메뉴 건너뛰기




Volumn 346, Issue 3, 2005, Pages 801-814

X-ray structure of Na-ASP-2, a pathogenesis-related-1 protein from the nematode parasite, Necator americanus, and a vaccine antigen for human hookworm infection

Author keywords

ASP; Crystal structure; Hookworm; Necator americanus; Pathogenesis related protein

Indexed keywords

ANCYLOSTOMA SECRETED PROTEIN 1; ANCYLOSTOMA SECRETED PROTEIN 2; ANTIGEN; CHEMOKINE; CYSTEINE; PATHOGENESIS RELATED PROTEIN 1; PROTEIN; UNCLASSIFIED DRUG; VACCINE;

EID: 13844275516     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.12.023     Document Type: Article
Times cited : (133)

References (66)
  • 3
    • 0036982347 scopus 로고    scopus 로고
    • Prevention control of schistosomiasis and soil-transmitted helminthiasis
    • WHO
    • WHO Prevention control of schistosomiasis and soil-transmitted helminthiasis World Health Organ. Tech. Rep. Ser. 912 2002 1 57
    • (2002) World Health Organ. Tech. Rep. Ser. , vol.912 , pp. 1-57
  • 4
    • 0041828329 scopus 로고    scopus 로고
    • Global anthelmintic chemotherapy programs: Learning from history
    • J. Horton Global anthelmintic chemotherapy programs: learning from history Trends Parasitol. 19 2003 405 409
    • (2003) Trends Parasitol. , vol.19 , pp. 405-409
    • Horton, J.1
  • 5
    • 0028851648 scopus 로고
    • Rate of reinfection with intestinal nematodes after treatment of children with mebendazole or albendazole in a highly endemic area
    • M. Albonico, P.G. Smith, E. Ercole, A. Hall, H.M. Chwaya, K.S. Alawi, and L. Savioli Rate of reinfection with intestinal nematodes after treatment of children with mebendazole or albendazole in a highly endemic area Trans. Roy. Soc. Trop. Med. Hyg. 89 1995 538 541
    • (1995) Trans. Roy. Soc. Trop. Med. Hyg. , vol.89 , pp. 538-541
    • Albonico, M.1    Smith, P.G.2    Ercole, E.3    Hall, A.4    Chwaya, H.M.5    Alawi, K.S.6    Savioli, L.7
  • 6
    • 0037899938 scopus 로고    scopus 로고
    • Efficacy of mebendazole and levamisole alone or in combination against intestinal nematode infections after repeated targeted mebendazole treatment in Zanzibar
    • M. Albonico, Q. Bickle, M. Ramsan, A. Montresor, L. Savioli, and M. Taylor Efficacy of mebendazole and levamisole alone or in combination against intestinal nematode infections after repeated targeted mebendazole treatment in Zanzibar Bull. World Health Organ. 81 2003 343 352
    • (2003) Bull. World Health Organ. , vol.81 , pp. 343-352
    • Albonico, M.1    Bickle, Q.2    Ramsan, M.3    Montresor, A.4    Savioli, L.5    Taylor, M.6
  • 7
    • 0038330641 scopus 로고    scopus 로고
    • Methods to sustain drug efficacy in helminth control programmes
    • M. Albonico Methods to sustain drug efficacy in helminth control programmes Acta Trop. 86 2003 233 242
    • (2003) Acta Trop. , vol.86 , pp. 233-242
    • Albonico, M.1
  • 9
    • 0042827212 scopus 로고    scopus 로고
    • Progress in the development of a recombinant vaccine for human hookworm disease: The Human Hookworm Vaccine Initiative
    • P.J. Hotez, B. Zhan, J.M. Bethony, A. Loukas, A. Williamson, and G.N. Goud Progress in the development of a recombinant vaccine for human hookworm disease: the Human Hookworm Vaccine Initiative Int. J. Parasitol. 33 2003 1245 1258
    • (2003) Int. J. Parasitol. , vol.33 , pp. 1245-1258
    • Hotez, P.J.1    Zhan, B.2    Bethony, J.M.3    Loukas, A.4    Williamson, A.5    Goud, G.N.6
  • 10
    • 0014992461 scopus 로고
    • Vaccination against the canine hookworm diseases
    • T.A. Miller Vaccination against the canine hookworm diseases Advan. Parasitol. 9 1971 153 183
