Binding Proteins - Explore the Science & Experts | ideXlab

Scan Science and Technology

Contact Leading Edge Experts & Companies

Binding Proteins

The Experts below are selected from a list of 255 Experts worldwide ranked by ideXlab platform

Binding Proteins – Free Register to Access Experts & Abstracts

Per-Åke Nygren – One of the best experts on this subject based on the ideXlab platform.

  • alternative Binding Proteins affibody Binding Proteins developed from a small three helix bundle scaffold
    FEBS Journal, 2008
    Co-Authors: Per-Åke Nygren
    Abstract:

    In recent years, classical antibody-based affinity reagents have been challenged by novel types of Binding Proteins developed by combinatorial protein engineering principles. One of these classes of Binding Proteins of non-Ig origin are the so-called affibody Binding Proteins, functionally selected from libraries of a small (6 kDa), non-cysteine three-helix bundle domain used as a scaffold. During the first 10 years since they were first described, high-affinity affibody Binding Proteins have been selected towards a large number of targets for use in a variety of applications, such as bioseparation, diagnostics, functional inhibition, viral targeting and in vivo tumor imaging/therapy. The small size offers the possibility to produce functional affibody Binding Proteins also by chemical synthesis production routes, which has been found to be advantageous for the site-specific introduction of various labels and radionuclide chelators.

  • Alternative Binding Proteins: Affibody Binding Proteins developed from a small three‐helix bundle scaffold
    The FEBS journal, 2008
    Co-Authors: Per-Åke Nygren
    Abstract:

    In recent years, classical antibody-based affinity reagents have been challenged by novel types of Binding Proteins developed by combinatorial protein engineering principles. One of these classes of Binding Proteins of non-Ig origin are the so-called affibody Binding Proteins, functionally selected from libraries of a small (6 kDa), non-cysteine three-helix bundle domain used as a scaffold. During the first 10 years since they were first described, high-affinity affibody Binding Proteins have been selected towards a large number of targets for use in a variety of applications, such as bioseparation, diagnostics, functional inhibition, viral targeting and in vivo tumor imaging/therapy. The small size offers the possibility to produce functional affibody Binding Proteins also by chemical synthesis production routes, which has been found to be advantageous for the site-specific introduction of various labels and radionuclide chelators.

Heinz Breer – One of the best experts on this subject based on the ideXlab platform.

  • Binding Proteins from the antennae of Bombyx mori
    Insect biochemistry and molecular biology, 1996
    Co-Authors: Jurgen Krieger, Paolo Pelosi, E. Von Nickisch-rosenegk, Marina Mameli, Heinz Breer
    Abstract:

    From an antennal library of Bombyx mori cDNA clones encoding different Binding Proteins have been isolated. The deduced amino acid sequences showed only moderate homology to each other but shared several common structural features. Based on a sequence comparison with the antennal Binding Proteins from different moth species, one of the clones appears to encode a pheromone Binding protein, whereas two others represent new members of the two general odorant Binding protein families. A fourth clone encodes a protein which is related to antennal Binding Proteins so far found only in Drosophila melanogaster.

  • odorant Binding Proteins of heliothis virescens
    Insect Biochemistry and Molecular Biology, 1993
    Co-Authors: Jurgen Krieger, Heinz Weiβ, K Raming, Heinz Breer
    Abstract:

    : cDNA clones coding for three different Binding Proteins were isolated from an antennal library of Heliothis virescens. The deduced amino acid sequences showed only moderate homology to each other but shared several common structural features. Based on a comparison with the predicted primary structures of antennal Binding Proteins from different moth species, one of the clones (Hel-1) was found to encode a pheromone Binding protein, whereas the two others (Hel-10 and -11) encode general odorant Binding Proteins.

Stephen A. Morse – One of the best experts on this subject based on the ideXlab platform.

