메뉴 건너뛰기




Volumn 392, Issue 1, 2009, Pages 154-165

Structural Insights into the Protease-like Antigen Plasmodium falciparum SERA5 and Its Noncanonical Active-Site Serine

Author keywords

Plasmodium falciparum; SERA5; structure; X ray crystallography

Indexed keywords

ANTIGEN; CYSTEINE PROTEINASE; PROTEINASE; SERINE; SERINE REPEAT ANTIGEN 5; UNCLASSIFIED DRUG;

EID: 68949172361     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.007     Document Type: Article
Times cited : (35)

References (61)
  • 1
    • 0024259125 scopus 로고
    • Protein p126: a parasitophorous vacuole antigen associated with the release of Plasmodium falciparum merozoites
    • Delplace P., Bhatia A., Cagnard M., Camus D., Colombet G., Debrabant A., et al. Protein p126: a parasitophorous vacuole antigen associated with the release of Plasmodium falciparum merozoites. Biol. Cell. 64 (1988) 215-221
    • (1988) Biol. Cell. , vol.64 , pp. 215-221
    • Delplace, P.1    Bhatia, A.2    Cagnard, M.3    Camus, D.4    Colombet, G.5    Debrabant, A.6
  • 2
    • 0033057904 scopus 로고    scopus 로고
    • Antibodies reactive with the N-terminal domain of Plasmodium falciparum serine repeat antigen inhibit cell proliferation by agglutinating merozoites and schizonts
    • Pang X.L., Mitamura T., and Horii T. Antibodies reactive with the N-terminal domain of Plasmodium falciparum serine repeat antigen inhibit cell proliferation by agglutinating merozoites and schizonts. Infect. Immun. 67 (1999) 1821-1827
    • (1999) Infect. Immun. , vol.67 , pp. 1821-1827
    • Pang, X.L.1    Mitamura, T.2    Horii, T.3
  • 3
    • 51449114441 scopus 로고    scopus 로고
    • Malarial proteases and host cell egress: an 'emerging' cascade
    • Blackman M.J. Malarial proteases and host cell egress: an 'emerging' cascade. Cell. Microbiol. 10 (2008) 1925-1934
    • (2008) Cell. Microbiol. , vol.10 , pp. 1925-1934
    • Blackman, M.J.1
  • 4
    • 0037033084 scopus 로고    scopus 로고
    • Serine repeat antigen (SERA5) is predominantly expressed among the SERA multigene family of Plasmodium falciparum, and the acquired antibody titers correlate with serum inhibition of the parasite growth
    • Aoki S., Li J., Itagaki S., Okech B.A., Egwang T.G., Matsuoka H., et al. Serine repeat antigen (SERA5) is predominantly expressed among the SERA multigene family of Plasmodium falciparum, and the acquired antibody titers correlate with serum inhibition of the parasite growth. J. Biol. Chem. 277 (2002) 47533-47540
    • (2002) J. Biol. Chem. , vol.277 , pp. 47533-47540
    • Aoki, S.1    Li, J.2    Itagaki, S.3    Okech, B.A.4    Egwang, T.G.5    Matsuoka, H.6
  • 5
    • 0023734159 scopus 로고
    • Amino acid sequence of the serine-repeat antigen (SERA) of Plasmodium falciparum determined from cloned cDNA
    • Bzik D.J., Li W.B., Horii T., and Inselburg J. Amino acid sequence of the serine-repeat antigen (SERA) of Plasmodium falciparum determined from cloned cDNA. Mol. Biochem. Parasitol. 30 (1988) 279-288
    • (1988) Mol. Biochem. Parasitol. , vol.30 , pp. 279-288
    • Bzik, D.J.1    Li, W.B.2    Horii, T.3    Inselburg, J.4
  • 7
    • 10744231797 scopus 로고    scopus 로고
    • Enzymic, phylogenetic, and structural characterization of the unusual papain-like protease domain of Plasmodium falciparum SERA5