    • (1971) Advan. Parasitol. , vol.9 , pp. 153-183
    • Miller, T.A.1
  • 11
    • 0018062307 scopus 로고
    • Industrial development and field use of the canine hookworm vaccine
    • T.A. Miller Industrial development and field use of the canine hookworm vaccine Advan. Parasitol. 16 1978 333 342
    • (1978) Advan. Parasitol. , vol.16 , pp. 333-342
    • Miller, T.A.1
  • 12
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins
    • L.C. Van Loon, and E.A. Van Strien The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins Physiol. Mol. Plant Pathol. 55 1999 85 97
    • (1999) Physiol. Mol. Plant Pathol. , vol.55 , pp. 85-97
    • Van Loon, L.C.1    Van Strien, E.A.2
  • 13
    • 0041731780 scopus 로고    scopus 로고
    • Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily
    • T.J. Milne, G. Abbenante, J.D. Tyndall, J. Halliday, and R.J. Lewis Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily J. Biol. Chem. 278 2003 31105 31110
    • (2003) J. Biol. Chem. , vol.278 , pp. 31105-31110
    • Milne, T.J.1    Abbenante, G.2    Tyndall, J.D.3    Halliday, J.4    Lewis, R.J.5
  • 15
    • 0024742682 scopus 로고
    • Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene
    • M. Kasahara, J. Gutknecht, K. Brew, N. Spurr, and P.N. Goodfellow Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene Genomics 5 1989 527 534
    • (1989) Genomics , vol.5 , pp. 527-534
    • Kasahara, M.1    Gutknecht, J.2    Brew, K.3    Spurr, N.4    Goodfellow, P.N.5
  • 16
    • 0037376935 scopus 로고    scopus 로고
    • Wide distribution of cysteine-rich secretory proteins in snake venoms: Isolation and cloning of novel snake venom cysteine-rich secretory proteins
    • Y. Yamazaki, F. Hyodo, and T. Morita Wide distribution of cysteine-rich secretory proteins in snake venoms: isolation and cloning of novel snake venom cysteine-rich secretory proteins Arch. Biochem. Biophys. 412 2003 133 141
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 133-141
    • Yamazaki, Y.1    Hyodo, F.2    Morita, T.3
  • 17
    • 0036272410 scopus 로고    scopus 로고
    • Cloning and characterization of novel snake venom proteins that block smooth muscle contraction
    • Y. Yamazaki, H. Koike, Y. Sugiyama, K. Motoyoshi, T. Wada, and S. Hishinuma Cloning and characterization of novel snake venom proteins that block smooth muscle contraction Eur. J. Biochem. 269 2002 2708 2715
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2708-2715
    • Yamazaki, Y.1    Koike, H.2    Sugiyama, Y.3    Motoyoshi, K.4    Wada, T.5    Hishinuma, S.6
  • 18
    • 0027245545 scopus 로고
    • Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets
    • G. Lu, M. Villalba, M.R. Coscia, D.R. Hoffman, and T.P. King Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets J. Immunol. 150 1993 2823 2830
    • (1993) J. Immunol. , vol.150 , pp. 2823-2830
    • Lu, G.1    Villalba, M.2    Coscia, M.R.3    Hoffman, D.R.4    King, T.P.5
  • 19
    • 0032554018 scopus 로고    scopus 로고
    • CDNA cloning of a novel trypsin inhibitor with similarity to pathogenesis-related proteins, and its frequent expression in human brain cancer cells
    • T. Yamakawa, S. Miyata, N. Ogawa, N. Koshikawa, H. Yasumitsu, T. Kanamori, and K. Miyazaki cDNA cloning of a novel trypsin inhibitor with similarity to pathogenesis-related proteins, and its frequent expression in human brain cancer cells Biochim. Biophys. Acta 1395 1998 202 208
    • (1998) Biochim. Biophys. Acta , vol.1395 , pp. 202-208
    • Yamakawa, T.1    Miyata, S.2    Ogawa, N.3    Koshikawa, N.4    Yasumitsu, H.5    Kanamori, T.6    Miyazaki, K.7
  • 20