  • The Role of Iron-Binding Proteins in the Survival of Pathogenic Bacteria
    Annual Review of Nutrition, 1994
    Co-Authors: Timothy A. Mietzner, Stephen A. Morse
    Abstract:

    THE ROLE OF IRON-Binding Proteins IN THE PATHOGENESIS OF INFECTIOUS DISEASE . . . . . . . . . . • • • • • • . . . . • • • • • . . . . . . . . • . . • . . . . . 471 Chemistry and Biologic Distribution of Host Iron • • • • • • • • • • • • • • • • • • • • • • • • • • • • 472 HOST IRON-Binding Proteins: THE RESERVOIR OF IRON FOR MICROBIAL PATHOGENS 473 General Classes of Host Iron-Binding Proteins • • • • • • • . • • • • • • . • • . • . • • • • • • • . . • 473 IRON-Binding Proteins OF PATHOGENIC BACfERIA . • • • . . . . • • • • • . • . . . • . 477 Iron-Binding Proteins and Metabolism of Pathogens • • • . • . • • • • • • • • • • • • • • . • • • • 477 Iron-Binding Proteins and Iron Acquisition by Pathogenic Microorganisms • . . . . . . 478 Expression of Iron-Binding Proteins in vivo . • • • • • • • • . . . • • • • . • . . • • • • . . . • • . • . • 487 CONCLUSIONS • . . . . . . . • . . . . . • . . . . . . • • . . . . . • • . . . . . . • • • . . . . . • . . . . . . • . . . . . 488

Jurgen Krieger – One of the best experts on this subject based on the ideXlab platform.

  • Binding Proteins from the antennae of Bombyx mori
    Insect biochemistry and molecular biology, 1996
    Co-Authors: Jurgen Krieger, Paolo Pelosi, E. Von Nickisch-rosenegk, Marina Mameli, Heinz Breer
    Abstract:

    From an antennal library of Bombyx mori cDNA clones encoding different Binding Proteins have been isolated. The deduced amino acid sequences showed only moderate homology to each other but shared several common structural features. Based on a sequence comparison with the antennal Binding Proteins from different moth species, one of the clones appears to encode a pheromone Binding protein, whereas two others represent new members of the two general odorant Binding protein families. A fourth clone encodes a protein which is related to antennal Binding Proteins so far found only in Drosophila melanogaster.

  • odorant Binding Proteins of heliothis virescens
    Insect Biochemistry and Molecular Biology, 1993
    Co-Authors: Jurgen Krieger, Heinz Weiβ, K Raming, Heinz Breer
    Abstract:

    : cDNA clones coding for three different Binding Proteins were isolated from an antennal library of Heliothis virescens. The deduced amino acid sequences showed only moderate homology to each other but shared several common structural features. Based on a comparison with the predicted primary structures of antennal Binding Proteins from different moth species, one of the clones (Hel-1) was found to encode a pheromone Binding protein, whereas the two others (Hel-10 and -11) encode general odorant Binding Proteins.

Timothy A. Mietzner – One of the best experts on this subject based on the ideXlab platform.

  • The Role of Iron-Binding Proteins in the Survival of Pathogenic Bacteria
    Annual Review of Nutrition, 1994
    Co-Authors: Timothy A. Mietzner, Stephen A. Morse
    Abstract:

    THE ROLE OF IRON-Binding Proteins IN THE PATHOGENESIS OF INFECTIOUS DISEASE . . . . . . . . . . • • • • • • . . . . • • • • • . . . . . . . . • . . • . . . . . 471 Chemistry and Biologic Distribution of Host Iron • • • • • • • • • • • • • • • • • • • • • • • • • • • • 472 HOST IRON-Binding Proteins: THE RESERVOIR OF IRON FOR MICROBIAL PATHOGENS 473 General Classes of Host Iron-Binding Proteins • • • • • • • . • • • • • • . • • . • . • • • • • • • . . • 473 IRON-Binding Proteins OF PATHOGENIC BACfERIA . • • • . . . . • • • • • . • . . . • . 477 Iron-Binding Proteins and Metabolism of Pathogens • • • . • . • • • • • • • • • • • • • • . • • • • 477 Iron-Binding Proteins and Iron Acquisition by Pathogenic Microorganisms • . . . . . . 478 Expression of Iron-Binding Proteins in vivo . • • • • • • • • . . . • • • • . • . . • • • • . . . • • . • . • 487 CONCLUSIONS • . . . . . . . • . . . . . • . . . . . . • • . . . . . • • . . . . . . • • • . . . . . • . . . . . . • . . . . . 488