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The S-100: A protein family in search of a function

Progress in Neurobiology, 1995
The S-100 is a group of low molecular weight (10-12 kD) calcium-binding proteins highly conserved among vertebrates. It is present in different tissues as dimers of homologous or different subunits (alpha, beta). In the nervous system, the S-100 exists as a mixture composed of beta beta and alpha beta dimers with the monomer beta represented more often.
FANO' ILLIC', Giorgio   +5 more
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Der Tumormarker S 100

Zentralblatt für Arbeitsmedizin, Arbeitsschutz und Ergonomie, 2017
Die vorliegende Ubersicht zum Tumormarker S‑100 wird im Rahmen der Serie „Tumormarker“ des Zentralblatts fur Arbeitsmedizin, Arbeitsschutz und Ergonomie publiziert, die sich mit dem immer haufigeren Gebrauch der Bestimmung von spezifischen Markern bei sog. Manager-Vorsorgen und Check-up-Untersuchungen beschaftigt.
K. Passek   +5 more
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The Heterogeneity of the S-100 Protein Fraction

1972
It is commonly accepted that the neurospecific protein S-100 is a single molecular species, on the basis of immunological data, and on the basis of its behaviour in several Chromatographic and electrophoretic systems (10) and during analytical ultracentrifugation (15).
G, Vincendon, J P, Zanetta, G, Gombos
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Binding of Chlorpromazine to S‐100 Protein

Journal of Neurochemistry, 1984
Abstract: Chlorpromazine (CPZ) induces in S‐100 conformational changes resulting in the exposure of titratable SH groups of the protein to the solvent. This effect is even greater in the presence of Mg2+± Ca2+. S‐100 possesses binding sites for CPZ. The binding of CPZ to 3 μM S‐100 is half‐saturated by 0.18 μM CPZ in the presence of Mg2+ plus Ca2+ and
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Protein S-100

1995
Protein S-100 is an acidic calcium-binding protein of molecular weight 21 000 Da found throughout the nervous system of all vertebrates. It has a dimeric structure with α- and β-subunits. S-100ββ is found in glial cells and Schwann cells, whilst S-100αβ is restricted to glial cells.
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Immunohistochemical localisation of S–100 protein in brain

Nature, 1975
IT is accepted that the brain-specific protein S–100 is associated predominantly with glial cells1–5. More equivocal evidence exists to suggest a possible relationship of S–100 to neurones3,6,7. Although well characterised antisera against S–100 have long been available8, few immunohistochemical studies of the location of S–100 antigen in brain have ...
A, Matus, S, Mughal
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S-100 Protein immunoreactivity in bovine testis

Andrologia, 2009
The present study deals with immunohistochemical localization of S-100 protein in the bovine testis. Immunoreactivity for the protein was seen in Sertoli cells of the seminiferous tubules and as a particularly intense staining in the terminal tubular segment (transitional region, middle portion, and terminal plug), which is mainly composed of modified ...
W, Amselgruber   +3 more
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IMMUNOCHEMICAL PROPERTIES OF S‐100 PROTEINS AND THEIR SUBUNITS

Journal of Neurochemistry, 1979
Abstract— The immunological activities of two populations of bovine S‐100 proteins with anti‐S‐100 serum were studied by complement fixation and rocket immunoelectrophoresis. The reactivities of subunits of these two populations were studied by crossed immunoelectrophoresis and rocket immunoelectrophoresis. Although the two populations conformed in all
S P, Mahadik   +3 more
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Chemistry and Biology of the S‐100 Protein

Scandinavian Journal of Immunology, 1982
The S-100 protein is specific for the nervous system and, being present in all vertebrates, shows a high degree of stability of structure during evolution. In adult animals it is primarily localized to glial elements, although there is some evidence that a small proportion may be present in neuronal nuclei or their plasma membranes.
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S-100 protein in carcinoid tumours of appendix

Acta Neuropathologica, 1985
A series of 12 carcinoid tumours of the appendix were examined with regard to S-100 protein immunoreactivity. All tumours were both argentaffin and argyrophil, and displayed immunoreactivity after application of a monoclonal antibody against serotonin.
E, Wilander, M, Lundqvist, T, Movin
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