    • 0032478175 scopus 로고    scopus 로고
    • Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system
    • T. Szyperski, C. Fernandez, C. Mumenthaler, and K. Wuthrich Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system Proc. Natl Acad Sci. USA 95 1998 2262 2266
    • (1998) Proc. Natl Acad Sci. USA , vol.95 , pp. 2262-2266
    • Szyperski, T.1    Fernandez, C.2    Mumenthaler, C.3    Wuthrich, K.4
  • 21
    • 0032934497 scopus 로고    scopus 로고
    • Ancylostoma secreted protein 2: Cloning and characterization of a second member of a family of nematode secreted proteins from Ancylostoma caninum
    • J.M. Hawdon, S. Narasimhan, and P.J. Hotez Ancylostoma secreted protein 2: cloning and characterization of a second member of a family of nematode secreted proteins from Ancylostoma caninum Mol. Biochem. Parasitol. 99 1999 149 165
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 149-165
    • Hawdon, J.M.1    Narasimhan, S.2    Hotez, P.J.3
  • 22
    • 0142124395 scopus 로고    scopus 로고
    • Molecular characterisation of the Ancylostoma-secreted protein family from the adult stage of Ancylostoma caninum
    • B. Zhan, Y. Liu, M. Badamchian, A. Williamson, J. Feng, and A. Loukas Molecular characterisation of the Ancylostoma-secreted protein family from the adult stage of Ancylostoma caninum Int. J. Parasitol. 33 2003 897 907
    • (2003) Int. J. Parasitol. , vol.33 , pp. 897-907
    • Zhan, B.1    Liu, Y.2    Badamchian, M.3    Williamson, A.4    Feng, J.5    Loukas, A.6
  • 23
    • 0035216926 scopus 로고    scopus 로고
    • Molecular characterisation and expression of two venom allergen-like protein genes in Heterodera glycines
    • B. Gao, R. Allen, T. Maier, E.L. Davis, T.J. Baum, and R.S. Hussey Molecular characterisation and expression of two venom allergen-like protein genes in Heterodera glycines Int. J. Parasitol. 31 2001 1617 1625
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1617-1625
    • Gao, B.1    Allen, R.2    Maier, T.3    Davis, E.L.4    Baum, T.J.5    Hussey, R.S.6
  • 24
    • 0035141084 scopus 로고    scopus 로고
    • A nuclear casein kinase 2 activity is involved in early events of transcriptional activation induced by salicylic acid in tobacco
    • P. Hidalgo, V. Garreton, C.G. Berrios, H. Ojeda, X. Jordana, and L. Holuigue A nuclear casein kinase 2 activity is involved in early events of transcriptional activation induced by salicylic acid in tobacco Plant Physiol. 125 2001 396 405
    • (2001) Plant Physiol. , vol.125 , pp. 396-405
    • Hidalgo, P.1    Garreton, V.2    Berrios, C.G.3    Ojeda, H.4    Jordana, X.5    Holuigue, L.6
  • 25
    • 0033968711 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of a venom allergen AG5-like cDNA from Meloidogyne incognita
    • X. Ding, J. Shields, R. Allen, and R.S. Hussey Molecular cloning and characterisation of a venom allergen AG5-like cDNA from Meloidogyne incognita Int. J. Parasitol. 30 2000 77 81
    • (2000) Int. J. Parasitol. , vol.30 , pp. 77-81
    • Ding, X.1    Shields, J.2    Allen, R.3    Hussey, R.S.4
  • 26
    • 0028896718 scopus 로고
    • Cloning and characterization of a cDNA encoding the catalytic subunit of a cAMP-dependent protein kinase from Ancylostoma caninum third-stage infective larvae
    • J.M. Hawdon, B.F. Jones, and P.J. Hotez Cloning and characterization of a cDNA encoding the catalytic subunit of a cAMP-dependent protein kinase from Ancylostoma caninum third-stage infective larvae Mol. Biochem. Parasitol. 69 1995 127 130
    • (1995) Mol. Biochem. Parasitol. , vol.69 , pp. 127-130
    • Hawdon, J.M.1    Jones, B.F.2    Hotez, P.J.3
  • 27
