메뉴 건너뛰기




Volumn 9, Issue 3, 2014, Pages

High-throughput epitope binning assays on label-free array-based biosensors can yield exquisite epitope discrimination that facilitates the selection of monoclonal antibodies with functional activity

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GRN PROTEIN, HUMAN; MONOCLONAL ANTIBODY; SIGNAL PEPTIDE;

EID: 84898614037     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0092451     Document Type: Article
Times cited : (87)

References (22)
  • 1
    • 84872875413 scopus 로고    scopus 로고
    • Epitope interactions of monoclonal antibodies targeting CD20 and their relationship to functional properties
    • Klein C, Lammens A, Schafer W, Georges G, Schwaiger M, et al. (2013) Epitope interactions of monoclonal antibodies targeting CD20 and their relationship to functional properties. MAbs 5: 22-33.
    • (2013) MAbs , vol.5 , pp. 22-33
    • Klein, C.1    Lammens, A.2    Schafer, W.3    Georges, G.4    Schwaiger, M.5
  • 2
    • 84878218869 scopus 로고    scopus 로고
    • The diversity of the immune response to the A2 domain of human factor VIII
    • Markovitz RC, Healey JF, Parker ET, Meeks SL, Lollar P (2013) The diversity of the immune response to the A2 domain of human factor VIII. Blood 121: 2785-2795.
    • (2013) Blood , vol.121 , pp. 2785-2795
    • Markovitz, R.C.1    Healey, J.F.2    Parker, E.T.3    Meeks, S.L.4    Lollar, P.5
  • 3
    • 78149293634 scopus 로고    scopus 로고
    • Recent advances in B-cell epitope prediction methods
    • EL-Manzalawy Y, Honavar V (2010) Recent advances in B-cell epitope prediction methods. Immunome Research (Suppl 2):S2.
    • (2010) Immunome Research , Issue.SUPPL. 2
    • El-Manzalawy, Y.1    Honavar, V.2
  • 4
    • 79953782986 scopus 로고    scopus 로고
    • Combining epitope-distinct antibodies to HER2: Cooperative inhibitory effects on invasive growth
    • Emde A, Pradeep C-R, Ferraro DA, Ben-Chetrit N, Sela M, et al. (2011) Combining epitope-distinct antibodies to HER2: cooperative inhibitory effects on invasive growth. Oncogene 30: 1631-1642.
    • (2011) Oncogene , vol.30 , pp. 1631-1642
    • Emde, A.1    Pradeep, C.-R.2    Ferraro, D.A.3    Ben-Chetrit, N.4    Sela, M.5
  • 5
    • 81255210858 scopus 로고    scopus 로고
    • Rational identification of an optimal antibody mixture for targeting the epidermal growth factor receptor
    • Koefoed K, Steinaa L, Søderberg JN, Kjær I, Jacobsen HJ, et al. (2011) Rational identification of an optimal antibody mixture for targeting the epidermal growth factor receptor. MAbs 3: 584-595.
    • (2011) MAbs , vol.3 , pp. 584-595
    • Koefoed, K.1    Steinaa, L.2    Søderberg, J.N.3    Kjær, I.4    Jacobsen, H.J.5
  • 6
  • 7
    • 84868570501 scopus 로고    scopus 로고
    • Rozrolimupab, a mixture of 25 recombinant human monoclonal RhD antibodies, in the treatment of primary immune thrombocytopenia
    • Robak T, Windyga J, Trelinski J, von Depka Prondzinski M, Giagounidis A, et al. (2012) Rozrolimupab, a mixture of 25 recombinant human monoclonal RhD antibodies, in the treatment of primary immune thrombocytopenia. Blood 120: 3670-3676.
    • (2012) Blood , vol.120 , pp. 3670-3676
    • Robak, T.1    Windyga, J.2    Trelinski, J.3    Von Depka Prondzinski, M.4    Giagounidis, A.5
  • 8
    • 84865513993 scopus 로고    scopus 로고
    • Triepitopic Antibody fusions inhibit Cetuximab-resistant BRAF and KRAS mutant tumors via EGFR signal repression
    • Spangler JB, Manzari MT, Rosalia EK, Chen TK, Wittrup KD (2012) Triepitopic Antibody fusions inhibit Cetuximab-resistant BRAF and KRAS mutant tumors via EGFR signal repression. J Mol Biol 422: 532-544.
    • (2012) J Mol Biol , vol.422 , pp. 532-544
    • Spangler, J.B.1    Manzari, M.T.2    Rosalia, E.K.3    Chen, T.K.4    Wittrup, K.D.5
  • 9
    • 33845902552 scopus 로고    scopus 로고
    • Higher-throughput, label-free, real-time molecular interaction analysis
    • DOI 10.1016/j.ab.2006.10.040, PII S0003269706008037
    • Rich RL, Myszka DG (2007) Higher-throughput, label-free, real-time molecular interaction analysis. Anal Biochem 361: 1-6. (Pubitemid 46026999)
    • (2007) Analytical Biochemistry , vol.361 , Issue.1 , pp. 1-6
    • Rich, R.L.1    Myszka, D.G.2
  • 10
  • 11
    • 48349091922 scopus 로고    scopus 로고
    • Several distinct properties of the IgE repertoire determine effector cell degranulation in response to allergen challenge
    • Christensen LH, Holm J, Lund G, Riise E, Lund K (2008) Several distinct properties of the IgE repertoire determine effector cell degranulation in response to allergen challenge. J Allergy Clin Immunol 122: 298-304.