    • Hodder A.N., Drew D.R., Epa V.C., Delorenzi M., Bourgon R., Miller S.K., et al. Enzymic, phylogenetic, and structural characterization of the unusual papain-like protease domain of Plasmodium falciparum SERA5. J. Biol. Chem. 278 (2003) 48169-48177
    • (2003) J. Biol. Chem. , vol.278 , pp. 48169-48177
    • Hodder, A.N.1    Drew, D.R.2    Epa, V.C.3    Delorenzi, M.4    Bourgon, R.5    Miller, S.K.6
  • 8
    • 0037033116 scopus 로고    scopus 로고
    • A subset of Plasmodium falciparum SERA genes are expressed and appear to play an important role in the erythrocytic cycle
    • Miller S.K., Good R.T., Drew D.R., Delorenzi M., Sanders P.R., Hodder A.N., et al. A subset of Plasmodium falciparum SERA genes are expressed and appear to play an important role in the erythrocytic cycle. J. Biol. Chem. 277 (2002) 47524-47532
    • (2002) J. Biol. Chem. , vol.277 , pp. 47524-47532
    • Miller, S.K.1    Good, R.T.2    Drew, D.R.3    Delorenzi, M.4    Sanders, P.R.5    Hodder, A.N.6
  • 9
    • 33645805004 scopus 로고    scopus 로고
    • High titers of IgG antibodies against Plasmodium falciparum serine repeat antigen 5 (SERA5) are associated with protection against severe malaria in Ugandan children
    • Okech B., Mujuzi G., Ogwal A., Shirai H., Horii T., and Egwang T.G. High titers of IgG antibodies against Plasmodium falciparum serine repeat antigen 5 (SERA5) are associated with protection against severe malaria in Ugandan children. Am. J. Trop. Med. Hyg. 74 (2006) 191-197
    • (2006) Am. J. Trop. Med. Hyg. , vol.74 , pp. 191-197
    • Okech, B.1    Mujuzi, G.2    Ogwal, A.3    Shirai, H.4    Horii, T.5    Egwang, T.G.6
  • 10
    • 51949096939 scopus 로고    scopus 로고
    • Inhibition of malaria parasite development by a cyclic peptide that targets the vital parasite protein SERA5
    • Fairlie W.D., Spurck T.P., McCoubrie J.E., Gilson P.R., Miller S.K., McFadden G.I., et al. Inhibition of malaria parasite development by a cyclic peptide that targets the vital parasite protein SERA5. Infect. Immun. 76 (2008) 4332-4344
    • (2008) Infect. Immun. , vol.76 , pp. 4332-4344
    • Fairlie, W.D.1    Spurck, T.P.2    McCoubrie, J.E.3    Gilson, P.R.4    Miller, S.K.5    McFadden, G.I.6
  • 11
    • 0024470488 scopus 로고
    • Molecular cloning, genomic structure and localization in a blood stage antigen of Plasmodium falciparum characterized by a serine stretch
    • Knapp B., Hundt E., Nau U., and Kupper H.A. Molecular cloning, genomic structure and localization in a blood stage antigen of Plasmodium falciparum characterized by a serine stretch. Mol. Biochem. Parasitol. 32 (1989) 73-83
    • (1989) Mol. Biochem. Parasitol. , vol.32 , pp. 73-83
    • Knapp, B.1    Hundt, E.2    Nau, U.3    Kupper, H.A.4
  • 12
    • 0025966022 scopus 로고
    • A new blood stage antigen of Plasmodium falciparum highly homologous to the serine-stretch protein SERP
    • Knapp B., Nau U., Hundt E., and Kupper H.A. A new blood stage antigen of Plasmodium falciparum highly homologous to the serine-stretch protein SERP. Mol. Biochem. Parasitol. 44 (1991) 1-13
    • (1991) Mol. Biochem. Parasitol. , vol.44 , pp. 1-13
    • Knapp, B.1    Nau, U.2    Hundt, E.3    Kupper, H.A.4
  • 13
    • 0026632573 scopus 로고
    • Intramolecular mapping of Plasmodium falciparum P126 proteolytic fragments by N-terminal amino acid sequencing
    • Debrabant A., Maes P., Delplace P., Dubremetz J.F., Tartar A., and Camus D. Intramolecular mapping of Plasmodium falciparum P126 proteolytic fragments by N-terminal amino acid sequencing. Mol. Biochem. Parasitol. 53 (1992) 89-95
