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Volumn 289, Issue 10, 2014, Pages 6332-6340

The three-dimensional structure of the extracellular adhesion domain of the sialic acid-binding adhesin SabA from Helicobacter pylori

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; X RAY CRYSTALLOGRAPHY;

EID: 84896801690     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.513135     Document Type: Article
Times cited : (54)

References (30)
  • 1
    • 25844438837 scopus 로고    scopus 로고
    • Bacteria and mucosal inflammation of the gut: Lessons from Helicobocter pylori
    • Kuipers, E. J., and Michetti, P. (2005) Bacteria and mucosal inflammation of the gut: Lessons from Helicobocter pylori. Helicobacter 10, 66-70
    • (2005) Helicobacter , vol.10 , pp. 66-70
    • Kuipers, E.J.1    Michetti, P.2
  • 2
    • 77954695213 scopus 로고    scopus 로고
    • Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors
    • Magalhães, A., and Reis, C. A. (2010) Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors. Braz. J. Med. Biol. Res. 43, 611-618
    • (2010) Braz. J. Med. Biol. Res. , vol.43 , pp. 611-618
    • Magalhães, A.1    Reis, C.A.2
  • 4
    • 0038798729 scopus 로고    scopus 로고
    • Host gastric Lewis expression determines the bacterial density of Helicobacter pylori in babA2 genopositive infection
    • Sheu, B. S., Sheu, S. M., Yang, H. B., Huang, A. H., and Wu, J. J. (2003) Host gastric Lewis expression determines the bacterial density of Helicobacter pylori in babA2 genopositive infection. Gut 52, 927-932
    • (2003) Gut , vol.52 , pp. 927-932
    • Sheu, B.S.1    Sheu, S.M.2    Yang, H.B.3    Huang, A.H.4    Wu, J.J.5
  • 6
    • 26444542946 scopus 로고    scopus 로고
    • Identification and characterization of binding properties of Helicobacter pylori by glycoconjugate arrays
    • Walz, A., Odenbreit, S., Mahdavi, J., Borén, T., and Ruhl, S. (2005) Identification and characterization of binding properties of Helicobacter pylori by glycoconjugate arrays. Glycobiology 15, 700-708
    • (2005) Glycobiology , vol.15 , pp. 700-708
    • Walz, A.1    Odenbreit, S.2    Mahdavi, J.3    Borén, T.4    Ruhl, S.5
  • 8
    • 17644415392 scopus 로고    scopus 로고
    • The sialic acid binding SabA adhesin of Helicobacter pylori is essential for nonopsonic activation of human neutrophils
    • Unemo, M., Aspholm-Hurtig, M., Ilver, D., Bergström, J., Borén, T., Danielsson, D., and Teneberg, S. (2005) The sialic acid binding SabA adhesin of Helicobacter pylori is essential for nonopsonic activation of human neutrophils. J. Biol. Chem. 280, 15390-15397
    • (2005) J. Biol. Chem. , vol.280 , pp. 15390-15397
    • Unemo, M.1    Aspholm-Hurtig, M.2    Ilver, D.3    Bergström, J.4    Borén, T.5    Danielsson, D.6    Teneberg, S.7
  • 9
    • 0033918170 scopus 로고    scopus 로고
    • Comparative genomics of Helicobacter pylori: Analysis of the outer membrane protein families
    • Alm, R. A., Bina, J., Andrews, B. M., Doig, P., Hancock, R. E., and Trust, T. J. (2000) Comparative genomics of Helicobacter pylori: analysis of the outer membrane protein families. Infect. Immun. 68, 4155-4168
    • (2000) Infect. Immun. , vol.68 , pp. 4155-4168
    • Alm, R.A.1    Bina, J.2    Andrews, B.M.3    Doig, P.4    Hancock, R.E.5    Trust, T.J.6
  • 14
    • 23844492576 scopus 로고    scopus 로고
    • Auto-rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an x-ray diffraction experiment
    • Panjikar, S., Parthasarathy, V., Lamzin, V. S., Weiss, M. S., and Tucker, P. A. (2005) Auto-rickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an x-ray diffraction experiment. Acta Crystallogr. D Biol. Crystallogr. 61, 449-457
    • (2005) Acta Crystallogr. D Biol. Crystallogr. , vol.61 , pp. 449-457
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 15
    • 70349602499 scopus 로고    scopus 로고
    • On the combination of molecular replacement and singlewavelength anomalous diffraction phasing for automated structure determination
    • Panjikar, S., Parthasarathy, V., Lamzin, V. S., Weiss, M. S., and Tucker, P. A. (2009) On the combination of molecular replacement and singlewavelength anomalous diffraction phasing for automated structure determination. Acta Crystallogr. D Biol. Crystallogr. 65, 1089-1097
