scholarly journals Identification and Characterization of Human and Mouse Ovastacin

2004 ◽  
Vol 279 (25) ◽  
pp. 26627-26634 ◽  
Author(s):  
Víctor Quesada ◽  
Luis M. Sánchez ◽  
Jesús Álvarez ◽  
Carlos López-Otín
2002 ◽  
Vol 301 (2) ◽  
pp. 705-713 ◽  
Author(s):  
Fang L. Zhang ◽  
Lin Luo ◽  
Eric Gustafson ◽  
Kyle Palmer ◽  
Xudong Qiao ◽  
...  

2000 ◽  
Vol 71 (4) ◽  
pp. 581-590 ◽  
Author(s):  
James D. Eudy ◽  
Ofer Spiegelstein ◽  
Robert C. Barber ◽  
Bogdan J. Wlodarczyk ◽  
Jeffrey Talbot ◽  
...  

2002 ◽  
Vol 158 (2) ◽  
pp. 235-246 ◽  
Author(s):  
J.-C. Bourdon ◽  
J. Renzing ◽  
P.L. Robertson ◽  
K.N. Fernandes ◽  
D.P. Lane

p53 is a transcription factor that induces growth arrest or apoptosis in response to cellular stress. To identify new p53-inducible proapoptotic genes, we compared, by differential display, the expression of genes in spleen or thymus of normal and p53 nullizygote mice after γ-irradiation of whole animals. We report the identification and characterization of human and mouse Scotin homologues, a novel gene directly transactivated by p53. The Scotin protein is localized to the ER and the nuclear membrane. Scotin can induce apoptosis in a caspase-dependent manner. Inhibition of endogenous Scotin expression increases resistance to p53-dependent apoptosis induced by DNA damage, suggesting that Scotin plays a role in p53-dependent apoptosis. The discovery of Scotin brings to light a role of the ER in p53-dependent apoptosis.


Genomics ◽  
1999 ◽  
Vol 60 (3) ◽  
pp. 251-257 ◽  
Author(s):  
Monica Piccini ◽  
Francesca Vitelli ◽  
Marco Seri ◽  
Luis J.V. Galietta ◽  
Oscar Moran ◽  
...  

2002 ◽  
Vol 383 (12) ◽  
pp. 1959-1965 ◽  
Author(s):  
B. Wilhelm ◽  
C. Keppler ◽  
A. Henkeler ◽  
M. Schilli-Westermann ◽  
D. Linder ◽  
...  

AbstractA merocrine released protein (named 115k protein) was highly enriched from the secretion of the rat coagulating gland. The protein has a molecular mass of 115 kDa as calculated by SDSPAGE under reducing conditions. Furthermore, the 115 kDa protein is glycosylated, and carries Man, GlcNAc, Gal, Fuc and sialic acid residues. For identification, Nterminal amino acid and nucleotide sequence analyses were performed. The sequences obtained showed 86 to 100% identity with human and mouse IgGFc binding proteins. The functional capacity of IgG binding of the 115 kDa protein was shown by overlay experiments, indicating its membership in the IgG binding protein family.


Author(s):  
Thomas A. Owen ◽  
Steven L. Smock ◽  
S. Prakash ◽  
L. Pinder ◽  
D. Brees ◽  
...  

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