    • (2008) J Allergy Clin Immunol , vol.122 , pp. 298-304
    • Christensen, L.H.1    Holm, J.2    Lund, G.3    Riise, E.4    Lund, K.5
  • 12
    • 84862927415 scopus 로고    scopus 로고
    • Comparative study of random and oriented antibody immobilization as measured by dual polarization interferometry and surface plasmon resonance spectroscopy
    • Song HY, Zhou X, Hobley J, Su X (2012) Comparative study of random and oriented antibody immobilization as measured by dual polarization interferometry and surface plasmon resonance spectroscopy. Langmuir 28: 997-1004.
    • (2012) Langmuir , vol.28 , pp. 997-1004
    • Song, H.Y.1    Zhou, X.2    Hobley, J.3    Su, X.4
  • 14
    • 0034469169 scopus 로고    scopus 로고
    • Localization of a binding site for herpes simplex virus glycoprotein D on herpesvirus entry mediator C by using antireceptor monoclonal antibodies
    • DOI 10.1128/JVI.74.23.10863-10872.2000
    • Krummenacher C, Baribaud I, Ponce de Leon M, Whitbeck JC, Lou H, et al. (2000) Localization of a binding site for herpes simplex virus glycoprotein D on herpesvirus entry mediator C by using antireceptor monoclonal antibodies. J Virol 74: 10863-10872. (Pubitemid 32223950)
    • (2000) Journal of Virology , vol.74 , Issue.23 , pp. 10863-10872
    • Krummenacher, C.1    Baribaud, I.2    Ponce, D.L.M.3    Whitbeck, J.C.4    Lou, H.5    Cohen, G.H.6    Eisenberg, R.J.7
  • 15
    • 21344452991 scopus 로고    scopus 로고
    • Direct optical detection of protein-ligand interactions
    • Gesellchen F, Zimmermann B, Herberg FW (2005) Direct optical detection of protein-ligand interactions. Methods Mol Biol 305: 17-46.
    • (2005) Methods Mol Biol , vol.305 , pp. 17-46
    • Gesellchen, F.1    Zimmermann, B.2    Herberg, F.W.3
  • 16
    • 84863598239 scopus 로고    scopus 로고
    • Label-free epitope binning assays of monoclonal antibodies enable the identification of antigen heterogeneity
    • Abdiche YN, Lindquist KC, Stone DM, Rajpal A, Pons J (2012) Label-free epitope binning assays of monoclonal antibodies enable the identification of antigen heterogeneity. J Immunol Methods 382: 101-116.
    • (2012) J Immunol Methods , vol.382 , pp. 101-116
    • Abdiche, Y.N.1    Lindquist, K.C.2    Stone, D.M.3    Rajpal, A.4    Pons, J.5
  • 17
    • 59749089793 scopus 로고    scopus 로고
    • Exploring blocking assays using Octet, ProteOn, and Biacore biosensors
    • Abdiche YN, Malashock DS, Pinkerton A, Pons J (2009) Exploring blocking assays using Octet, ProteOn, and Biacore biosensors. Anal Biochem 386: 172-180.
    • (2009) Anal Biochem , vol.386 , pp. 172-180
    • Abdiche, Y.N.1    Malashock, D.S.2    Pinkerton, A.3    Pons, J.4
  • 18
    • 79951579299 scopus 로고    scopus 로고
    • Expanding the ProteOn XPR36 biosensor into a 36-ligand array expedites protein interaction analysis
    • Abdiche YN, Lindquist KC, Pinkerton A, Pons J, Rajpal A (2011) Expanding the ProteOn XPR36 biosensor into a 36-ligand array expedites protein interaction analysis. Anal Biochem 411: 139-151.
    • (2011) Anal Biochem , vol.411 , pp. 139-151
    • Abdiche, Y.N.1    Lindquist, K.C.2    Pinkerton, A.3    Pons, J.4    Rajpal, A.5
  • 19
    • 42749087930 scopus 로고    scopus 로고
    • Preparation of ultrapure bovine and human hemoglobin by anion exchange chromatography
    • Sun G, Palmer AF (2008) Preparation of ultrapure bovine and human hemoglobin by anion exchange chromatography. J Chromat B 867: 1-7.
    • (2008) J Chromat B , vol.867 , pp. 1-7
    • Sun, G.1    Palmer, A.F.2
  • 21
    • 0029095204 scopus 로고
    • Identification of the ligand-binding domain of the surface-located fibrinogen receptor (clumping factor) of Staphylococcus aureus
    • McDevitt D, Francois P, Vaudaux P, Foster TJ (1995) Identification of the ligand-binding domain of the surface-located fibrinogen receptor (clumping factor) of Staphylococcus aureus. Mol Microbiol.16: 895-907.
    • (1995) Mol Microbiol , vol.16 , pp. 895-907
    • McDevitt, D.1    Francois, P.2    Vaudaux, P.3    Foster, T.J.4
  • 22
    • 33845428586 scopus 로고    scopus 로고
    • Staphylococcus aureus IsdB is a hemoglobin receptor required for heme iron utilization
    • DOI 10.1128/JB.01335-06
    • Torres VJ, Pishchany G, Humayun M, Schneewind O, Skaar EP (2006) Staphylococcus aureus IsdB is a hemoglobin receptor required for heme iron utilization. J Bacteriol 188: 8421-8429. (Pubitemid 44894042)
    • (2006) Journal of Bacteriology , vol.188 , Issue.24 , pp. 8421-8429
    • Torres, V.J.1    Pishchany, G.2    Humayun, M.3    Schneewind, O.4    Skaar, E.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.