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PMID |
Sentence |
1 |
3192279
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The humoral antibody response of CAF1 mice to low doses (1-100 micrograms) of egg albumin (EA) encapsulated in or covalently bound to the surface of liposomes was studied for three routes of administration.
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2 |
8422670
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The immune response of CAF1 mice to various synthetic peptides (SP) related to the amino acid sequence (PDTRPAPGSTAPPAHGVTSA) of the tandem repeat of the MUC1 human breast mucin core peptide was evaluated.
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3 |
16840777
|
Sequential proteolytic processing of the capsular Caf1 antigen of Yersinia pestis for major histocompatibility complex class II-restricted presentation to T lymphocytes.
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4 |
16840777
|
We studied the mechanisms of antigen presentation of CD4 T cell epitopes of the capsular Caf1 antigen of Yersinia pestis using murine bone marrow macrophages as antigen presenting cells and T cell hybridomas specific for major histocompatibility complex (MHC) class II-restricted epitopes distributed throughout the Caf1 sequence.
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5 |
16840777
|
The data revealed diversity in the pathways used and the degrees of antigen processing required depending on the structural context of epitopes within the Caf1 molecule.
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6 |
16840777
|
A fourth epitope located between the two regions of Caf1 showed intermediate behavior.
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7 |
16840777
|
The Caf1 capsular protein is a component of second generation plague vaccines and an understanding of the mechanisms and pathways of MHC class II-restricted presentation of multiple epitopes from this candidate vaccine antigen should inform the choice of delivery systems and adjuvants that target vaccines successfully to appropriate intracellular locations to induce protective immune responses against as wide a T cell repertoire as possible.
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8 |
16840777
|
Sequential proteolytic processing of the capsular Caf1 antigen of Yersinia pestis for major histocompatibility complex class II-restricted presentation to T lymphocytes.
|
9 |
16840777
|
We studied the mechanisms of antigen presentation of CD4 T cell epitopes of the capsular Caf1 antigen of Yersinia pestis using murine bone marrow macrophages as antigen presenting cells and T cell hybridomas specific for major histocompatibility complex (MHC) class II-restricted epitopes distributed throughout the Caf1 sequence.
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10 |
16840777
|
The data revealed diversity in the pathways used and the degrees of antigen processing required depending on the structural context of epitopes within the Caf1 molecule.
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11 |
16840777
|
A fourth epitope located between the two regions of Caf1 showed intermediate behavior.
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12 |
16840777
|
The Caf1 capsular protein is a component of second generation plague vaccines and an understanding of the mechanisms and pathways of MHC class II-restricted presentation of multiple epitopes from this candidate vaccine antigen should inform the choice of delivery systems and adjuvants that target vaccines successfully to appropriate intracellular locations to induce protective immune responses against as wide a T cell repertoire as possible.
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13 |
16840777
|
Sequential proteolytic processing of the capsular Caf1 antigen of Yersinia pestis for major histocompatibility complex class II-restricted presentation to T lymphocytes.
|
14 |
16840777
|
We studied the mechanisms of antigen presentation of CD4 T cell epitopes of the capsular Caf1 antigen of Yersinia pestis using murine bone marrow macrophages as antigen presenting cells and T cell hybridomas specific for major histocompatibility complex (MHC) class II-restricted epitopes distributed throughout the Caf1 sequence.
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15 |
16840777
|
The data revealed diversity in the pathways used and the degrees of antigen processing required depending on the structural context of epitopes within the Caf1 molecule.
|
16 |
16840777
|
A fourth epitope located between the two regions of Caf1 showed intermediate behavior.
|
17 |
16840777
|
The Caf1 capsular protein is a component of second generation plague vaccines and an understanding of the mechanisms and pathways of MHC class II-restricted presentation of multiple epitopes from this candidate vaccine antigen should inform the choice of delivery systems and adjuvants that target vaccines successfully to appropriate intracellular locations to induce protective immune responses against as wide a T cell repertoire as possible.
|
18 |
16840777
|
Sequential proteolytic processing of the capsular Caf1 antigen of Yersinia pestis for major histocompatibility complex class II-restricted presentation to T lymphocytes.
|
19 |
16840777
|
We studied the mechanisms of antigen presentation of CD4 T cell epitopes of the capsular Caf1 antigen of Yersinia pestis using murine bone marrow macrophages as antigen presenting cells and T cell hybridomas specific for major histocompatibility complex (MHC) class II-restricted epitopes distributed throughout the Caf1 sequence.