    • (1992) Mol. Biochem. Parasitol. , vol.53 , pp. 89-95
    • Debrabant, A.1    Maes, P.2    Delplace, P.3    Dubremetz, J.F.4    Tartar, A.5    Camus, D.6
  • 14
    • 0037046096 scopus 로고    scopus 로고
    • Characterization of proteases involved in the processing of Plasmodium falciparum serine repeat antigen (SERA)
    • Li J., Matsuoka H., Mitamura T., and Horii T. Characterization of proteases involved in the processing of Plasmodium falciparum serine repeat antigen (SERA). Mol. Biochem. Parasitol. 120 (2002) 177-186
    • (2002) Mol. Biochem. Parasitol. , vol.120 , pp. 177-186
    • Li, J.1    Matsuoka, H.2    Mitamura, T.3    Horii, T.4
  • 15
    • 0036888247 scopus 로고    scopus 로고
    • Differential localization of processed fragments of Plasmodium falciparum serine repeat antigen and further processing of its N-terminal 47 kDa fragment
    • Li J., Mitamura T., Fox B., Bzik D., and Horii T. Differential localization of processed fragments of Plasmodium falciparum serine repeat antigen and further processing of its N-terminal 47 kDa fragment. Parasitol. Int. 51 (2002) 343-352
    • (2002) Parasitol. Int. , vol.51 , pp. 343-352
    • Li, J.1    Mitamura, T.2    Fox, B.3    Bzik, D.4    Horii, T.5
  • 16
    • 34547667334 scopus 로고    scopus 로고
    • Phylogeny and evolution of the SERA multigene family in the genus Plasmodium
    • Arisue N., Hirai M., Arai M., Matsuoka H., and Horii T. Phylogeny and evolution of the SERA multigene family in the genus Plasmodium. J. Mol. Evol. 65 (2007) 82-91
    • (2007) J. Mol. Evol. , vol.65 , pp. 82-91
    • Arisue, N.1    Hirai, M.2    Arai, M.3    Matsuoka, H.4    Horii, T.5
  • 17
    • 6344225452 scopus 로고    scopus 로고
    • The serine repeat antigen (SERA) gene family phylogeny in Plasmodium: the impact of GC content, and reconciliation of gene and species trees
    • Bourgon R., Delorenzi M., Sargeant T., Hodder A.N., Crabb B.S., and Speed T.P. The serine repeat antigen (SERA) gene family phylogeny in Plasmodium: the impact of GC content, and reconciliation of gene and species trees. Mol. Biol. Evol. 21 (2004) 2161-2171
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 2161-2171
    • Bourgon, R.1    Delorenzi, M.2    Sargeant, T.3    Hodder, A.N.4    Crabb, B.S.5    Speed, T.P.6
  • 18
    • 36749042579 scopus 로고    scopus 로고
    • Evidence for a common role for the serine-type Plasmodium falciparum SERA proteases: Implications for vaccine and drug design
    • McCoubrie J.E., Miller S.K., Sargeant T., Good R.T., Hodder A.N., Speed T.P., et al. Evidence for a common role for the serine-type Plasmodium falciparum SERA proteases: Implications for vaccine and drug design. Infect. Immun. 75 (2007) 5565-5574
    • (2007) Infect. Immun. , vol.75 , pp. 5565-5574
    • McCoubrie, J.E.1    Miller, S.K.2    Sargeant, T.3    Good, R.T.4    Hodder, A.N.5    Speed, T.P.6
  • 19
    • 36849090615 scopus 로고    scopus 로고
    • Subcellular discharge of a serine protease mediates release of invasive malaria parasites from host erythrocytes
    • Yeoh S., O'Donnell R.A., Koussis K., Dluzewski A.R., Ansell K.H., Osborne S.A., et al. Subcellular discharge of a serine protease mediates release of invasive malaria parasites from host erythrocytes. Cell 131 (2007) 1072-1083
    • (2007) Cell , vol.131 , pp. 1072-1083
    • Yeoh, S.1    O'Donnell, R.A.2    Koussis, K.3    Dluzewski, A.R.4    Ansell, K.H.5    Osborne, S.A.6
