Abstract: An exemplary system, method and computer-accessible medium for determining a location a radioactive seed(s) within a body, can include, for example receiving first imaging information of the radioactive seed(s) within the body based on a first imaging modality, receiving second imaging information of the radioactive seed(s) within the body based on a second imaging modality, and determining the location of the radioactive seed(s) within the body based on the first and second imaging information. The first imaging modality can be computed tomography, and the second imaging modality can be an ultrasound, which can be a transrectal ultrasound. Third information related to a seed implantation plan for a patient(s) can be received.

Abstract: Methods are disclosed for detecting anthrax protective antigen polypeptides and inhibiting their binding to ?2 integrin ?. A domain polypeptides, for example ?2 integrin receptors. The disclosed methods are useful, for example, in diagnosing the presence of an anthrax toxin in the environment or in a subject and also for reducing anthrax intoxication in a subject. The methods can also be used to identify compounds that inhibit binding of an anthrax toxin to a ?2 integrin.

Abstract: Polypeptides comprising all or part of a variant integrin ? subunit A domain and its flanking region are described. In solution or in membrane-associated form, the A domain polypeptides of the invention exists predominantly in a high affinity conformation. In the polypeptides of the invention, referred to as variant integrin polypeptides, a crucial isoleucine or glutamic acid residue is altered. For example, the glutamic acid can be either deleted or replaced with different amino acids residue, e.g., glutamine, aspartic acid, or alanine The variant integrin polypeptides of the invention selectively impair binding of activation-dependent ligands, but not independent ligands. They are useful in screening assays for the identification of molecules that enhance binding of variant polypeptides with impaired binding. In addition, they are useful in distinguishing between activation-dependent ligands and activation-independent ligands. They are also useful for generating antibodies, e.g.

Abstract: Polypeptides comprising all or part of a variant integrin ? subunit A domain and its flanking region are described. In solution or in membrane-associated form, the A domain polypeptides of the invention exists predominantly in a high affinity conformation. In the polypeptides of the invention, referred to as variant integrin polypeptides, a crucial isoleucine or glutamic acid residue is altered. For example, the glutamic acid can be either deleted or replaced with different amino acids residue, e.g., glutamine, aspartic acid, or alanine The variant integrin polypeptides of the invention selectively impair binding of activation-dependent ligands, but not independent ligands. They are useful in screening assays for the identification of molecules that enhance binding of variant polypeptides with impaired binding. In addition, they are useful in distinguishing between activation-dependent ligands and activation-independent ligands. They are also useful for generating antibodies, e.g.

Abstract: The invention features the structural coordinates of a portion of a ?V?3 integrin and the use of the coordinates in methods for identifying molecules which will bind to ?V?3 integrin and, preferably, modulate, e.g., increase or decrease, ?V?3 integrin-mediated adhesion and/or signalling. The identification methods generally involve computer-based structural modelling methods. Such methods can be combined with in vitro or in vivo screening methods to identify candidate therapeutic agent.

Abstract: Polypeptides comprising all or part of a variant integrin ? subunit A domain or a variant integrin ? subunit A-like domain are described. In solution or in membrane-associated form, the A domain or the A-like domain of the polypeptides of the invention exists predominantly in a high affinity conformation. In the polypeptides of the invention, referred to as variant integrin polypeptides, a crucial isoleucine residue (described in greater detail below) is absent. The isoleucine can be either deleted or replaced with different amino acids residue, preferably a smaller or less hydrophobic amino acid residue, e.g., alanine or glycine. Because the variant integrin polypeptides of the invention exist in solution or in membrane-associated form predominantly in a high affinity conformation, they are useful in screening assays for the identification of molecules that bind to (and/or mediate the activity of) an integrin. They are also useful for generating antibodies, e.g.

Abstract: Polypeptides comprising all or part of a variant integrin ? subunit A domain or a variant integrin ? subunit A-like domain are described. In solution or in membrane-associated form, the A domain or the A-like domain of the polypeptides of the invention exists predominantly in a high affinity conformation. In the polypeptides of the invention, referred to as variant integrin polypeptides, a crucial isoleucine residue (described in greater detail below) is absent. The isoleucine can be either deleted or replaced with different amino acids residue, preferably a smaller or less hydrophobic amino acid residue, e.g., alanine or glycine. Because the variant integrin polypeptides of the invention exist in solution or in membrane-associated form predominantly in a high affinity conformation, they are useful in screening assays for the identification of molecules that bind to (and/or mediate the activity of) an integrin. They are also useful for generating antibodies, e.g.

Abstract: Polypeptides comprising all or part of a variant integrin &agr; subunit A domain or a variant integrin &bgr; subunit A-like domain are described. In solution or in membrane-associated form, the A domain or the A-like domain of the polypeptides of the invention exists predominantly in a high affinity conformation. In the polypeptides of the invention, referred to as variant integrin polypeptides, a crucial isoleucine residue (described in greater detail below) is absent. The isoleucine can be either deleted or replaced with different amino acids residue, preferably a smaller or less hydrophobic amino acid residue, e.g., alanine or glycine. Because the variant integrin polypeptides of the invention exist in solution or in membrane-associated form predominantly in a high affinity conformation, they are useful in screening assays for the identification of molecules that bind to (and/or mediate the activity of) an integrin. They are also useful for generating antibodies, e.g.

Abstract: Polypeptides comprising all or part of a variant integrin &agr; subunit A domain and its flanking region are described. In solution or in membrane-associated form, the A domain polypeptides of the invention exists predominantly in a high affinity conformation. In the polypeptides of the invention, referred to as variant integrin polypeptides, a crucial isoleucine or glutamic acid residue is altered. For example, the glutamic acid can be either deleted or replaced with different amino acids residue, e.g., glutamine, aspartic acid, or alanine The variant integrin polypeptides of the invention selectively impair binding of activation-dependent ligands, but not independent ligands. They are useful in screening assays for the identification of molecules that enhance binding of variant polypeptides with impaired binding. In addition, they are useful in distinguishing between activation-dependent ligands and activation-independent ligands. They are also useful for generating antibodies, e.g.

Abstract: Polypeptides comprising all or part of a variant integrin &agr; subunit A domain or a variant integrin &bgr; subunit A-like domain are described. In solution or in membrane-associated form, the A domain or the A-like domain of the polypeptides of the invention exists predominantly in a high affinity conformation. In the polypeptides of the invention, referred to as variant integrin polypeptides, a crucial isoleucine residue (described in greater detail below) is absent. The isoleucine can be either deleted or replaced with different amino acids residue, preferably a smaller or less hydrophobic amino acid residue, e.g., alanine or glycine. Because the variant integrin polypeptides of the invention exist in solution or in membrane-associated form predominantly in a high affinity conformation, they are useful in screening assays for the identification of molecules that bind to (and/or mediate the activity of) an integrin. They are also useful for generating antibodies, e.g.