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  1. AU="Finton, Kathryn A K"
  2. AU="Lou Alcaine, María Luz"
  3. AU="Patterson, G Taylor"
  4. AU="Champey, Patrick R" AU="Champey, Patrick R"
  5. AU="Zyriax, Birgit-Christiane"
  6. AU="Kim, Elaine H"
  7. AU="Zhou, Gui-Xiu"
  8. AU="Baer, Rebecca J"
  9. AU="Fleck, Robert J"

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  1. Artikel ; Online: The Broadly Neutralizing, Anti-HIV Antibody 4E10: an Open and Shut Case?

    Strong, Roland K / Finton, Kathryn A K

    Journal of virology

    2016  Band 90, Heft 6, Seite(n) 3274–3275

    Mesh-Begriff(e) Antibodies, Monoclonal/chemistry ; Antibodies, Neutralizing/chemistry ; Epitopes/metabolism ; HIV Antibodies/chemistry ; HIV Envelope Protein gp41/metabolism ; Humans ; Models, Molecular
    Chemische Substanzen Antibodies, Monoclonal ; Antibodies, Neutralizing ; Epitopes ; HIV Antibodies ; HIV Envelope Protein gp41
    Sprache Englisch
    Erscheinungsdatum 2016-03
    Erscheinungsland United States
    Dokumenttyp Comment ; Letter ; Research Support, N.I.H., Extramural
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.02935-15
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Effects of HLA single chain trimer design on peptide presentation and stability.

    Finton, Kathryn A K / Rupert, Peter B / Friend, Della J / Dinca, Ana / Lovelace, Erica S / Buerger, Matthew / Rusnac, Domnita V / Foote-McNabb, Ulysses / Chour, William / Heath, James R / Campbell, Jean S / Pierce, Robert H / Strong, Roland K

    Frontiers in immunology

    2023  Band 14, Seite(n) 1170462

    Abstract: MHC class I " ...

    Abstract MHC class I "
    Mesh-Begriff(e) Humans ; Mice ; Animals ; Histocompatibility Antigens Class I/genetics ; Peptides/metabolism ; Epitopes/chemistry
    Chemische Substanzen Histocompatibility Antigens Class I ; Peptides ; Epitopes
    Sprache Englisch
    Erscheinungsdatum 2023-05-03
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2023.1170462
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: ARTEMIS: A Novel Mass-Spec Platform for HLA-Restricted Self and Disease-Associated Peptide Discovery.

    Finton, Kathryn A K / Brusniak, Mi-Youn / Jones, Lisa A / Lin, Chenwei / Fioré-Gartland, Andrew J / Brock, Chance / Gafken, Philip R / Strong, Roland K

    Frontiers in immunology

    2021  Band 12, Seite(n) 658372

    Abstract: Conventional immunoprecipitation/mass spectroscopy identification of HLA-restricted peptides remains the purview of specializing laboratories, due to the complexity of the methodology, and requires computational post-analysis to assign peptides to ... ...

    Abstract Conventional immunoprecipitation/mass spectroscopy identification of HLA-restricted peptides remains the purview of specializing laboratories, due to the complexity of the methodology, and requires computational post-analysis to assign peptides to individual alleles when using pan-HLA antibodies. We have addressed these limitations with ARTEMIS: a simple, robust, and flexible platform for peptide discovery across ligandomes, optionally including specific proteins-of-interest, that combines novel, secreted HLA-I discovery reagents spanning multiple alleles, optimized lentiviral transduction, and streamlined affinity-tag purification to improve upon conventional methods. This platform fills a middle ground between existing techniques: sensitive and adaptable, but easy and affordable enough to be widely employed by general laboratories. We used ARTEMIS to catalog allele-specific ligandomes from HEK293 cells for seven classical HLA alleles and compared results across replicates, against computational predictions, and against high-quality conventional datasets. We also applied ARTEMIS to identify potentially useful, novel HLA-restricted peptide targets from oncovirus oncoproteins and tumor-associated antigens.
    Mesh-Begriff(e) Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Line ; Epitope Mapping/methods ; Histocompatibility Antigens Class I/immunology ; Histocompatibility Antigens Class II/immunology ; Humans ; Mass Spectrometry/methods ; Mice ; Models, Molecular ; Peptides/chemistry ; Peptides/immunology ; Protein Binding ; Reproducibility of Results ; Structure-Activity Relationship ; Workflow
    Chemische Substanzen Histocompatibility Antigens Class I ; Histocompatibility Antigens Class II ; Peptides
    Sprache Englisch
    Erscheinungsdatum 2021-04-23
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2021.658372
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: A TfR-Binding Cystine-Dense Peptide Promotes Blood-Brain Barrier Penetration of Bioactive Molecules.