  • 20
    • 62649150175 scopus 로고    scopus 로고
    • A multifunctional serine protease primes the malaria parasite for red blood cell invasion
    • Koussis K., Withers-Martinez C., Yeoh S., Child M., Hackett F., Knuepfer E., et al. A multifunctional serine protease primes the malaria parasite for red blood cell invasion. EMBO J. 28 (2009) 725-735
    • (2009) EMBO J. , vol.28 , pp. 725-735
    • Koussis, K.1    Withers-Martinez, C.2    Yeoh, S.3    Child, M.4    Hackett, F.5    Knuepfer, E.6
  • 21
    • 39349098031 scopus 로고    scopus 로고
    • Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum
    • Arastu-Kupur S., Ponder E.L., Fonovic U.P., Yeoh S., Yuan F., Fonovic M., et al. Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum. Nat. Chem. Biol. 4 (2008) 203-213
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 203-213
    • Arastu-Kupur, S.1    Ponder, E.L.2    Fonovic, U.P.3    Yeoh, S.4    Yuan, F.5    Fonovic, M.6
  • 22
    • 2942700177 scopus 로고    scopus 로고
    • Inactive enzyme-homologues find new function in regulatory processes
    • Pils B., and Schultz J. Inactive enzyme-homologues find new function in regulatory processes. J. Mol. Biol. 340 (2004) 399-404
    • (2004) J. Mol. Biol. , vol.340 , pp. 399-404
    • Pils, B.1    Schultz, J.2
  • 23
    • 24744444923 scopus 로고    scopus 로고
    • Plasmodium falciparum serine-repeat antigen (SERA) forms a homodimer through disulfide bond
    • Sato D., Li J., Mitamura T., and Horii T. Plasmodium falciparum serine-repeat antigen (SERA) forms a homodimer through disulfide bond. Parasitol. Int. 54 (2005) 261-265
    • (2005) Parasitol. Int. , vol.54 , pp. 261-265
    • Sato, D.1    Li, J.2    Mitamura, T.3    Horii, T.4
  • 24
    • 0028830072 scopus 로고
    • Rat testin is a newly identified component of the junctional complexes in various tissues whose mRNA is predominantly expressed in the testis and ovary
    • Grima J., Zhu L.J., Zong S.D., Catterall J.F., Bardin C.W., and Cheng C.Y. Rat testin is a newly identified component of the junctional complexes in various tissues whose mRNA is predominantly expressed in the testis and ovary. Biol. Reprod. 52 (1995) 340-355
    • (1995) Biol. Reprod. , vol.52 , pp. 340-355
    • Grima, J.1    Zhu, L.J.2    Zong, S.D.3    Catterall, J.F.4    Bardin, C.W.5    Cheng, C.Y.6
  • 25
  • 26
    • 57349170755 scopus 로고    scopus 로고
    • Silicatein and the translation of its molecular mechanism of biosilicification into low temperature nanomaterial synthesis
    • Brutchey R.L., and Morse D.E. Silicatein and the translation of its molecular mechanism of biosilicification into low temperature nanomaterial synthesis. Chem. Rev. 108 (2008) 4915-4934
    • (2008) Chem. Rev. , vol.108 , pp. 4915-4934
    • Brutchey, R.L.1    Morse, D.E.2
  • 27
    • 41549158169 scopus 로고    scopus 로고
    • Crystal structure and silica condensing activities of silicatein α-cathepsin L chimeras
    • Fairhead M., Johnson K.A., Kowatz T., McMahon S.A., Carter L.G., Oke M., et al. Crystal structure and silica condensing activities of silicatein α-cathepsin L chimeras. Chem. Commun. (2008) 1765-1767
    • (2008) Chem. Commun. , pp. 1765-1767
    • Fairhead, M.1    Johnson, K.A.2    Kowatz, T.3    McMahon, S.A.4    Carter, L.G.5    Oke, M.6
  • 28
    • 0028069676 scopus 로고
    • Tubulointerstitial nephritis antigen interacts with laminin and type IV collagen and promotes cell adhesion
