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S-100 proteins

Cell Calcium, 1986
S-100 is a group of closely related, small, acidic Ca2+-binding proteins (S-100a0, S-100a and S-100b, which are alpha alpha, alpha beta, and beta beta in composition, respectively). S-100 is structurally related to calmodulin and other Ca2+-binding proteins.
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The effect of antiserum to S 100 protein on behavior and amount of S 100 in brain cells

Journal of Neurobiology, 1981
AbstractSince antiserum raised against the S 100 protein has an impairing effect on acquisition in behavioral tests, when interacting with S 100 on hippocampal cells, the effect of S 100 antiserum was studied in rats on the S 100 content of the hippocampus and thalamus, as well as on behavior.
H, Hydén, P W, Lange
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Heterogeneity of S-100 protein: Comparison of bovine and guinea-pig S-100 proteins

International Journal of Biochemistry, 1981
Abstract 1. 1. Two populations of S-100 proteins (I & II) were obtained from bovine and guinea-pig brains after DEAE-cellulose chromatography. 2. 2. While S-100 I was predominant in bovine (70%), S-100 II was present in major amounts in guinea-pig (92%) brain. Both S-100 populations were active against anti-S-100 serum. 3. 3.
A S, Perumal, V K, Murthi
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S-100 Proteins

2015
AKT Protein kinase B BCL2 B-cell lymphoma 2 CCL2 Chemokine CC ligand 2 CREB Camp response element-binding protein DLC1 Deleted in liver cancer 1 EGF Epithelial growth factor EMT Epithelial mesenchymal transduction ERK Extracellular regulated kinases ESCC Esophageal squamous cell carcinoma FGF-1 Fibroblast growth factor 1 IDC Invasive ductal carcinaoma ...
Mohamad Elbaz   +3 more
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NUCLEAR LOCALIZATION OF S‐100 PROTEIN

Journal of Neurochemistry, 1974
Abstract— S‐100 protein has been found in the nuclei isolated from the brain cortex of rabbit. The nuclear S‐100 constitutes a small portion (0.55 per cent) of the S‐100 present in the cytosol. Most of the large and pale nuclei appear to contain much more S‐100 than the small and dark ones.
F, Michetti   +4 more
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S‐100 PROTEIN IN MALIGNANT MESOTHELIOMAS

Acta Pathologica Microbiologica Scandinavica Series A :Pathology, 1985
Recently, the presence of S‐100 protein has been described in a few tissues that are not of neuro‐ectodermal origin. Here we report the presence of S‐100 protein in epithelial and biphasic malignant mesotheliomas and one of seven reactively proliferating mesothelial lesions. Sarcomatous malignant mesotheliomas, six of seven reactive mesothelial lesions
O O, Rasmussen, K E, Larsen
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S-100 protein in human chondrocytes

Nature, 1982
Chondrocytes in the fetal skull and visceral cartilage are considered to be of neural crest origin1 while those found elsewhere in the body are thought to be derived from mesoderm2,3 (mesodermal chondrocytes). Chondrocytes of pelvic rudiments from chick embryos are the only cells known to respond to nerve growth factor that are not of neuroectodermal ...
K, Stefansson   +3 more
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S-100 protein in adipose tissue

International Journal of Biochemistry, 1983
1. The nervous system-specific S-100 protein is present at high levels in adipose tissues of various animal species. 2. The adipose S-100 protein levels in beef and rat were 1.13 and 1.59 micrograms/mg protein, respectively, which were comparable to the brain levels (beef, 4.85 micrograms/mg; rat, 1.98 micrograms/mg). 3.
K, Kato, F, Suzuki, T, Nakajima
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S-100 protein and myoepithelial neoplasms

The Journal of Laryngology & Otology, 1986
AbstractBesides advancing our knowledge of histogenesis, immuno-cytochemical studies of salivery gland tumors have added an important objective component to the diagnosis and classification of the tumors. Cellular localization of S-100 protein now allows identification of myoepithelial cells and tumors composed of these cells. The four tumors presented
J G, Batsakis   +4 more
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S-100 protein in the testis

Cell and Tissue Research, 1985
S-100, a protein originally believed to be unique to the nervous system, has recently been found in extraneural presence of S-100 in the testis, namely in Leydig cells and in lymphatic endothelial cells, using immunohistochemical and immunochemical methods. We show that the protein in the testis is immunologically identical to brain S-100.
Michetti F   +5 more
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