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Supplementary InformationA general strategy for generating intact, full-length IgG antibodies that penetrate into the cytosol of living cellsDong-Ki Choi, Jeomil Bae, Seung-Min Shin, Ju-Yeon Shin, Sunghoon Kim, and Yong-Sung KimInventory of Supplementary InformationSupplementary Figure legends S1 to S8Supplementary Movie S1 Supplementary Materials and MethodsSupplementary ReferencesSupplementary Figure S1. (A) Amino acid sequence alignment of m3D8, hT0, hT2 and hT3 VL single domain antibodies. CDR residues are indicated by brackets ([ ]). The Vernier zone residues in the β-sheet framework closely underlying CDRs are underlined and bolded. The two Vernier zone residues back mutated in hT2 and hT3 VLs with the corresponding murine residues (I2L and L4M) are indicated by bold, red color. Amino acids changes in Vκ1 framework of hT3 VL from Vκ3 framework of hT2 VL are colored by blue. Residues are numbered according to the Kabat numbering system. ADDIN EN.CITE <EndNote><Cite><Author>Kabat</Author><Year>1991</Year><RecNum>403</RecNum><DisplayText><style face="superscript">1</style></DisplayText><record><rec-number>403</rec-number><foreign-keys><key app="EN" db-id="5sz0e52zssawxcea2xppw558frz5zzs2d02v">403</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kabat, E. A.</author><author>Wu, T. T.</author></authors></contributors><auth-address>Department of Microbiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.</auth-address><titles><title>Identical V region amino acid sequences and segments of sequences in antibodies of different specificities. Relative contributions of VH and VL genes, minigenes, and complementarity-determining regions to binding of antibody-combining sites</title><secondary-title>J Immunol</secondary-title><alt-title>Journal of immunology</alt-title></titles><periodical><full-title>J Immunol</full-title></periodical><pages>1709-19</pages><volume>147</volume><number>5</number><keywords><keyword>Amino Acid Sequence</keyword><keyword>Animals</keyword><keyword>*Antibody Specificity</keyword><keyword>*Binding Sites, Antibody</keyword><keyword>*Genes, Immunoglobulin</keyword><keyword>Guinea Pigs</keyword><keyword>Humans</keyword><keyword>Immunoglobulin Heavy Chains/*genetics</keyword><keyword>Immunoglobulin Light Chains/*genetics</keyword><keyword>Immunoglobulin Variable Region/*chemistry/genetics/immunology</keyword><keyword>Mice</keyword><keyword>Molecular Sequence Data</keyword><keyword>Protein Conformation</keyword><keyword>Rabbits</keyword><keyword>Rats</keyword></keywords><dates><year>1991</year><pub-dates><date>Sep 1</date></pub-dates></dates><isbn>0022-1767 (Print)
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ADDIN EN.CITE.DATA 2, 3 prior to the confocal microscopy analysis. In (C), HeLa cells were pre-treated for 30 min with CPZ (10 μg/ml), MβCD (5 mM) or Cyt-D (1 μg/ml) and then incubated each VL for additional for 2 h, followed by confocal microscopy analysis. In (B and C), internalized Protein-A-tagged VLs were detected with rabbit IgG and subsequent TRITC-conjugated goat anti-rabbit antibody.PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5MZWU8L0F1dGhvcj48WWVhcj4yMDEwPC9ZZWFyPjxSZWNO
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ADDIN EN.CITE.DATA 3 Images show the merging of markers (green) and/or VLs (red) and Hochest33342-stained nuclei (blue) at the centered single confocal section. Image magnification, 630×; scale bar, 5 μm.Supplementary Figure S2. Generation of humanized hT4 VL with the highest frequent amino acids at the main VH-interacting positions on the consensus sequence of Vκ1 family germline segments. (A) Analysis of VH-VL interface of antibodies tested in our study. Left cartoon represents the VH-VL interface based on the three-dimensional structure of adalimumab (PDB 3wd5) PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5IdTwvQXV0aG9yPjxZZWFyPjIwMTM8L1llYXI+PFJlY051