    • Kalfa T.A., Thull J.D., Butkowski R.J., and Charonis A.S. Tubulointerstitial nephritis antigen interacts with laminin and type IV collagen and promotes cell adhesion. J. Biol. Chem. 269 (1994) 1654-1659
    • (1994) J. Biol. Chem. , vol.269 , pp. 1654-1659
    • Kalfa, T.A.1    Thull, J.D.2    Butkowski, R.J.3    Charonis, A.S.4
  • 29
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L., and Park J. DaliLite workbench for protein structure comparison. Bioinformatics 16 (2000) 566-567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 30
    • 0034767886 scopus 로고    scopus 로고
    • Active site mapping, biochemical properties and subcellular localization of rhodesain, the major cysteine protease of Trypanosoma brucei rhodesiense
    • Caffrey C.R., Hansell E., Lucas K.D., Brinen L.S., Hernandez A.A., Cheng J., et al. Active site mapping, biochemical properties and subcellular localization of rhodesain, the major cysteine protease of Trypanosoma brucei rhodesiense. Mol. Biochem. Parasitol. 118 (2001) 61-73
    • (2001) Mol. Biochem. Parasitol. , vol.118 , pp. 61-73
    • Caffrey, C.R.1    Hansell, E.2    Lucas, K.D.3    Brinen, L.S.4    Hernandez, A.A.5    Cheng, J.6
  • 31
    • 0030841381 scopus 로고    scopus 로고
    • Structural determinants of specificity in the cysteine protease cruzain
    • Gillmor S.A., Craik C.S., and Fletterick R.J. Structural determinants of specificity in the cysteine protease cruzain. Protein Sci. 6 (1997) 1603-1611
    • (1997) Protein Sci. , vol.6 , pp. 1603-1611
    • Gillmor, S.A.1    Craik, C.S.2    Fletterick, R.J.3
  • 32
    • 0038617318 scopus 로고    scopus 로고
    • Proposed amino acid sequence and the 1.63 Å X-ray crystal structure of a plant cysteine protease, ervatamin B: some insights into the structural basis of its stability and substrate specificity
    • Biswas S., Chakrabarti C., Kundu S., Jagannadham M.V., and Dattagupta J.K. Proposed amino acid sequence and the 1.63 Å X-ray crystal structure of a plant cysteine protease, ervatamin B: some insights into the structural basis of its stability and substrate specificity. Proteins 51 (2003) 489-497
    • (2003) Proteins , vol.51 , pp. 489-497
    • Biswas, S.1    Chakrabarti, C.2    Kundu, S.3    Jagannadham, M.V.4    Dattagupta, J.K.5
  • 33
    • 0037153194 scopus 로고    scopus 로고
    • Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides
    • Chowdhury S., Sivaraman J., Wang J., Devanathan G., Lachance P., Qi H., et al. Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides. J. Med. Chem. 45 (2002) 5321-5329
    • (2002) J. Med. Chem. , vol.45 , pp. 5321-5329
    • Chowdhury, S.1    Sivaraman, J.2    Wang, J.3    Devanathan, G.4    Lachance, P.5    Qi, H.6
  • 34
    • 0345310073 scopus 로고    scopus 로고
    • Revised definition of substrate binding sites of papain-like cysteine proteases
    • Turk D., Guncar G., Podobnik M., and Turk B. Revised definition of substrate binding sites of papain-like cysteine proteases. Biol. Chem. 379 (1998) 137-147
    • (1998) Biol. Chem. , vol.379 , pp. 137-147
    • Turk, D.1    Guncar, G.2    Podobnik, M.3    Turk, B.4
  • 35
    • 0037322932 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases (cathepsins): promising drug targets
    • Turk D., and Guncar G. Lysosomal cysteine proteases (cathepsins): promising drug targets. Acta Crystallogr., Sect. D: Biol. Crystallogr. D59 (2003) 203-213