    • 0030272242 scopus 로고    scopus 로고
    • Hookworm: Developmental biology of the infectious process
    • J.M. Hawdon, and P.J. Hotez Hookworm: developmental biology of the infectious process Curr. Opin. Genet. Dev. 6 1996 618 623
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 618-623
    • Hawdon, J.M.1    Hotez, P.J.2
  • 28
    • 0029989299 scopus 로고    scopus 로고
    • Cloning and characterization of Ancylostoma-secreted protein. A novel protein associated with the transition to parasitism by infective hookworm larvae
    • J.M. Hawdon, B.F. Jones, D.R. Hoffman, and P.J. Hotez Cloning and characterization of Ancylostoma-secreted protein. A novel protein associated with the transition to parasitism by infective hookworm larvae J. Biol. Chem. 271 1996 6672 6678
    • (1996) J. Biol. Chem. , vol.271 , pp. 6672-6678
    • Hawdon, J.M.1    Jones, B.F.2    Hoffman, D.R.3    Hotez, P.J.4
  • 30
    • 12144287751 scopus 로고    scopus 로고
    • Cloning, yeast expression, isolation, and vaccine testing of recombinant Ancylostoma-secreted protein (ASP)-1 and ASP-2 from Ancylostoma ceylanicum
    • G.N. Goud, B. Zhan, K. Ghosh, A. Loukas, J. Hawdon, and A. Dobardzic Cloning, yeast expression, isolation, and vaccine testing of recombinant Ancylostoma-secreted protein (ASP)-1 and ASP-2 from Ancylostoma ceylanicum J. Infect. Dis. 189 2004 919 929
    • (2004) J. Infect. Dis. , vol.189 , pp. 919-929
    • Goud, G.N.1    Zhan, B.2    Ghosh, K.3    Loukas, A.4    Hawdon, J.5    Dobardzic, A.6
  • 31
    • 3042693970 scopus 로고    scopus 로고
    • Ov-ASP-1, the Onchocerca volvulus homologue of the activation associated secreted protein family is immunostimulatory and can induce protective anti-larval immunity
    • A.J. MacDonald, W. Tawe, O. Leon, L. Cao, J. Liu, and Y. Oksov Ov-ASP-1, the Onchocerca volvulus homologue of the activation associated secreted protein family is immunostimulatory and can induce protective anti-larval immunity Parasite Immunol. 26 2004 53 62
    • (2004) Parasite Immunol. , vol.26 , pp. 53-62
    • MacDonald, A.J.1    Tawe, W.2    Leon, O.3    Cao, L.4    Liu, J.5    Oksov, Y.6
  • 32
    • 85030828665 scopus 로고    scopus 로고
    • Antibodies against a secreted protein from hookworm larvae reduce the intensity of infection in humans and vaccinated laboratory animals
    • J.M. Bethony, A. Loukas, M.J. Smout, S. Mendez, Y. Wang, and M.E. Bottazzi Antibodies against a secreted protein from hookworm larvae reduce the intensity of infection in humans and vaccinated laboratory animals Nature Med 2004 In the press
    • (2004) Nature Med
    • Bethony, J.M.1    Loukas, A.2    Smout, M.J.3    Mendez, S.4    Wang, Y.5    Bottazzi, M.E.6
  • 33
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • R.J. Morris, A. Perrakis, and V.S. Lamzin ARP/wARP and automatic interpretation of protein electron density maps Methods Enzymol. 374 2003 229 244
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 37
    • 0033762983 scopus 로고    scopus 로고
    • Current state of automated crystallographic data analysis
    • V.S. Lamzin, and A. Perrakis Current state of automated crystallographic data analysis Nature Struct. Biol. 7 2000 978 981
    • (2000) Nature Struct. Biol. , vol.7 , pp. 978-981
    • Lamzin, V.S.1    Perrakis, A.2
  • 39
    • 0032796996 scopus 로고    scopus 로고
    • Molecular, crystal and solution structure of a beta-cyclodextrin complex with the bromide salt of 2-(3-dimethylaminopropyl)tricyclo[3.3.1.1(3,7)]decan-2- ol, a potent antimicrobial drug