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ADDIN EN.CITE.DATA 4, prepared by PyMol software. The right panel shows the 10 positions mostly involved in VH-VL interactions and the frequency of amino acids at each position in percentage (grey boxes), determined by structural analyses of 23 crystallized VH-VL interfaces. ADDIN EN.CITE <EndNote><Cite><Author>Vargas-Madrazo</Author><Year>2003</Year><RecNum>364</RecNum><DisplayText><style face="superscript">5</style></DisplayText><record><rec-number>364</rec-number><foreign-keys><key app="EN" db-id="5sz0e52zssawxcea2xppw558frz5zzs2d02v">364</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Vargas-Madrazo, E.</author><author>Paz-Garcia, E.</author></authors></contributors><auth-address>Instituto de Investigaciones Biologicas, Universidad Veracruzana, Xalapa, Veracruz, Mexico. evargas@uv.mx</auth-address><titles><title>An improved model of association for VH-VL immunoglobulin domains: asymmetries between VH and VL in the packing of some interface residues</title><secondary-title>J Mol Recognit</secondary-title></titles><periodical><full-title>J Mol Recognit</full-title></periodical><pages>113-20</pages><volume>16</volume><number>3</number><edition>2003/07/02</edition><keywords><keyword>Animals</keyword><keyword>Binding Sites, Antibody</keyword><keyword>Humans</keyword><keyword>Immunoglobulin Heavy Chains/*chemistry</keyword><keyword>Immunoglobulin Light Chains/*chemistry</keyword><keyword>Models, Molecular</keyword><keyword>Protein Conformation</keyword></keywords><dates><year>2003</year><pub-dates><date>May-Jun</date></pub-dates></dates><isbn>0952-3499 (Print)
0952-3499 (Linking)</isbn><accession-num>12833565</accession-num><urls><related-urls><url> Each position is color-coded based on the observed contact frequency from the analyses of 23 VH-VL interfaces. The interacting residues at the VH-VL interface with contact frequency above 50 % and between 20 % and 50 % are also indicated by red solid lines and black dotted lines, respectively. The amino acids at the 10 positions of VH and VL of antibodies (adalimumab, bevacizumab, TMab3 and TMab4) used in this study are also shown in single letter code. The hT3 VL conserved the highest frequent amino acids at all of the VH-interacting positions, except for two residues of K89 and S91 in VL-CDR3 that commonly interact with 103-3 and 95 residues in VH-CDR3, respectively. Thus we designed a hT3 variant, dubbed hT4, with two substitutions of K89Q and S91Y to have the most frequently used amino acids of human VLs at the two positions so that hT4 can be broadly associated with various human VH gene family. (B) Sequence alignment of VLs of hT3, hT4, adalimumab, and bevacizumab. The 10 positions of VL mostly involved in the interactions with VH are indicated by bold, blue color. CDRs indicated by brackets. Supplementary Figure S3. Biochemical characterizations of the purified parent mAbs and cytotransmabs. (A) Direct ELISA to determine the antigen binding activity of TMab4, HuT4, AvaT4, bevacizumab, and adalimumab antibodies (100 nM) to plate-coated antigen VEGF-A (0.05 ?g/ml) or TNFα (0.1 ?g/ml). (B) DNA hydrolyzing activity assay of the indicated antibodies by agarose gel electrophoresis. The supercoiled plasmid pUC19 (2.2 nM) was incubated with m3D8 scFv (100 nM, 500 nM) or IgG-format cytotransmabs (TMab4, HuT4, and AvaT4, 100 nM) for 1 h at 37 °C in TBS buffer (pH 7.4) containing 2 mM MgCl2 (indicated as ‘Mg’) or 50 mM EDTA (indicated as ‘E’). The reaction mixtures were analyzed by 0.7 % agarose gel electrophoresis, and then stained with ethidium bromide (EtBr). The plasmid incubated with the buffer alone and molecular mass markers were labeled as ‘Buffer’ and ‘M’, respectively. The m3D8 scFv was used as a positive control. We previously reported that m3D8 scFv hydrolyzes DNAs in the presence of Mg2+, but not EDTA.PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5KYW5nPC9BdXRob3I+PFllYXI+MjAwOTwvWWVhcj48UmVj