|
20 |
16840777
|
The data revealed diversity in the pathways used and the degrees of antigen processing required depending on the structural context of epitopes within the Caf1 molecule.
|
21 |
16840777
|
A fourth epitope located between the two regions of Caf1 showed intermediate behavior.
|
22 |
16840777
|
The Caf1 capsular protein is a component of second generation plague vaccines and an understanding of the mechanisms and pathways of MHC class II-restricted presentation of multiple epitopes from this candidate vaccine antigen should inform the choice of delivery systems and adjuvants that target vaccines successfully to appropriate intracellular locations to induce protective immune responses against as wide a T cell repertoire as possible.
|
23 |
16840777
|
Sequential proteolytic processing of the capsular Caf1 antigen of Yersinia pestis for major histocompatibility complex class II-restricted presentation to T lymphocytes.
|
24 |
16840777
|
We studied the mechanisms of antigen presentation of CD4 T cell epitopes of the capsular Caf1 antigen of Yersinia pestis using murine bone marrow macrophages as antigen presenting cells and T cell hybridomas specific for major histocompatibility complex (MHC) class II-restricted epitopes distributed throughout the Caf1 sequence.
|
25 |
16840777
|
The data revealed diversity in the pathways used and the degrees of antigen processing required depending on the structural context of epitopes within the Caf1 molecule.
|
26 |
16840777
|
A fourth epitope located between the two regions of Caf1 showed intermediate behavior.
|
27 |
16840777
|
The Caf1 capsular protein is a component of second generation plague vaccines and an understanding of the mechanisms and pathways of MHC class II-restricted presentation of multiple epitopes from this candidate vaccine antigen should inform the choice of delivery systems and adjuvants that target vaccines successfully to appropriate intracellular locations to induce protective immune responses against as wide a T cell repertoire as possible.
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28 |
16982834
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We compared the immunogenicity of the engineered monomer with polymeric Caf1 in antigen presentation assays to CD4 T-cell hybridomas in vitro, as well as in the induction of antibody responses and protection against subcutaneous challenge with Y. pestis in vivo.
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29 |
20600492
|
The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states.
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30 |
20600492
|
Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism.
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31 |
20600492
|
Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa).
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32 |
20600492
|
The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins.
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33 |
20600492
|
Caf1, hemocyanin and anthrax PA are all resolved clearly and Caf1 exhibits adjuvant bound stretches with long intervening loops draped from the edges.
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34 |
20600492
|
The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states.
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35 |
20600492
|
Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism.
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36 |
20600492
|
Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa).
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37 |
20600492
|
The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins.
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38 |
20600492
|
Caf1, hemocyanin and anthrax PA are all resolved clearly and Caf1 exhibits adjuvant bound stretches with long intervening loops draped from the edges.
|
39 |
20600492
|
The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states.
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40 |
20600492
|
Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism.
|
41 |
20600492
|
Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa).
|
42 |
20600492
|
The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins.
|
43 |
20600492
|
Caf1, hemocyanin and anthrax PA are all resolved clearly and Caf1 exhibits adjuvant bound stretches with long intervening loops draped from the edges.
|
44 |
20600492
|
The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states.
|
45 |
20600492
|
Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism.
|
46 |
20600492
|
Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa).
|
47 |
20600492
|
The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins.
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48 |
20600492
|
Caf1, hemocyanin and anthrax PA are all resolved clearly and Caf1 exhibits adjuvant bound stretches with long intervening loops draped from the edges.
|
49 |
20600492
|
The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states.
|
50 |
20600492
|
Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism.
|
51 |
20600492
|
Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa).
|
52 |
20600492
|
The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins.
|
53 |
20600492
|
Caf1, hemocyanin and anthrax PA are all resolved clearly and Caf1 exhibits adjuvant bound stretches with long intervening loops draped from the edges.
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54 |
20660611
|
Repertoire of HLA-DR1-restricted CD4 T-cell responses to capsular Caf1 antigen of Yersinia pestis in human leukocyte antigen transgenic mice.
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55 |
20660611
|
The capsular Caf1 protein of Y. pestis is a protective antigen under development as a recombinant vaccine.
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56 |
20660611
|
We characterized CD4 T-cell epitopes of Caf1 in "humanized" HLA-DR1 transgenic mice lacking endogenous major histocompatibility complex class II molecules.
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57 |
20660611
|
Mice were immunized with Caf1 or each of a complete set of overlapping synthetic peptides, and CD4 T-cell immunity was measured with respect to proliferative and gamma interferon T-cell responses and recognition by a panel of T-cell hybridomas, as well as direct determination of binding affinities of Caf1 peptides to purified HLA-DR molecules.
