Proc. Natl. Acad. Sci. USA 94:12809-12816.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12809-12816
    • Xie, S.1    Green, J.2    Bixby, J.B.3    Szafranska, B.4    DeMartini, J.C.5    Hecht, S.6    Roberts, R.M.7
  • 29
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity
    • Yan, R., M. J. Bienkowski, M. E. Shuck et al. (15 co-authors). 1999. Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity. Nature 402:533-537.
    • (1999) Nature , vol.402 , pp. 533-537
    • Yan, R.1    Bienkowski, M.J.2    Shuck, M.E.3
  • 30
    • 0028820333 scopus 로고
    • A new method of inference of ancestral nucleotide and amino acid sequences
    • Yang, Z., S. Kumar, and M. Nei. 1995. A new method of inference of ancestral nucleotide and amino acid sequences. Genetics 141:1641-1650.
    • (1995) Genetics , vol.141 , pp. 1641-1650
    • Yang, Z.1    Kumar, S.2    Nei, M.3
  • 31
    • 0031025677 scopus 로고    scopus 로고
    • Accuracies of ancestral amino acid sequences inferred by the parsimony, likelihood, and distance methods
    • Zhang, J., and M. Nei. 1997. Accuracies of ancestral amino acid sequences inferred by the parsimony, likelihood, and distance methods. J. Mol. Evol. 44(Suppl. 1):S139-S146.
    • (1997) J. Mol. Evol. , vol.44 , Issue.SUPPL. 1
    • Zhang, J.1    Nei, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.