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ADDIN EN.CITE.DATA 2, 3, 6Supplementary Figure S4. Cytotransmabs internalizes into various types of live cells with internalizing efficiency of almost 100%. (A) Cellular internalization and localization of cytotransmabs (TMab4, HuT4 and AvaT4) and control mAbs (adalimumab and bevacizumab) in PANC-1, HT-29 and MCF-7 cells, treated with the antibodies (1 ?M) for 6 h at 37 °C. Image magnification, 630× (zoom factor 2); scale bar, 5 μm. (B) Internalization efficiency of cytotransmabs (TMab4, HuT4 and AvaT4) observed for numerous cells of HeLa, PANC-1, HT-29 and MCF-7, treated with the antibodies (1 ?M) for 6 h at 37 °C. The images are representative of hundreds of cells examined by confocal microscopy. Image magnification, 400× (zoom factor 1); scale bar, 20 μm. In (A and B), after removing cell-surface bound antibodies with low pH glycine buffer (pH 2.5), internalized antibodies were visualized with FITC-conjugated anti-human IgG Fc antibody. Images show the merging of antibodies (green) and Hochest33342-stained nuclei (blue) at the centered single confocal section. (C) Representative FACS scatter plots of HeLa cells, treated with the indicated antibodies (1 ?M) for 6 h at 37 °C prior to FACS analysis, showing the internalization efficiency of cytotransmabs (TMab4 and AvaT4) and the control mAb (Bevacizumab). Internalized antibodies were stained with Alexa Fluor 488-conjugated anti-human IgG antibody. 'Control' means the cells left untreated with antibodies. Gating (rectangles) indicate the cells with Alexa Fluor 488 positive fluorescence compared to the untreated control. The indicated percentages were the frequency of positive cell population entering the boxed gate.Supplementary Figure S5. Cytotoxicity of internalized cytotransmabs in PANC-1 cells, treated with the indicated antibodies (1 ?M) at 37 °C for 24 h or 48 h. (A) The morphological features of cells were taken by phase-contrast microscopy after 48 h. Image magnification, 100×; scale bar, 20 μm. (B) The cell viability was determined by MTT assay after 24 h or 48 h. The data represent mean ± SD versus PBS-treated controls.Supplementary Figure S6. Confocal fluorescence images showing effects of endocytosis inhibitors on TMab4 internalization into HeLa cells, as described in Fig. 3E. HeLa cells were pre-treated for 30 min at 37 °C with CPZ (10 μg/ml), dansylcadaverine (200 μM), MβCD (5 mM), nystatin (50 μg/ml), EIPA (10 μM), wortmannin (200 nM), Cyt-D (1μg/ml) or dynasore (40 μM) and then incubated with TMab4 for additional 2 h. Internalized TMab4 was stained with TRITC-conjugated anti-human IgG Fc antibody and analyzed by confocal microscopy. Images show the merging of TMab4 (red) and Hochest33342-stained nuclei (blue) at the centered single confocal section. Scale bar represents 5 m.Supplementary Figure S7. Time-lapse live cell imaging to monitor cellular internalization and endosomal release of TMab4. HeLa cells were incubated with Alexa Flour 488-labeled TMab4 (1 μM) and real-time internalization of TMab4 was observed by time-lapse imaging. The dead time between TMab4 treatment and image taking was about 5 min. (A and B) Montage image (A) and quantification of TMab4 internalization and cytosolic accumulation (B), monitored for 2 h with 3 min interval. In (A), representative montage images showing cellular internalization and localization, taken at the indicated times at the centered single confocal section during 2 h TMab4 internalization. Left-top DIC image was added to show cytosolic region and nucleus of cells. Cell boundary was drawn with green line and nucleus was filled with blue color. Image magnification, 630×; scale bar, 10 μm. In (B), measurement of TMab4 fluorescence intensity in the cytosolic regions (n = 13 cells) with the incubation time. Data are presented as mean ± SEM. Supplementary Figure S8. Kinetic parameters for the interactions of C20 and KT4 IgG antibodies with soluble