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58 |
20660611
|
Although a number of DR1-restricted epitopes were identified following Caf1 immunization, the response was biased toward a single immunodominant epitope near the C terminus of Caf1.
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59 |
20660611
|
Repertoire of HLA-DR1-restricted CD4 T-cell responses to capsular Caf1 antigen of Yersinia pestis in human leukocyte antigen transgenic mice.
|
60 |
20660611
|
The capsular Caf1 protein of Y. pestis is a protective antigen under development as a recombinant vaccine.
|
61 |
20660611
|
We characterized CD4 T-cell epitopes of Caf1 in "humanized" HLA-DR1 transgenic mice lacking endogenous major histocompatibility complex class II molecules.
|
62 |
20660611
|
Mice were immunized with Caf1 or each of a complete set of overlapping synthetic peptides, and CD4 T-cell immunity was measured with respect to proliferative and gamma interferon T-cell responses and recognition by a panel of T-cell hybridomas, as well as direct determination of binding affinities of Caf1 peptides to purified HLA-DR molecules.
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63 |
20660611
|
Although a number of DR1-restricted epitopes were identified following Caf1 immunization, the response was biased toward a single immunodominant epitope near the C terminus of Caf1.
|
64 |
20660611
|
Repertoire of HLA-DR1-restricted CD4 T-cell responses to capsular Caf1 antigen of Yersinia pestis in human leukocyte antigen transgenic mice.
|
65 |
20660611
|
The capsular Caf1 protein of Y. pestis is a protective antigen under development as a recombinant vaccine.
|
66 |
20660611
|
We characterized CD4 T-cell epitopes of Caf1 in "humanized" HLA-DR1 transgenic mice lacking endogenous major histocompatibility complex class II molecules.
|
67 |
20660611
|
Mice were immunized with Caf1 or each of a complete set of overlapping synthetic peptides, and CD4 T-cell immunity was measured with respect to proliferative and gamma interferon T-cell responses and recognition by a panel of T-cell hybridomas, as well as direct determination of binding affinities of Caf1 peptides to purified HLA-DR molecules.
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68 |
20660611
|
Although a number of DR1-restricted epitopes were identified following Caf1 immunization, the response was biased toward a single immunodominant epitope near the C terminus of Caf1.
|
69 |
20660611
|
Repertoire of HLA-DR1-restricted CD4 T-cell responses to capsular Caf1 antigen of Yersinia pestis in human leukocyte antigen transgenic mice.
|
70 |
20660611
|
The capsular Caf1 protein of Y. pestis is a protective antigen under development as a recombinant vaccine.
|
71 |
20660611
|
We characterized CD4 T-cell epitopes of Caf1 in "humanized" HLA-DR1 transgenic mice lacking endogenous major histocompatibility complex class II molecules.
|
72 |
20660611
|
Mice were immunized with Caf1 or each of a complete set of overlapping synthetic peptides, and CD4 T-cell immunity was measured with respect to proliferative and gamma interferon T-cell responses and recognition by a panel of T-cell hybridomas, as well as direct determination of binding affinities of Caf1 peptides to purified HLA-DR molecules.
|
73 |
20660611
|
Although a number of DR1-restricted epitopes were identified following Caf1 immunization, the response was biased toward a single immunodominant epitope near the C terminus of Caf1.
|
74 |
20660611
|
Repertoire of HLA-DR1-restricted CD4 T-cell responses to capsular Caf1 antigen of Yersinia pestis in human leukocyte antigen transgenic mice.
|
75 |
20660611
|
The capsular Caf1 protein of Y. pestis is a protective antigen under development as a recombinant vaccine.
|
76 |
20660611
|
We characterized CD4 T-cell epitopes of Caf1 in "humanized" HLA-DR1 transgenic mice lacking endogenous major histocompatibility complex class II molecules.
|
77 |
20660611
|
Mice were immunized with Caf1 or each of a complete set of overlapping synthetic peptides, and CD4 T-cell immunity was measured with respect to proliferative and gamma interferon T-cell responses and recognition by a panel of T-cell hybridomas, as well as direct determination of binding affinities of Caf1 peptides to purified HLA-DR molecules.
|
78 |
20660611
|
Although a number of DR1-restricted epitopes were identified following Caf1 immunization, the response was biased toward a single immunodominant epitope near the C terminus of Caf1.
|