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rb phosphorylation
Rb phosphorylation is mediated by cyclin-dependent kinases (CDKs), whose activity is enhanced by cyclins and inhibited by CDK inhibitors.
      
Although one mechanism for its tumor suppression may be prevention of Rb phosphorylation, thereby causing G1 arrest, many normal cell types express p16INK4A, and are still able to traverse the cell cycle.
      
The INK4a/ARF locus on chromosome 9p21 encodes two gene products that are involved in cell cycle regulation through inhibition of CDK4-mediated RB phosphorylation (p16INK4a) and binding to MDM2 leading to p53 stabilization (p14ARF).
      
Rb phosphorylation was more rapid in MCF-7 cells than in MCF10A cells, whereas Rb dephosphorylation appeared deregulated in MDA-MB-231 cells.
      
Antineoplaston caused the down-regulation of PKCα protein expression, resulting in inhibition of ERK MAPK phosphorylation, with resultant inhibition of Rb phosphorylation leading to G1 arrest.
      
The experiments supporting G1-phase-specific Rb phosphorylation and the historical development of this idea are reviewed.
      
However, etoposide treatment led to hypo-phosphorylation of Rb, while serum withdrawal did not alter the Rb phosphorylation pattern.
      
No correlation of p16 expression with clinical stage, HER2/neu immunostaining, Rb expression or Rb phosphorylation was found.
      
NAC and GEE also abolished the decease in Rb phosphorylation by ACA.
      
As Rb phosphorylation is regulated by G1 cyclin dependent kinase and CDK inhibitor p27kip1, which is an important regulator of the mammalian cell cycle, we estimated the amount of p27kip1 levels by western blotting.
      
As a final consideration, it is possible that Rb phosphorylation does not accurately reflect D kinase activity in B lymphocytes.
      
Cultures of arrested cells, via contact inhibition or DNA damage, exhibited decreased Rb phosphorylation and increased Rb acetylation.
      
Cells were collected after 24 h for flow cytometric analysis of RB phosphorylation at residue Ser807/811.
      
Cyclin D1 expression and Rb phosphorylation were assayed as the number of positive nuclei and compared to control cells not treated with estrogen.
      
Cyclin E forms a complex with cdk2 which completes RB phosphorylation.
      
CVB3 infection prevents Rb phosphorylation and activation of G1 cyclin kinases.
      
Expression of p16 in HFFs also caused a shift in Rb phosphorylation to primarily the hypophosphorylated form.
      
Experiments reveal that p53 accumulation and prevention of Rb phosphorylation must occur before the R-point in the mid G1 phase.
      
Enforced expression of cyclin D1 protein in late G1 rescues Rb phosphorylation and entry into S phase in nonadherent cells.
      
Furthermore, Cyclin D1/Cdk2 complexes catalyze Rb phosphorylation on multiple sites in vitro.
      
 

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