    • A. Perrakis, E. Antoniadou-Vyza, P. Tsitsa, V.S. Lamzin, K.S. Wilson, and S.J. Hamodrakas Molecular, crystal and solution structure of a beta-cyclodextrin complex with the bromide salt of 2-(3-dimethylaminopropyl) tricyclo[3.3.1.1(3,7)]decan-2-ol, a potent antimicrobial drug Carbohydr. Res. 317 1999 19 28
    • (1999) Carbohydr. Res. , vol.317 , pp. 19-28
    • Perrakis, A.1    Antoniadou-Vyza, E.2    Tsitsa, P.3    Lamzin, V.S.4    Wilson, K.S.5    Hamodrakas, S.J.6
  • 40
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 41
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and G. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, G.4
  • 42
    • 0032212015 scopus 로고    scopus 로고
    • Incorporation of prior phase information strengthens maximum-likelihood structure refinement
    • N.S. Pannu, G.N. Murshudov, E.J. Dodson, and R.J. Read Incorporation of prior phase information strengthens maximum-likelihood structure refinement Acta Crystallog. sect. D 54 1998 1285 1294
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 1285-1294
    • Pannu, N.S.1    Murshudov, G.N.2    Dodson, E.J.3    Read, R.J.4
  • 44
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1
  • 45
    • 0035576365 scopus 로고    scopus 로고
    • Major venom allergen of yellow jackets, Ves v 5: Structural characterization of a pathogenesis-related protein superfamily
    • A. Henriksen, T.P. King, O. Mirza, R.I. Monsalve, K. Meno, and H. Ipsen Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily Proteins: Struct. Funct. Genet. 45 2001 438 448
    • (2001) Proteins: Struct. Funct. Genet. , vol.45 , pp. 438-448
    • Henriksen, A.1    King, T.P.2    Mirza, O.3    Monsalve, R.I.4    Meno, K.5    Ipsen, H.6
  • 47
    • 0038173766 scopus 로고    scopus 로고
    • Angiogenic activity of an Onchocerca volvulus Ancylostoma secreted protein homologue
    • T.B. Higazi, E. Pearlman, D.R. Whikehart, and T.R. Unnasch Angiogenic activity of an Onchocerca volvulus Ancylostoma secreted protein homologue Mol. Biochem. Parasitol. 129 2003 61 68
    • (2003) Mol. Biochem. Parasitol. , vol.129 , pp. 61-68
    • Higazi, T.B.1    Pearlman, E.2    Whikehart, D.R.3    Unnasch, T.R.4
  • 48
    • 0034762477 scopus 로고    scopus 로고
    • Expression and immune recognition of Brugia malayi VAL-1, a homologue of vespid venom allergens and Ancylostoma secreted proteins
    • J. Murray, W.F. Gregory, N. Gomez-Escobar, A.K. Atmadja, and R.M. Maizels Expression and immune recognition of Brugia malayi VAL-1, a homologue of vespid venom allergens and Ancylostoma secreted proteins Mol. Biochem. Parasitol. 118 2001 89 96
    • (2001) Mol. Biochem. Parasitol. , vol.118 , pp. 89-96
    • Murray, J.1    Gregory, W.F.2    Gomez-Escobar, N.3    Atmadja, A.K.4    Maizels, R.M.5
  • 50
    • 0028508692 scopus 로고
    • Immunosuppression in Nigerians with hookworm infection
    • B.O. Olatunde, and G.C. Onyemelukwe Immunosuppression in Nigerians with hookworm infection Afr. J. Med. Med. Sci. 23 1994 221 225
    • (1994) Afr. J. Med. Med. Sci. , vol.23 , pp. 221-225
    • Olatunde, B.O.1    Onyemelukwe, G.C.2
  • 51
    • 0034767749 scopus 로고    scopus 로고
    • Immune responses in hookworm infections
    • A. Loukas, and P. Prociv Immune responses in hookworm infections Clin. Microbiol. Rev. 14 2001 689 703
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 689-703
    • Loukas, A.1    Prociv, P.2
  • 52
    • 0036776107 scopus 로고    scopus 로고
    • Viruses in control of the immune system. Workshop on molecular mechanisms of immune modulation: Lessons from viruses
    • A. Alcami, P. Ghazal, and J.W. Yewdell Viruses in control of the immune system. Workshop on molecular mechanisms of immune modulation: lessons from viruses EMBO Rep. 3 2002 927 932
