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pro vyhledávání: '"339"'
Publikováno v:
The Journal of biological chemistry. 266(12)
We have identified, in nuclear extracts of NIH-3T3 fibroblasts, a factor which binds a sequence between -339 and -361 in the mouse alpha 1(I) collagen promoter. A 3-base pair substitution mutation introduced in this promoter element, which abolishes
Autor:
Anne-Françoise Burnol, Armelle Leturque, Nadim Kassis, Maria J. Muñoz-Alonso, Jean Girard, Ghislaine Guillemain
Publikováno v:
The Journal of biological chemistry. 275(42)
A novel protein was cloned from a rat liver cDNA library by interaction with the liver glucokinase. This protein contained 339 residues and possessed a canonical consensus sequence for a dual specificity phosphatase. The recombinant protein was able
Autor:
Jacques U. Baenziger, Jeremy J. Keusch, Stephen M. Manzella, Kwame Nyame, Richard D. Cummings
Publikováno v:
The Journal of biological chemistry. 275(33)
The large array of different glycolipids described in mammalian tissues is a reflection, in part, of diverse glycosyltransferase expression. Herein, we describe the cloning of a UDP-galactose: beta-d-galactosyl-1,4-glucosylceramide alpha-1, 3-galacto
Publikováno v:
The Journal of biological chemistry. 266(16)
An RNA helicase, isolated from nuclear extracts of HeLa cells, displaced duplex RNA in the presence of any one of the eight common nucleoside triphosphates. The unwinding reaction was supported most efficiently by ATP and GTP and poorly by dCTP and d
Two nicking enzyme systems specific for mismatch-containing DNA in nuclear extracts from human cells
Publikováno v:
The Journal of biological chemistry. 266(10)
We have identified two novel enzyme systems in human HeLa nuclear extracts that can nick at specific sites of DNA molecules with base mismatches, in addition to the T/G mismatch-specific nicking enzyme system (Wiebauer, K., and Jiricny, J. (1989) Nat
Autor:
D L, Sackett, J, Wolff
Publikováno v:
The Journal of biological chemistry. 261(19)
The alpha and beta subunits of tubulin each have a single highly reactive site for a variety of proteases that divides each subunit into two unequal regions. The position of cleavage is not the same for alpha and beta, since alpha is consistently cle