    • (2003) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.D59 , pp. 203-213
    • Turk, D.1    Guncar, G.2
  • 37
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities
    • Choe Y., Leonetti F., Greenbaum D.C., Lecaille F., Bogyo M., Brömme D., et al. Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem. 281 (2006) 12824-12832
    • (2006) J. Biol. Chem. , vol.281 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3    Lecaille, F.4    Bogyo, M.5    Brömme, D.6
  • 38
    • 0031826072 scopus 로고    scopus 로고
    • Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes
    • Groves M.R., Coulombe R., Jenkins J., and Cygler M. Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes. Proteins 32 (1998) 504-514
    • (1998) Proteins , vol.32 , pp. 504-514
    • Groves, M.R.1    Coulombe, R.2    Jenkins, J.3    Cygler, M.4
  • 39
    • 12044253640 scopus 로고
    • The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity
    • Musil D., Zucic D., Turk D., Engh R.A., Mayr I., Huber R., et al. The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J. 10 (1991) 2321-2330
    • (1991) EMBO J. , vol.10 , pp. 2321-2330
    • Musil, D.1    Zucic, D.2    Turk, D.3    Engh, R.A.4    Mayr, I.5    Huber, R.6
  • 41
    • 0032518496 scopus 로고    scopus 로고
    • Crystal structure of procine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
    • Guncar G., Podobnik M., Pungercak J., Strukelj B., Turk V., and Turk D. Crystal structure of procine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure 6 (1998) 51-61
    • (1998) Structure , vol.6 , pp. 51-61
    • Guncar, G.1    Podobnik, M.2    Pungercak, J.3    Strukelj, B.4    Turk, V.5    Turk, D.6
  • 42
    • 24744439695 scopus 로고    scopus 로고
    • The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen
    • Meno K., Thorsted P.B., Ipsen H., Kristensen O., Larsen J.N., Spangfort M.D., et al. The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen. J. Immunol. 175 (2005) 3835-3845
    • (2005) J. Immunol. , vol.175 , pp. 3835-3845
    • Meno, K.1    Thorsted, P.B.2    Ipsen, H.3    Kristensen, O.4    Larsen, J.N.5    Spangfort, M.D.6
  • 43
    • 33644777433 scopus 로고    scopus 로고
    • Three-dimensional structure and IgE-binding properties of mature fully active Der p 1, a clinically relevant major allergen
    • de Halleux S., Stura E., VanderElst L., Carlier V., Jacquemin M., and Saint-Remy J.M. Three-dimensional structure and IgE-binding properties of mature fully active Der p 1, a clinically relevant major allergen. J. Allergy Clin. Immunol. 117 (2006) 571-576
    • (2006) J. Allergy Clin. Immunol. , vol.117 , pp. 571-576
    • de Halleux, S.1    Stura, E.2    VanderElst, L.3    Carlier, V.4    Jacquemin, M.5    Saint-Remy, J.M.6
  • 44
    • 0028818335 scopus 로고
    • A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: innate protection by antiproteases
    • Hewitt C.R.A., Brown A.P., Hart B.J., and Pritchard D.I. A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: innate protection by antiproteases. J. Exp. Med. 182 (1995) 1537-1544
    • (1995) J. Exp. Med. , vol.182 , pp. 1537-1544
    • Hewitt, C.R.A.1    Brown, A.P.2    Hart, B.J.3    Pritchard, D.I.4
  • 45
    • 0031975246 scopus 로고    scopus 로고
    • Proteolytic cleavage of CD25, the α subunit of the human T cell interleukin 2 receptor, by Der p 1, a major mite allergen with cysteine protease activity
