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A novel two- and three-dimensional autoradiographic device offers to improve the imaging of body tissues. Numerous methods and apparati have been proposed to produce a three-dimensional map or image of a distribution of radioactively-tagged tissues or chemical substances; however, many of these devices merely detect the radiation, not image it. This new device uses a charged coupling device (CCD) in combination with a microtome to produce numerous two-dimensional images of the radioactively-tagged tissue.

The second leading cause of death in the United States is cancer and more than one million Americans are diagnosed with cancer each year, with this number likely to increase as the population ages.

Multiple Sclerosis (MS) is a life-long chronic autoimmune disease diagnosed primarily in young adults who have a virtually normal life expectancy. Estimates place the annual costs of MS in the United States in excess of $2.5 billion. There are approximately 250,000 to 400,000 persons in the United States with MS, and approximately 2.5 million persons worldwide suffer from MS. A variety of therapies are used to treat MS, but there is no single therapy that can be used to treat all patients.

SMADs are a novel set of mammalian proteins that act downstream of TGF-beta family ligands. These proteins can be categorized into three distinct functional sets, receptor-activated SMADs (SMADs 1,2,3,5, and 8), the common mediator SMAD (SMAD 4), and inhibitory SMADs (SMADs 6 and 7). SMAD proteins are thought to play a role in vertebrate development and tumorigenesis.

Biological materials are important research tools that can be used for diagnostic as well as therapeutic purposes. Antibodies have become viable drugs in the market today and there is a general market need for systems that may facilitate production of efficient and effective antibodies. In recent years, monoclonal antibodies have gained significant importance in their use, both as diagnostics and therapeutics, to intervene and combat diseases such as cancer, cardiovascular diseases, and infections.

In many instances, it is desirable to express exogenous genes only in certain tissues, and/or at will at certain times, and/or only to a certain degree. However, current gene transfer and exogenous gene expression protocols do not provide adequate means of simultaneously controlling which cells in a heterogeneous population are transformed and when, where, and to what degree the transferred genes are expressed. The invention provides methods for using local heat to control gene expression.

Autoreactive T cell clones such as TL3A6 and TL5F6 that recognize an autoantigen, which is potentially relevant for an autoimmune disease, for example, multiple sclerosis (MS), offer the potential to examine the disease pathogenesis and develop new treatments. Such treatments aim at disrupting or interfering with the specific interaction between autoreactive T cells, antigen presenting cells and antigenic peptide. Current treatments have immunomodulatory effects and side effects. These T cell lines will be useful for developing novel treatment approaches for multiple sclerosis.

The present invention relates to the field of apoptosis, in particular, it relates to apoptosis-modifying fusion proteins with at least two domains, one of which targets the fusion proteins to a target cell, and another of which modifies an apoptotic response of the target cell. For example, fusing various cell-binding domains to Bcl-X_L and Bad allows targeting to specific subsets of cells in vivo, permitting treatment and/or prevention of cell-death related consequences of various diseases and injuries.

The claimed invention provides a method of detecting the presence of a parvovirus in a sample. Parvoviruses infect animals and man. In man, the only known pathogenic member of this family is parvovirus B19. The inventors have identified the parvovirus B19 receptor which provides for a method to diagnose, prevent, and treat parvovirus infection utilizing the binding affinity for the receptor.

Neurotransmitter release is dependent on a binding complex (designated as SNAR) of three proteins, synaptic-vesicle-associated protein synaptobrevin/VAMP, syntaxin and SNAP-25 (snaptosome-associated protein-25) with results in a calcium dependent fusion between synaptic vesicles and the presynaptic terminal. SNAPIN, a neuron specific protein found predominately on synaptic vesicles, binds to the SNAR complex, most likely to the SNAP-25.