Abstract: In one aspect the present invention provides methods for assessing a physiological state of a mammalian retina in vivo, the methods of this aspect of the invention each include the steps of (a) irradiating a portion of a mammalian retina, in vivo, with light having a wavelength in the range of from 600 nm to 1000 nm at an intensity sufficient to stimulate two-photon-induced fluorescence in the retina; and (b) assessing a physiological state of the retina by analyzing the fluorescence.

Abstract: In one aspect the present invention provides methods for assessing a physiological state of a mammalian retina in vivo, the methods of this aspect of the invention each include the steps of (a) irradiating a portion of a mammalian retina, in vivo, with light having a wavelength in the range of from 600 nm to 1000 nm at an intensity sufficient to stimulate two-photon-induced fluorescence in the retina; and (b) assessing a physiological state of the retina by analyzing the fluorescence.

Abstract: In one aspect the present invention provides methods for assessing a physiological state of a mammalian retina in vivo, the methods of this aspect of the invention each include the steps of: (a) irradiating a portion of a mammalian retina, in vivo, with light having a wavelength in the range of from 600 nm to 1000 nm at an intensity sufficient to stimulate two-photon-induced fluorescence in the retina; and (b) assessing a physiological state of the retina by analyzing the fluorescence.

Abstract: A textured, demineralized, and unitary mammalian bone section for providing a rigid, foraminous, collagen scaffold for allogenic skeletal reconstruction. The allograft is prepared by treating a section of cadaver bone to remove all soft tissue, then texturing the bone surface to produce a pattern of holes of selected size, density, and depth, and finally demineralizing the bone section to leave a rigid, insoluble collagen scaffold suitable for osteoinduction upon implantation. All such steps are performed with minimal denaturing of the extracellular matrix proteins which remain bound to the collagen scaffold and which are necessary to complete the process of new bone formation.

Abstract: A cartilage-inducing factor has been isolated from dentin and characterized as a polypeptide having an apparent molecular weight of 6,000 to 8,500, an isoelectric pH of from 4.5 to 6.5, and, biologically, as being capable of inducing muscle fibroblast cells to produce cartilage-specific proteoglycan and Type II collagen.