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1.
Figure 4

Figure 4. From: In vitro evolution of a T cell receptor with high affinity for peptide/MHC.

QL9/Ld binding by soluble scTCRs. T2-Ld cells loaded with QL9 were incubated with 125I-labeled anti-Ld Fab fragments (30–5-7) and various concentrations of unlabeled Fab (□), scTCR-T7 (■), or mutant scTCR-m6 (●). Bound and unbound [125I]30–5-7 Fab fragments were separated by centrifugation through olive oil/dibutyl phthalate. Binding of 125I-labeled anti-Ld Fab fragments to T2-Ld cells loaded with the control peptide MCMV was not inhibited even at the highest concentrations of scTCRs (data not shown).

Phillip D. Holler, et al. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5387-5392.

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2.
Figure 5

Figure 5. From: In vitro evolution of a T cell receptor with high affinity for peptide/MHC.

Flow cytometric analysis of the binding of scTCR/biotin to cell surface peptide/MHC. Peptide-loaded T2-Ld cells were incubated with biotinylated m6 scTCR (≈0.3 μM) or T7 scTCR (≈1.6 μM) scTCR followed by streptavidin-PE and analyzed by flow cytometry. (A) Flow cytometry histograms of T2-Ld cells loaded with QL9 (unshaded), p2Ca (light shade), or MCMV (dark shade) and stained with m6 scTCR/biotin. (B) Mean fluorescent units (MFU) of T2-Ld cells loaded with QL9, p2Ca, or MCMV and stained with either secondary SA-PE only, T7 scTCR/biotin + SA-PE, or m6 scTCR/biotin + SA-PE.

Phillip D. Holler, et al. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5387-5392.

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3.
Figure 3

Figure 3. From: In vitro evolution of a T cell receptor with high affinity for peptide/MHC.

Fine specificity analysis of mutant scTCR binding to different QL9 variant peptides bound to Ld. The original T cell clone 2C and various yeast clones were analyzed by flow cytometry for binding to Ld/Ig dimers loaded with wild-type QL9 (QL9–5F), position 5 variants of QL9 (QL9–5Y, QL9–5H, and QL9–5E) or MCMV. Binding was detected with FITC-labeled goat anti-mouse IgG. Relative fluorescence was measured by comparison with mean fluorescence values of 2C cells or yeast cells stained with anti-Vβ8 antibody F23.2.

Phillip D. Holler, et al. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5387-5392.

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4.
Figure 2

Figure 2. From: In vitro evolution of a T cell receptor with high affinity for peptide/MHC.

Structure and sequences of the 2C TCR CDR3α. (A) X-ray crystallographic structure of the 2C/dEV8/Kb complex with CDR3α aa highlighted. Five residues of the 2C VαCDR3 that were randomized by PCR with a degenerate primer are shown in red. The adjacent CDR3 residues, Ser-93 and Leu-104 shown in blue, were retained in the yeast display library because they have been shown to be important in pMHC binding (, , ). (B) Alignment of aa sequences of mutant scTCRs isolated by yeast display and selection with QL9/Ld. Display plasmids were isolated from yeast clones after selection and sequenced to determine CDR3α sequences. Mutants m1, m2, m3, m4, m10, and m11 were isolated after the third round of sorting. All other mutants were isolated after the fourth round of sorting.

Phillip D. Holler, et al. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5387-5392.

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5.
Figure 1

Figure 1. From: In vitro evolution of a T cell receptor with high affinity for peptide/MHC.

Flow cytometric analysis of yeast cells that express wild-type and mutant 2C TCR on their surface. Yeast cells displaying wild-type (T7) and mutant (m6 and m13) scTCR were stained with anti-Vβ8 antibody F23.2 (120 nM), the specific alloantigenic peptide-MHC, QL9/Ld/Ig (40 nM), or a null peptide MCMV/Ld/Ig (40 nM). The peptides used in this study were QL9 (QLSPFPFDL), MCMV (YPHFMPTNL), and p2Ca (LSPFPFDL). Binding was detected by FITC-conjugated goat anti-mouse IgG F(ab′)2 and analyzed by flow cytometry. The negative population (e.g., seen with F23.2 staining) has been observed for all yeast-displayed proteins and is thought to be caused by cells at a stage of growth or induction that are incapable of expressing surface fusion protein (, , ).

Phillip D. Holler, et al. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5387-5392.

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