KRS, monitored by SPR. The binding affinity of the anti-KRS antibodies were measured using purified protein by surface resonance plasmon method measured using a BIAcore 2000. (A) SPR sensograms showing the kinetic interactions of C20 and KT4 with surface-immobilized KRS. (B) Kinetic interaction parameters obtained from (A) data using BIAevaluation software. aThe equilibrium dissociation constants (KD1) were calculated from the relationship of KD1 = kd1 / ka1 using the bivalent binding model. bThe apparent equilibrium dissociation constants (KD) including the avidity binding were analyzed using the 1:1 Langmuir model. Each value represents the mean ± SD of two independent experiments. In each experiment, at least five data sets were used in the determination of the kinetic constants.Supplementary Movie S1. Live cell imaging to monitor cellular internalization and endosomal release of Alexa488-labeled TMab4. Movies showing the internalization and endosomal escape of TMab4, tracked for 2 h with 3 min interval. Rapid internalization of TMab4 was indicated by the appearance of small intracellular punctuate structures, the number of which increased with time in the cytoplasmic regions. The cytosolic release of TMab4 was indicated by gradual increase diffuse fluorescence signal intensity in the cytosolic regions.Supplementary Materials and MethodsReagents and antibodies Chlorpromazine (CPZ, C8138), dansylcadaverine (30432), methyl-β-cyclodextrin (MβCD, C4555), nystatin (N6261), 5-(N-Ethyl-N-isopropyl) amiloride (EIPA, A3085), wortmannin (W1628), cytochalasin D (Cyt-D, C8273), dynasore (D7693), MG132 (M7449), rabbit IgG (I5006), FITC-cholera toxin B (Ctx-B, C1655), fluorescein isothiocyanate (FITC) conjugated anti-human IgG (Fc specific, F9512) and tetramethyl-rhodamine isothiocyanate (TRITC) conjugated anti-rabbit IgG (T6778) antibodies were purchased from Sigma-Aldrich. Alexa 488-transferrin (TF, T13342), Oregon green-dextran (D7173), LysoTracker? Red DND-99 (L7528) and were obtained from Invitrogen (Molecular Probes). Horse radish peroxidase (HRP) conjugated anti-mouse IgG (Fc specific, #7076) and anti-p53 (#9282) antibodies were from Cell Signaling. HRP conjugated anti-rabbit IgG (Fc specific, sc-2004), HRP-conjugated anti-goat IgG (Fc specific, sc-2033), anti-β-actin (sc-69879), anti-EEA1 (sc-53939), anti-caveolin-1 (sc-53564), anti-calnexin (sc-70481) and anti-58K Golgi protein (sc-58770) antibodies were purchased from Santa Cruz Biotechnology. Anti-human IgG (Fc specific, 31125) antibody was from Thermo scientific. TRITC-conjugated anti-human IgG (Fc specific, H581) antibody was from Leinco Technologies and anti-KRS mAb was from BIOCON (Medicinal Bioconvergence Research Center, Gyeonggi, Korea).PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5LaW08L0F1dGhvcj48WWVhcj4yMDE0PC9ZZWFyPjxSZWNO
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ADDIN EN.CITE.DATA 7 The recombinant proteins, KRS, histidyl-tRNA synthetase (HRS), tryptophanyl-tRNA synthetase (WRS), and ARS-interacting multifunctional protein 1 (AIMP1), and were provided from BIOCON.PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5LaW08L0F1dGhvcj48WWVhcj4yMDE0PC9ZZWFyPjxSZWNO
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ADDIN EN.CITE.DATA 8 equilibrated with 12 mM sodium phosphate buffer (pH 7.4) containing 500 mM NaCl, 2.7 mM KCl at a flow rate of 0.5 ml/min. Antibodies were analyzed by SEC at a concentration of 200 ?g/ml in 70 ?l of sample volume. Chromatograms were obtained by monitoring absorbance at 280 nm. The molecular mass of antibodies was estimated by calculating elution time into the calibration curve, obtained using standard molecular mass marker (alcohol dehydrogenase, 150 KDa; bovine serum albumin, 66 KDa; carbonic anhydrase, 29 KDa) (Sigma-Aldrich).ELISABinding specificity of antibodies to antigens was determined by ELISA. ELISA plates (Nunc, Invitrogen) were coated for 1 h at 4 °C with the indicated antigens (0.05 ?g/ml of VEGF, 0.1 ?g/ml of TNFα, or 1 ?g/ml of KRS, HRS, WRS, or AIMP1) and blocked with 5% (wt/vol) skim milk. After washing with PBST (PBS pH 7.4, 0.01% Tween-20), diluted antibodies in 5 % (wt/vol) skim milk were applied to each well for 1 h at 25 °C. After washing with PBST, bound antibodies were detected by labeling with alkaline phosphatase-conjugated goat anti-human IgG (Fc-specific) mAb (Sigma-Aldrich) and then incubating with p-nitrophenylphosphate. Absorbance was read at 405 nm on a VersaMax microplate reader (Molecular devices).Surface plasmon resonance (SPR)Kinetic interactions of antibody-protein were measured at 25 °C using Biacore 2000 (GE Healthcare), as previously described. ADDIN EN.CITE <EndNote><Cite><Author>Shin</Author><Year>2014</Year><RecNum>367</RecNum><DisplayText><style face="superscript">9</style></DisplayText><record><rec-number>367</rec-number><foreign-keys><key app="EN" db-id="5sz0e52zssawxcea2xppw558frz5zzs2d02v">367</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Shin, T. H.</author><author>Sung, E. S.</author><author>Kim, Y. J.</author><author>Kim, K. S.</author><author>Kim, S. H.</author><author>Kim, S. K.</author><author>Lee, Y. D.</author><author>Kim, Y. S.</author></authors></contributors><auth-address>Corresponding Author: Yong-Sung Kim, Ajou University, 206 Worldcup-ro, Suwon, 443-749, Korea. kimys@ajou.ac.kr.</auth-address><titles><title>Enhancement of the tumor penetration of monoclonal antibody by fusion of a neuropilin-targeting Peptide improves the antitumor efficacy</title><secondary-title>Mol Cancer Ther</secondary-title><alt-title>Molecular cancer therapeutics</alt-title></titles><periodical><full-title>Mol Cancer Ther</full-title><abbr-1>Molecular cancer therapeutics</abbr-1></periodical><alt-periodical><full-title>Mol Cancer Ther</full-title><abbr-1>Molecular cancer therapeutics</abbr-1></alt-periodical><pages>651-61</pages><volume>13</volume><number>3</number><dates><year>2014</year><pub-dates><date>Mar</date></pub-dates></dates><isbn>1538-8514 (Electronic)
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ADDIN EN.CITE.DATA 10, 11 The apparent equilibrium dissociation constant (KD) including the avidity binding was also calculated using 1:1 Langmuir binding model.PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5QZXJpY2xlb3VzPC9BdXRob3I+PFllYXI+MjAwNTwvWWVh
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ADDIN EN.CITE.DATA 11, 12DNA hydrolyzing assayAs a substrate, supercoiled plasmid pUC19 were purified using a plasmid miniprep kit (Nanohelix, FPL200). DNA hydrolyzing experiments were initiated by mixing proteins such as m3D8 scFv (0.1 ~ 0.5 ?M) and indicated cytotransmabs (0.1 ?M) with DNA substrates (2.2 nM) in a TBS buffer (50 mM Tris-Cl, pH 7.4, 50 mM NaCl) containing either 2 mM MgCl2 or 50 mM EDTA, as previously described previously.PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5LaW08L0F1dGhvcj48WWVhcj4yMDA5PC9ZZWFyPjxSZWNO
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ADDIN EN.CITE.DATA 3, 6 Reactions were performed at 37 °C for 1 h and then terminated by incubating with 50 mM EDTA for 10 min at 37 °C. Samples were analyzed on 0.7 % agarose gel electrophoresis.Live cell imaging Live-cell time-lapse imaging was performed with Nikon A1 confocal system mounted on eclipse T1 microscope and using a 63× oil objective (NA 1.4). The cell incubation chamber was maintained with humidified atmosphere of 5 % CO2 and 37 °C. TMab4 labeled with Alexa Fluor 488 antibody labeling kit (Molecular Probes, Invitrogen) were excited at 488 nm and detected with a 500-530 nm band-pass filter, simultaneously acquiring differential-interference-contrast (DIC) images with excitation at 488 nm and detection in the transmission channel. For imaging, laser power was 0.5 % at 488 nm and gain value was 100. To quantify internalized TMab4 in cytosol for time course, cytosolic area of cells was set as region of interest (ROI) and