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 1089-1097
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 18
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr.DBiol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr.DBiol. Crystallogr. , vol.50 , pp. 760-763
  • 19
    • 0141890986 scopus 로고    scopus 로고
    • Application of the complex multivariate normal distribution to crystallographic methods with insights into multiple isomorphous replacement phasing
    • Pannu, N. S., McCoy, A. J., and Read, R. J. (2003) Application of the complex multivariate normal distribution to crystallographic methods with insights into multiple isomorphous replacement phasing. Acta Crystallogr. D Biol. Crystallogr. 59, 1801-1808
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 1801-1808
    • Pannu, N.S.1    McCoy, A.J.2    Read, R.J.3
  • 20
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for x-ray crystallography using ARP/ wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S., and Perrakis, A. (2008) Automated macromolecular model building for x-ray crystallography using ARP/ wARP version 7. Nat. Protoc. 3, 1171-1179
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 23
    • 84876191281 scopus 로고    scopus 로고
    • Campylobacter jejuni Dps protein binds DNA in the presence of iron or hydrogen peroxide
    • Huergo, L. F., Rahman, H., Ibrahimovic, A., Day, C. J., and Korolik, V. (2013) Campylobacter jejuni Dps protein binds DNA in the presence of iron or hydrogen peroxide. J. Bacteriol. 195, 1970-1978
    • (2013) J. Bacteriol. , vol.195 , pp. 1970-1978
    • Huergo, L.F.1    Rahman, H.2    Ibrahimovic, A.3    Day, C.J.4    Korolik, V.5
  • 24
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 25
    • 34250167965 scopus 로고    scopus 로고
    • Plot derived structural alphabet and BLOSUM-like substitution matrix for rapid search of protein structure database
    • Tung, C. H., Huang, J. W., and Yang, J. M. (2007) plot derived structural alphabet and BLOSUM-like substitution matrix for rapid search of protein structure database. Genome Biol. 8, R31
    • (2007) Genome Biol. , vol.8
    • Tung, C.H.1    Huang, J.W.2    Yang, J.M.3
  • 26
    • 0037446733 scopus 로고    scopus 로고
    • Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: Insight into autoproteolytic activation
    • Kim, J. K., Yang, I. S., Rhee, S., Dauter, Z., Lee, Y. S., Park, S. S., and Kim, K. H. (2003) Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation. Biochemistry 42, 4084-4093
    • (2003) Biochemistry , vol.42 , pp. 4084-4093
    • Kim, J.K.1    Yang, I.S.2    Rhee, S.3    Dauter, Z.4    Lee, Y.S.5    Park, S.S.6    Kim, K.H.7
  • 27
    • 13844293071 scopus 로고    scopus 로고
    • Structural insights into the target specificity of plant invertase and pectin methylesterase inhibitory proteins
    • Hothorn, M., Wolf, S., Aloy, P., Greiner, S., and Scheffzek, K. (2004) Structural insights into the target specificity of plant invertase and pectin methylesterase inhibitory proteins. Plant Cell 16, 3437-3447
    • (2004) Plant Cell , vol.16 , pp. 3437-3447
    • Hothorn, M.1    Wolf, S.2    Aloy, P.3    Greiner, S.4    Scheffzek, K.5
  • 28
    • 84861092830 scopus 로고    scopus 로고
    • Two distinct binding modes define the interaction of Brox with the C-terminal tails ofCHMP5and CHMP4B
    • Mu, R., Dussupt, V., Jiang, J., Sette, P., Rudd, V., Chuenchor, W., Bello, N. F., Bouamr, F., and Xiao, T. S. (2012) Two distinct binding modes define the interaction of Brox with the C-terminal tails ofCHMP5and CHMP4B. Structure 20, 887-898
    • (2012) Structure , vol.20 , pp. 887-898
    • Mu, R.1    Dussupt, V.2    Jiang, J.3    Sette, P.4    Rudd, V.5    Chuenchor, W.6    Bello, N.F.7    Bouamr, F.8    Xiao, T.S.9
  • 29
    • 75249088440 scopus 로고    scopus 로고
    • Roll: A new algorithm for the detection of protein pockets and cavities with a rolling probe sphere
    • Yu, J., Zhou, Y., Tanaka, I., and Yao, M. (2010) Roll: a new algorithm for the detection of protein pockets and cavities with a rolling probe sphere. Bioinformatics 26, 46-52
    • (2010) Bioinformatics , vol.26 , pp. 46-52
    • Yu, J.1    Zhou, Y.2    Tanaka, I.3    Yao, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.