Results 191 to 200 of about 25,202 (233)
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Differential Expression of Tenascin-C, Tenascin-R, Tenascin/J1, and Tenascin-X in Spinal Cord Scar Tissue and in the Olfactory System

Experimental Neurology, 2000
The members of the tenascin family are involved in a number of developmental processes, mainly by their ability to regulate cell adhesion. We have here studied the distribution of mRNAs for tenascin-X, -C, and -R and the closely related molecule tenascin/J1 in the olfactory system and spinal cord. The olfactory bulb and nasal mucosa were studied during
M, Deckner   +3 more
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Tenascin-C

International Journal of Biochemistry and Cell Biology, 1997
Eleanor J. Mackie
exaly   +2 more sources

Tenascins in CNS lesions

Seminars in Cell & Developmental Biology, 2019
The tenascin family of glycoproteins comprises four members in vertebrates, of which tenascin-C (Tnc) and tenascin-R (Tnr) are particularly important in the context of lesions in the central nervous system (CNS). Tnc is expressed in the developing CNS, before it is down-regulated and mainly restricted to the adult neural stem cell niches.
Lars Roll, Andreas Faissner
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Tenascin in human neoplasia

International Journal of Oncology, 1996
Tenascin (TN), a recently characterized extracellular matrix protein, largely confined to the process with the development of embryo in areas of epithelial-mesenchymal interactions, developing neural tissues, bone and cartilage where there are morphogenetic movements and tissue patterning, has a highly restricted expression in adult tissues.
P, Shrestha, M, Kusakabe, M, Mori
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Tenascin-C knockout mouse has no detectable tenascin-C protein

Journal of Neuroscience Research, 1997
A recent study by Mitrovic and Schachner (J Neurosci Res 42:710-717, 1995) reported the detection of a small amount of truncated tensacin-C (TN-C) in the nervous system of the TN-C knockout mice created by Saga et al. (Genes Dev 6:1821-1831, 1992).
D L, Settles   +4 more
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Generation and characterization of dromedary Tenascin-C and Tenascin-W specific antibodies

Biochemical and Biophysical Research Communications, 2020
Tenascin-C (TNC) and tenascin-W (TNW), large hexameric glycoproteins overexpressed in the tumor microenvironment, are useful tumor biomarkers for theranostic applications. For now, polyclonal and monoclonal antibodies, as well as aptamers targeting TNC and TNW have been developed.
Sayda Dhaouadi   +11 more
openaire   +4 more sources

Detection of tenascin‐C in the nervous system of the tenascin‐C mutant mouse

Journal of Neuroscience Research, 1995
AbstractWe have investigated the expression of tenascin‐C (TN‐C) in the somatosensory cortex of early postnatal mutant mice in which lacZ was reported to be expressed in place of tenascin (Saga et al.: Genes Dev 6:1821‐1831, 1992). At both the mRNA and protein levels, TN‐C was detected at levels lower in the mutant than in wild type animals by in situ ...
Mitrovic N, Schachner M
openaire   +3 more sources

Tenascin in breast cancer development — is epithelial tenascin a marker for poor prognosis?

Cancer Letters, 1995
(1) In mouse mammary gland development, immunoreactive tenascin (TN) is expressed in the dense mesenchyme surrounding the epithelial component of 14-day embryos, endbuds at puberty, and tumors. (2) Cells that produce TN are myofibroblastic and are characterized by nuclear invaginations, rough endoplasmic reticulum, and pinocytotic vesicles. These cells
T, Yoshida   +4 more
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Tenascin-C in astrocytic tumors

Surgical Neurology, 2002
Abstract The authors studied the expression of tenascin-C in 52 astrocytic tumor specimens and correlated it with proliferative indices. Tenascin-C immunoreactivity was found to be greater in tumor vessels and tumor networks of high-grade astrocytic tumors, and expression of TN-C in tumor vessels correlated with proliferative indices.
Giuseppe, Viale   +3 more
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Tenascin: A hexameric adhesive glycoprotein

International Journal of Cancer, 1989
Tenascin (TN) is a large glycoprotein composed of 6 similar subunits joined together at their amino terminal by disulfide bonds. The peculiarity of its structure, properties and of its tissue distribution makes this protein extremely attractive.
P G, Natali, L, Zardi
openaire   +2 more sources

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