    • (2002) EMBO Rep. , vol.3 , pp. 927-932
    • Alcami, A.1    Ghazal, P.2    Yewdell, J.W.3
  • 53
    • 0035259780 scopus 로고    scopus 로고
    • Viral exploitation and subversion of the immune system through chemokine mimicry
    • P.M. Murphy Viral exploitation and subversion of the immune system through chemokine mimicry Nature Immunol. 2 2001 116 122
    • (2001) Nature Immunol. , vol.2 , pp. 116-122
    • Murphy, P.M.1
  • 54
    • 0034122721 scopus 로고    scopus 로고
    • CR3: A general purpose adhesion-recognition receptor essential for innate immunity
    • M.R. Ehlers CR3: a general purpose adhesion-recognition receptor essential for innate immunity Microb. Infect. 2 2000 289 294
    • (2000) Microb. Infect. , vol.2 , pp. 289-294
    • Ehlers, M.R.1
  • 55
    • 0030039741 scopus 로고    scopus 로고
    • Solvent-accessible residues on the metal ion-dependent adhesion site face of integrin CR3 mediate its binding to the neutrophil inhibitory factor
    • P. Rieu, T. Sugimori, D.L. Griffith, and M.A. Arnaout Solvent-accessible residues on the metal ion-dependent adhesion site face of integrin CR3 mediate its binding to the neutrophil inhibitory factor J. Biol. Chem. 271 1996 15858 15861
    • (1996) J. Biol. Chem. , vol.271 , pp. 15858-15861
    • Rieu, P.1    Sugimori, T.2    Griffith, D.L.3    Arnaout, M.A.4
  • 56
    • 0028142840 scopus 로고
    • Integrin-ligand interactions: A year in review
    • T.A. Haas, and E.F. Plow Integrin-ligand interactions: a year in review Curr. Opin. Cell Biol. 6 1994 656 662
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 656-662
    • Haas, T.A.1    Plow, E.F.2
  • 57
    • 0030749838 scopus 로고    scopus 로고
    • Identification and reconstruction of the binding site within alphaMbeta2 for a specific and high affinity ligand, NIF
    • L. Zhang, and E.F. Plow Identification and reconstruction of the binding site within alphaMbeta2 for a specific and high affinity ligand, NIF J. Biol. Chem. 272 1997 17558 17564
    • (1997) J. Biol. Chem. , vol.272 , pp. 17558-17564
    • Zhang, L.1    Plow, E.F.2
  • 58
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • J.W. Pflugrath The finer things in X-ray diffraction data collection Acta Crystallog. sect. D 55 1999 1718 1725
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 59
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 60
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brunger The free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 474
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 61
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of annotated three-dimensional protein structure homology models
    • J. Kopp, and T. Schwede The SWISS-MODEL repository of annotated three-dimensional protein structure homology models Nucl. Acids Res. 32 2004 D230 D234
    • (2004) Nucl. Acids Res. , vol.32
    • Kopp, J.1    Schwede, T.2
  • 62
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucl. Acids Res. 31 2003 3381 3385
    • (2003) Nucl. Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 63
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 64
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • R.M. Esnouf An extensively modified version of MolScript that includes greatly enhanced coloring capabilities J. Mol. Graph. Model. 15 1997 132 134
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 65
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 66
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Struct. Funct. Genet. 11 1991 281 296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.