mean fluorescence intensities were measured in all time points using ImageJ software. Fluorescence photobleaching was compensated by measuring the fluorescence of entire image and applying decreased fluorescence ratio. After background correction, all data were plotted using SigmaPlot software. Flow cytometryTo determine the internalization efficiency of cytotransmabs, HeLa cells were incubated with 1 μM of indicated antibodies for 6 h at 37 °C. After washing the cells with PBS and subsequently with the low pH glycine buffer to remove nonspecifically cell surface-bound antibodies, the cells were trypsinized, fixed, permeabilized, and then blocked prior to the staining of internalized cytotransmabs with Alexa Fluor 488-conjugated anti-human IgG antibody. About 1 × 104 of cells were analyzed using a FACS Calibur flow cytometer (Becton-Dickinson, Franklin Lakes, NJ), as previously described.PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5TdW5nPC9BdXRob3I+PFllYXI+MjAxMDwvWWVhcj48UmVj
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ADDIN EN.CITE.DATA 13Supplementary References ADDIN EN.REFLIST 1.Kabat EA, Wu TT. Identical V region amino acid sequences and segments of sequences in antibodies of different specificities. Relative contributions of VH and VL genes, minigenes, and complementarity-determining regions to binding of antibody-combining sites. J Immunol 1991; 147:1709-19.2.Jang JY, Jeong JG, Jun HR, Lee SC, Kim JS, Kim YS, et al. A nucleic acid-hydrolyzing antibody penetrates into cells via caveolae-mediated endocytosis, localizes in the cytosol and exhibits cytotoxicity. Cell Mol Life Sci 2009; 66:1985-97.3.Lee WR, Jang JY, Kim JS, Kwon MH, Kim YS. Gene silencing by cell-penetrating, sequence-selective and nucleic-acid hydrolyzing antibodies. Nucleic Acids Res 2010; 38:1596-609.4.Hu S, Liang S, Guo H, Zhang D, Li H, Wang X, et al. Comparison of the inhibition mechanisms of adalimumab and infliximab in treating tumor necrosis factor alpha-associated diseases from a molecular view. J Biol Chem 2013; 288:27059-67.5.Vargas-Madrazo E, Paz-Garcia E. An improved model of association for VH-VL immunoglobulin domains: asymmetries between VH and VL in the packing of some interface residues. J Mol Recognit 2003; 16:113-20.6.Kim DS, Lee SH, Kim JS, Lee SC, Kwon MH, Kim YS. Generation of humanized anti-DNA hydrolyzing catalytic antibodies by complementarity determining region grafting. Biochem Biophys Res Commun 2009; 379:314-8.7.Kim DG, Lee JY, Kwon NH, Fang P, Zhang Q, Wang J, et al. Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction. Nat Chem Biol 2014; 10:29-34.8.Lee SH, Park DW, Sung ES, Park HR, Kim JK, Kim YS. Humanization of an agonistic anti-death receptor 4 single chain variable fragment antibody and avidity-mediated enhancement of its cell death-inducing activity. Mol Immunol 2010; 47:816-24.9.Shin TH, Sung ES, Kim YJ, Kim KS, Kim SH, Kim SK, et al. Enhancement of the tumor penetration of monoclonal antibody by fusion of a neuropilin-targeting Peptide improves the antitumor efficacy. Mol Cancer Ther 2014; 13:651-61.10.Lee YH, Iijima M, Kado Y, Mizohata E, Inoue T, Sugiyama A, et al. Construction and characterization of functional anti-epiregulin humanized monoclonal antibodies. Biochem Biophys Res Commun 2013; 441:1011-7.11.Pericleous LM, Richards J, Epenetos AA, Courtenay-Luck N, Deonarain MP. Characterisation and internalisation of recombinant humanised HMFG-1 antibodies against MUC1. Br J Cancer 2005; 93:1257-66.12.Troise F, Cafaro V, Giancola C, D'Alessio G, De Lorenzo C. Differential binding of human immunoagents and Herceptin to the ErbB2 receptor. FEBS J 2008; 275:4967-79.13.Sung ES, Kim A, Park JS, Chung J, Kwon MH, Kim YS. Histone deacetylase inhibitors synergistically potentiate death receptor 4-mediated apoptotic cell death of human T-cell acute lymphoblastic leukemia cells. Apoptosis 2010; 15:1256-69. ................
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