    Crook, Zachary R / Girard, Emily / Sevilla, Gregory P / Merrill, Morgan / Friend, Della / Rupert, Peter B / Pakiam, Fiona / Nguyen, Elizabeth / Yin, Chunfeng / Ruff, Raymond O / Hopping, Gene / Strand, Andrew D / Finton, Kathryn A K / Coxon, Margo / Mhyre, Andrew J / Strong, Roland K / Olson, James M

    Journal of molecular biology

    2020  Band 432, Heft 14, Seite(n) 3989–4009

    Abstract: The impenetrability of the blood-brain barrier (BBB) to most conventional drugs impedes the treatment of central nervous system (CNS) disorders. Interventions for diseases like brain cancer, neurodegeneration, or age-associated inflammatory processes ... ...

    Abstract The impenetrability of the blood-brain barrier (BBB) to most conventional drugs impedes the treatment of central nervous system (CNS) disorders. Interventions for diseases like brain cancer, neurodegeneration, or age-associated inflammatory processes require varied approaches to CNS drug delivery. Cystine-dense peptides (CDPs) have drawn recent interest as drugs or drug-delivery vehicles. Found throughout the phylogenetic tree, often in drug-like roles, their size, stability, and protein interaction capabilities make CDPs an attractive mid-size biologic scaffold to complement conventional antibody-based drugs. Here, we describe the identification, maturation, characterization, and utilization of a CDP that binds to the transferrin receptor (TfR), a native receptor and BBB transporter for the iron chaperone transferrin. We developed variants with varying binding affinities (K
    Mesh-Begriff(e) Animals ; Antigens, CD/chemistry ; Antigens, CD/drug effects ; Antigens, CD/genetics ; Antigens, CD/pharmacology ; Blood-Brain Barrier/drug effects ; Central Nervous System/drug effects ; Central Nervous System Diseases/drug therapy ; Cystine/chemistry ; Cystine/genetics ; Drug Delivery Systems ; Humans ; Inflammation/drug therapy ; Inflammation/pathology ; Mice ; Neuropeptides/chemistry ; Neuropeptides/pharmacology ; Neurotensin/chemistry ; Neurotensin/pharmacology ; Peptides/chemistry ; Peptides/pharmacology ; Protein Binding/drug effects ; Receptors, Transferrin/chemistry ; Receptors, Transferrin/drug effects ; Receptors, Transferrin/genetics
    Chemische Substanzen Antigens, CD ; CD71 antigen ; Neuropeptides ; Peptides ; Receptors, Transferrin ; Neurotensin (39379-15-2) ; Cystine (48TCX9A1VT)
    Sprache Englisch
    Erscheinungsdatum 2020-04-15
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2020.04.002
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 867: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Artikel ; Online: HLA-F and MHC-I Open Conformers Bind Natural Killer Cell Ig-Like Receptor KIR3DS1.

    Burian, Aura / Wang, Kevin L / Finton, Kathryn A K / Lee, Ni / Ishitani, Akiko / Strong, Roland K / Geraghty, Daniel E

    PloS one

    2016  Band 11, Heft 9, Seite(n) e0163297

    Abstract: Based on previous findings supporting HLA-F as a ligand for KIR3DL2 and KIR2DS4, we investigated the potential for MHC-I open conformers (OCs) as ligands for KIR3DS1 and KIR3DL1 through interactions measured by surface plasmon resonance. These ... ...

