메뉴 건너뛰기




Volumn 106, Issue 42, 2009, Pages 17717-17722

Correction for "The crystal structure of sphingosine-1-phosphate in complex with a Fab fragment reveals metal bridging of an antibody and its antigen" (Proceedings of the National Academy of Sciences of the United States of America (2009) 106, 42, (17717-17722) DOI: 10.1073/pnas.0906153106);The crystal structure of sphingosine-1-phosphate in complex with a Fab fragment reveals metal bridging of an antibody and its antigen

Author keywords

Antibody structure; Calcium; Lipid signaling; X ray crystallography

Indexed keywords

AMINO ACID; AMINOALCOHOL; ANTIGEN; CHELATING AGENT; IMMUNOGLOBULIN F(AB) FRAGMENT; LT 1009; METAL; MONOCLONAL ANTIBODY; SONEPCIZUMAB; SPHINGOSINE; SPHINGOSINE 1 PHOSPHATE; UNCLASSIFIED DRUG;

EID: 70449578266     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0911794106     Document Type: Erratum
Times cited : (47)

References (29)
  • 1
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • Hannun YA, Obeid LM (2008) Principles of bioactive lipid signalling: Lessons from sphingolipids. Nat Rev Mol Cell Biol 9:139-150.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 2
    • 46949104885 scopus 로고    scopus 로고
    • Inside-out signaling of sphingosine-1-phosphate: Therapeutic targets
    • DOI 10.1124/pr.107.07113
    • Takabe K, Paugh SW, Milstien S, Spiegel S (2008) "Inside-out" signaling of sphingosine- 1-phosphate: Therapeutic targets. Pharmacol Rev 60:181-195. (Pubitemid 351962008)
    • (2008) Pharmacological Reviews , vol.60 , Issue.2 , pp. 181-195
    • Takabe, K.1    Paugh, S.W.2    Milstien, S.3    Spiegel, S.4
  • 4
    • 0032429270 scopus 로고    scopus 로고
    • Signaling mechanisms and molecular characteristics of G protein-coupled receptors for lysophosphatidic acid and sphingosine 1-phosphate
    • An S, Goetzl EJ, Lee H (1998) Signaling mechanisms and molecular characteristics of G protein-coupled receptors for lysophosphatidic acid and sphingosine 1-phosphate. J Cell Biochem Suppl 30-31:147-157.
    • (1998) J Cell Biochem Suppl , vol.30-31 , pp. 147-157
    • An, S.1    Goetzl, E.J.2    Lee, H.3
  • 7
    • 32044448106 scopus 로고    scopus 로고
    • Emerging medicinal roles for lysophospholipid signaling
    • Gardell SE, Dubin AE, Chun J (2006) Emerging medicinal roles for lysophospholipid signaling. Trends Mol Med 12:65-75.
    • (2006) Trends Mol Med , vol.12 , pp. 65-75
    • Gardell, S.E.1    Dubin, A.E.2    Chun, J.3
  • 9
    • 70350399322 scopus 로고    scopus 로고
    • Production and characterization of monoclonal antisphingosine-1-phosphate antibodies
    • June 9, 10.1194/jlr.M900048-JLR200
    • O'Brien N, et al. (June 9, 2009) Production and characterization of monoclonal antisphingosine-1-phosphate antibodies. J Lipid Res, 10.1194/jlr.M900048-JLR200.
    • (2009) J Lipid Res
    • O'Brien, N.1
  • 11
    • 0037197254 scopus 로고    scopus 로고
    • Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature
    • Tsodikov OV, Record MT, Jr, Sergeev YV (2002) Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature. J Comput Chem 23:600-609.
    • (2002) J Comput Chem , vol.23 , pp. 600-609
    • Tsodikov, O.V.1    Record Jr., M.T.2    Sergeev, Y.V.3
  • 13
    • 0031717755 scopus 로고    scopus 로고
    • The role of metals in catalysis by the restriction endonuclease bamhi
    • DOI 10.1038/2352
    • Viadiu H, Aggarwal AK (1998) The role of metals in catalysis by the restriction endonuclease BamHI. Nat Struct Biol 5:910-916. (Pubitemid 28467415)
    • (1998) Nature Structural Biology , vol.5 , Issue.10 , pp. 910-916
    • Viadiu, H.1    Aggarwal, A.K.2
  • 14
    • 0034725527 scopus 로고    scopus 로고
    • PvuII endonuclease contains two calcium ions in active sites
    • Horton JR, Cheng X (2000) PvuII endonuclease contains two calcium ions in active sites. J Mol Biol 300:1049-1056.
    • (2000) J Mol Biol , vol.300 , pp. 1049-1056
    • Horton, J.R.1    Cheng, X.2
  • 15
    • 0028783371 scopus 로고
    • 2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V
    • 2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nat Struct Biol 2:968-974.
    • (1995) Nat Struct Biol , vol.2 , pp. 968-974
    • Swairjo, M.A.1
  • 16
    • 0033571223 scopus 로고    scopus 로고
    • 2+ bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine
    • 2+ bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine. EMBO J 18:6329-6338.
    • (1999) EMBO J , vol.18 , pp. 6329-6338
    • Verdaguer, N.1
  • 18
  • 20
    • 26844529196 scopus 로고    scopus 로고
    • Interfacial metal and antibody recognition
    • Zhou T, et al. (2005) Interfacial metal and antibody recognition. Proc Natl Acad Sci USA 102:14575-14580.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14575-14580
    • Zhou, T.1
  • 21
    • 0035906591 scopus 로고    scopus 로고
    • Antibody recognition of a conformational epitope in a peptide antigen: Fv-peptide complex of an antibody fragment specific for the mutant EGF receptor, EGFRvIII
    • Landry RC, et al. (2001) Antibody recognition of a conformational epitope in a peptide antigen: Fv-peptide complex of an antibody fragment specific for the mutant EGF receptor, EGFRvIII. J Mol Biol 308:883-893.
    • (2001) J Mol Biol , vol.308 , pp. 883-893
    • Landry, R.C.1
  • 23
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Crystallogr 40:658-674.
    • (2007) J Appl Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 24
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53:240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 25
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee DE (1999) XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density. J Struct Biol 125:156-165.
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 26
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • Kleywegt GJ, Jones TA (1998) Databases in protein crystallography. Acta Crystallogr D 54:1119-1131.
    • (1998) Acta Crystallogr D , vol.54 , pp. 1119-1131
    • Kleywegt, G.J.1    Jones, T.A.2
  • 27
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, et al. (2007) MolProbity: All-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35:W375-W383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1
  • 28
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman HM, et al. (2000) The Protein Data Bank. Nucleic Acids Res 28:235-242.
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, H.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.