    • Schulz O., Sewell H.F., and Shakib F. Proteolytic cleavage of CD25, the α subunit of the human T cell interleukin 2 receptor, by Der p 1, a major mite allergen with cysteine protease activity. J. Exp. Med. 187 (1998) 271-275
    • (1998) J. Exp. Med. , vol.187 , pp. 271-275
    • Schulz, O.1    Sewell, H.F.2    Shakib, F.3
  • 46
    • 0028799348 scopus 로고
    • Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity
    • O'Hara B.P., Hemmings A.M., Buttle D.J., and Pearl L.H. Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity. Biochemistry 34 (1995) 13190-13195
    • (1995) Biochemistry , vol.34 , pp. 13190-13195
    • O'Hara, B.P.1    Hemmings, A.M.2    Buttle, D.J.3    Pearl, L.H.4
  • 47
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., and Cygler M. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15 (1996) 5492-5503
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Menard, R.4    Mort, J.S.5    Cygler, M.6
  • 48
    • 0031554904 scopus 로고    scopus 로고
    • Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen
    • Podobnik M., Kuhelj R., Turk V., and Turk D. Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen. J. Mol. Biol. 271 (1997) 774-788
    • (1997) J. Mol. Biol. , vol.271 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 49
    • 22944473016 scopus 로고    scopus 로고
    • A malarial cysteine protease is necessary for Plasmodium sporozoite egress from oocysts
    • Aly A.S.I., and Matuschewshi K. A malarial cysteine protease is necessary for Plasmodium sporozoite egress from oocysts. J. Exp. Med. 202 (2005) 225-230
    • (2005) J. Exp. Med. , vol.202 , pp. 225-230
    • Aly, A.S.I.1    Matuschewshi, K.2
  • 50
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expression Purif. 41 (2005) 207-234
    • (2005) Protein Expression Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr., Part A 276 (1997) 307-326
    • (1997) Macromol. Crystallogr., Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs
    • Pape T., and Schneider T.R. HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs. J. Appl. Crystallogr. 37 (2004) 843-844
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 57
    • 0030945495 scopus 로고    scopus 로고
    • Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties
    • Alexov E.G., and Gunner M.R. Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties. Biophys. J. 72 (1997) 2075-2093
    • (1997) Biophys. J. , vol.72 , pp. 2075-2093
    • Alexov, E.G.1    Gunner, M.R.2
  • 58
    • 0036787760 scopus 로고    scopus 로고
    • Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins
    • Georgescu R.E., Alexov E.G., and Gunner M.R. Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins. Biophys. J. 83 (2002) 1731-1748
    • (2002) Biophys. J. , vol.83 , pp. 1731-1748
    • Georgescu, R.E.1    Alexov, E.G.2    Gunner, M.R.3
  • 59
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free-energies using macroscopic solvent models
    • Sitkoff D., Sharp K.A., and Honig B. Accurate calculation of hydration free-energies using macroscopic solvent models. J. Phys. Chem. 98 (1994) 1978-1988
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 60
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls A., and Honig B. A rapid finite difference algorithm utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comp. Chem. 12 (1991) 435-445
    • (1991) J. Comp. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.