    Abstract Based on previous findings supporting HLA-F as a ligand for KIR3DL2 and KIR2DS4, we investigated the potential for MHC-I open conformers (OCs) as ligands for KIR3DS1 and KIR3DL1 through interactions measured by surface plasmon resonance. These measurements showed physical binding of KIR3DS1 but not KIR3DL1 with HLA-F and other MHC-I OC while also confirming the allotype specific binding of KIR3DL1 with MHC-I peptide complex. Concordant results were obtained with biochemical pull-down from cell lines and biochemical heterodimerization experiments with recombinant proteins. In addition, surface binding of HLA-F and KIR3DS1 to native and activated NK and T cells was coincident with specific expression of the putative ligand or receptor. A functional response of KIR3DS1 was indicated by increased granule exocytosis in activated cells incubated with HLA-F bound to surfaces. The data extend a model for interaction between MHC-I open conformers and activating KIR receptors expressed during an inflammatory response, potentially contributing to communication between the innate and adaptive immune response.
    Mesh-Begriff(e) Histocompatibility Antigens Class I/metabolism ; Humans ; Killer Cells, Natural/cytology ; Killer Cells, Natural/metabolism ; Leukocytes, Mononuclear/cytology ; Leukocytes, Mononuclear/metabolism ; Models, Molecular ; Protein Binding ; Protein Folding ; Receptors, KIR3DS1/metabolism
    Chemische Substanzen HLA-F antigens ; Histocompatibility Antigens Class I ; Receptors, KIR3DS1
    Sprache Englisch
    Erscheinungsdatum 2016
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0163297
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Ontogeny of recognition specificity and functionality for the broadly neutralizing anti-HIV antibody 4E10.

    Finton, Kathryn A K / Friend, Della / Jaffe, James / Gewe, Mesfin / Holmes, Margaret A / Larman, H Benjamin / Stuart, Andrew / Larimore, Kevin / Greenberg, Philip D / Elledge, Stephen J / Stamatatos, Leonidas / Strong, Roland K

    PLoS pathogens

    2014  Band 10, Heft 9, Seite(n) e1004403

    Abstract: The process of antibody ontogeny typically improves affinity, on-rate, and thermostability, narrows polyspecificity, and rigidifies the combining site to the conformer optimal for binding from the broader ensemble accessible to the precursor. However, ... ...

    Abstract The process of antibody ontogeny typically improves affinity, on-rate, and thermostability, narrows polyspecificity, and rigidifies the combining site to the conformer optimal for binding from the broader ensemble accessible to the precursor. However, many broadly-neutralizing anti-HIV antibodies incorporate unusual structural elements and recognition specificities or properties that often lead to autoreactivity. The ontogeny of 4E10, an autoreactive antibody with unexpected combining site flexibility, was delineated through structural and biophysical comparisons of the mature antibody with multiple potential precursors. 4E10 gained affinity primarily by off-rate enhancement through a small number of mutations to a highly conserved recognition surface. Controverting the conventional paradigm, the combining site gained flexibility and autoreactivity during ontogeny, while losing thermostability, though polyspecificity was unaffected. Details of the recognition mechanism, including inferred global effects due to 4E10 binding, suggest that neutralization by 4E10 may involve mechanisms beyond simply binding, also requiring the ability of the antibody to induce conformational changes distant from its binding site. 4E10 is, therefore, unlikely to be re-elicited by conventional vaccination strategies.
    Mesh-Begriff(e) Amino Acid Sequence ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Antibody Specificity ; Broadly Neutralizing Antibodies ; Crystallography, X-Ray ; HIV Antibodies/chemistry ; HIV Antibodies/immunology ; HIV Antibodies/metabolism ; HIV Infections/immunology ; HIV Infections/virology ; HIV-1/immunology ; Humans ; Molecular Sequence Data ; Neutralization Tests ; Sequence Homology, Amino Acid ; Surface Plasmon Resonance
    Chemische Substanzen 4E10 monoclonal antibody ; Antibodies, Monoclonal ; Broadly Neutralizing Antibodies ; HIV Antibodies
    Sprache Englisch
    Erscheinungsdatum 2014-09-25
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1004403
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Autoreactivity and exceptional CDR plasticity (but not unusual polyspecificity) hinder elicitation of the anti-HIV antibody 4E10.

