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Institution

Torrey Pines Institute for Molecular Studies

NonprofitSan Diego, California, United States
About: Torrey Pines Institute for Molecular Studies is a nonprofit organization based out in San Diego, California, United States. It is known for research contribution in the topics: T cell & Antigen. The organization has 2323 authors who have published 2217 publications receiving 112618 citations.


Papers
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Patent
28 Jan 2005
TL;DR: In this article, a modified human growth hormone polypeptides of which amino acid sequence is SEQ ID NO: 2, comprising hGH polypeptic of one non-naturally encoded amino acids are substituted at a residue position of 35 of the SEQID No: 2.
Abstract: The present invention provides modified human growth hormone polypeptides of which amino acid sequence is SEQ ID NO: 2, comprising hGH polypeptides of one non-naturally encoded amino acids. The non-naturally encoded amino acids are substituted at a residue position of 35 of the SEQ ID NO: 2, the human growth hormone polypeptides are in covalent linkage with a 30kDa straight chain polyethylene glycol molecule through an oxime bond, wherein the oxime bond is formed between the non-naturally encoded amino acids and the polyethylene glycol molecule, the non-naturally encoded amino acids are p-acetyl-phenylalanine.

83 citations

Journal ArticleDOI
TL;DR: It is demonstrated that the same CTL epitope can be seen by murine and human CD8+ CTLs, as previously demonstrated for epitopes recognized by CD4+ helper T cells, and suggests the utility of screening for immunodominant C TL epitopes in mice prior to carrying out studies in humans.
Abstract: T-cell-mediated cytotoxicity may play an important role in control of infection by the human immunodeficiency virus (HIV). In this study, we have identified and characterized a relatively conserved epitope in the HIV-1 reverse transcriptase recognized by murine and human cytotoxic T cells. This epitope was identified using a murine antigen-specific CD8+ class I major histocompatibility complex-restricted cytotoxic T-cell (CTL) line, a transfected fibroblast cell line expressing the HIV-1 pol gene, recombinant vaccinia viruses containing different truncated versions of the pol gene, and overlapping synthetic peptides. The optimal antigenic site was identified as residues 203-219 by synthesizing extended or truncated peptide analogs of the antigenic fragment. The optimal peptide was then tested for sensitization of autologous Epstein-Barr virus-transformed B-cell targets for killing by fresh human peripheral blood mononuclear cells. It was recognized by CTLs from several HIV-seropositive patients but not from any seronegative donor. Therefore, this peptide is a good candidate for inclusion in an AIDS vaccine. This study demonstrates that the same CTL epitope can be seen by murine and human CD8+ CTLs, as previously demonstrated for epitopes recognized by CD4+ helper T cells, and suggests the utility of screening for immunodominant CTL epitopes in mice prior to carrying out studies in humans.

83 citations

Journal ArticleDOI
TL;DR: Responsible peptide I-Ag7 dimers induce tolerance of BDC2.5 TCR T cells through a combination of the induction of clonal anergy and anti-inflammatory cytokines and Anti-IL-10R therapy reversed the tolerogenic effects of the dimer.
Abstract: Type 1 diabetes is an autoimmune disorder caused by autoreactive T cells that mediate destruction of insulin-producing beta cells of the pancreas. Studies have shown that T cell tolerance can be restored by inducing a partial or altered signal through the TCR. To investigate the potential of bivalent peptide-MHC class II/Ig fusion proteins as therapeutics to restore Ag-specific tolerance, we have developed soluble peptide I-A(g7) dimers for use in the nonobese diabetic mouse model of diabetes. I-A(g7) dimers with a linked peptide specific for islet-reactive BDC2.5 TCR transgenic CD4(+) T cells were shown to specifically bind BDC2.5 T cells as well as a small population of Ag-specific T cells in nonobese diabetic mice. In vivo treatment with BDC2.5 peptide I-A(g7) dimers protected mice from diabetes mediated by the adoptive transfer of diabetogenic BDC2.5 CD4(+) T cells. The dimer therapy resulted in the activation and increased cell death of transferred BDC2.5 CD4(+) T cells. Surviving cells were hypoproliferative to challenge by Ag and produced increased levels of IL-10 and decreased levels of IFN-gamma compared with cells from control I-A(g7) dimer-treated mice. Anti-IL-10R therapy reversed the tolerogenic effects of the dimer. Thus, peptide I-A(g7) dimers induce tolerance of BDC2.5 TCR T cells through a combination of the induction of clonal anergy and anti-inflammatory cytokines.

83 citations

Journal ArticleDOI
TL;DR: The synthesis of a novel bispecific antibody, αCLL1-αCD3, is described, using the genetically encoded unnatural amino acid, p-acetylphenylalanine, which demonstrates potent and selective cytotoxicity against several human AML cell lines and primary AML patient derived cells in vitro.
Abstract: Acute myeloid leukemia (AML), which is the most common acute adult leukemia and the second most common pediatric leukemia, still has a poor prognosis. Human C-type lectin-like molecule-1 (CLL1) is a recently identified myeloid lineage restricted cell surface marker, which is overexpressed in over 90% of AML patient myeloid blasts and in leukemic stem cells. Here, we describe the synthesis of a novel bispecific antibody, αCLL1-αCD3, using the genetically encoded unnatural amino acid, p-acetylphenylalanine. The resulting αCLL1-αCD3 recruits cytotoxic T cells to CLL1 positive cells, and demonstrates potent and selective cytotoxicity against several human AML cell lines and primary AML patient derived cells in vitro. Moreover, αCLL1-αCD3 treatment completely eliminates established tumors in an U937 AML cell line xenograft model. These results validate the clinical potential of CLL1 as an AML-specific antigen for the generation of a novel immunotherapeutic for AML.

83 citations

Journal ArticleDOI
17 Nov 2011-Blood
TL;DR: It is concluded that Plg-R(KT) plays a key role in the plasminogen-dependent regulation of macrophage invasion, chemotactic migration, and recruitment in the inflammatory response.

82 citations


Authors

Showing all 2327 results

NameH-indexPapersCitations
Eric J. Topol1931373151025
John R. Yates1771036129029
George F. Koob171935112521
Ian A. Wilson15897198221
Peter G. Schultz15689389716
Gerald M. Edelman14754569091
Floyd E. Bloom13961672641
Stuart A. Lipton13448871297
Benjamin F. Cravatt13166661932
Chi-Huey Wong129122066349
Klaus Ley12949557964
Nicholas J. Schork12558762131
Michael Andreeff11795954734
Susan L. McElroy11757044992
Peter E. Wright11544455388
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20235
202210
202153
202060
201950
201842