    Finton, Kathryn A K / Larimore, Kevin / Larman, H Benjamin / Friend, Della / Correnti, Colin / Rupert, Peter B / Elledge, Stephen J / Greenberg, Philip D / Strong, Roland K

    PLoS pathogens

    2013  Band 9, Heft 9, Seite(n) e1003639

    Abstract: The broadly-neutralizing anti-HIV antibody 4E10 recognizes an epitope in the membrane-proximal external region of the HIV envelope protein gp41. Previous attempts to elicit 4E10 by vaccination with envelope-derived or reverse-engineered immunogens have ... ...

    Abstract The broadly-neutralizing anti-HIV antibody 4E10 recognizes an epitope in the membrane-proximal external region of the HIV envelope protein gp41. Previous attempts to elicit 4E10 by vaccination with envelope-derived or reverse-engineered immunogens have failed. It was presumed that the ontogeny of 4E10-equivalent responses was blocked by inherent autoreactivity and exceptional polyreactivity. We generated 4E10 heavy-chain knock-in mice, which displayed significant B cell dysregulation, consistent with recognition of autoantigen/s by 4E10 and the presumption that tolerance mechanisms may hinder the elicitation of 4E10 or 4E10-equivalent responses. Previously proposed candidate 4E10 autoantigens include the mitochondrial lipid cardiolipin and a nuclear splicing factor, 3B3. However, using carefully-controlled assays, 4E10 bound only weakly to cardiolipin-containing liposomes, but also bound negatively-charged, non-cardiolipin-containing liposomes comparably poorly. 4E10/liposome binding was predominantly mediated by electrostatic interactions rather than presumed hydrophobic interactions. The crystal structure of 4E10 free of bound ligands showed a dramatic restructuring of the combining site, occluding the HIV epitope binding site and revealing profound flexibility, but creating an electropositive pocket consistent with non-specific binding of phospholipid headgroups. These results strongly suggested that antigens other than cardiolipin mediate 4E10 autoreactivity. Using a synthetic peptide library spanning the human proteome, we determined that 4E10 displays limited and focused, but unexceptional, polyspecificity. We also identified a novel autoepitope shared by three ER-resident inositol trisphosphate receptors, validated through binding studies and immunohistochemistry. Tissue staining with 4E10 demonstrated reactivity consistent with the type 1 inositol trisphosphate receptor as the most likely candidate autoantigen, but is inconsistent with splicing factor 3B3. These results demonstrate that 4E10 recognition of liposomes competes with MPER recognition and that HIV antigen and autoepitope recognition may be distinct enough to permit eliciting 4E10-like antibodies, evading autoimmunity through directed engineering. However, 4E10 combining site flexibility, exceptional for a highly-matured antibody, may preclude eliciting 4E10 by conventional immunization strategies.
    Mesh-Begriff(e) Animals ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; Autoantibodies/genetics ; Autoantibodies/immunology ; Autoantigens/genetics ; Autoantigens/immunology ; Broadly Neutralizing Antibodies ; Cardiolipins/genetics ; Cardiolipins/immunology ; Complementarity Determining Regions/genetics ; Complementarity Determining Regions/immunology ; Epitopes/genetics ; Epitopes/immunology ; HIV Antibodies/genetics ; HIV Antibodies/immunology ; HIV-1/immunology ; Humans ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Heavy Chains/immunology ; Inositol 1,4,5-Trisphosphate Receptors/genetics ; Inositol 1,4,5-Trisphosphate Receptors/immunology ; Mice ; Mice, Transgenic ; Proteome/genetics ; Proteome/immunology
    Chemische Substanzen 4E10 monoclonal antibody ; Antibodies, Monoclonal ; Autoantibodies ; Autoantigens ; Broadly Neutralizing Antibodies ; Cardiolipins ; Complementarity Determining Regions ; Epitopes ; HIV Antibodies ; Immunoglobulin Heavy Chains ; Inositol 1,4,5-Trisphosphate Receptors ; Proteome
    Sprache Englisch
    Erscheinungsdatum 2013-09-26
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7366
    ISSN (online) 1553-7374
    ISSN 1553-7366
    DOI 10.1371/journal.ppat.1003639
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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