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gi protein
However, if the pathways are the same for deformation and SO2-dependent release of ATP then Gi protein seems a likely link in the chain of events.
      
Increased inhibitory Gi protein levels would be expected to enhance vasoconstrictor action as a result of suppressed cAMP production.
      
Inverse agonist may induce or stabilize a CB2/Gi protein complex that remains inactive.
      
In HEK293 and HeLa cells Mel1c receptors may be coupled functionally via several distinct Gi protein subtypes.
      
Like MCP-1-mediated migration, repulsion is Bordetella pertussis toxin sensitive, indicating the involvement of Gi protein-coupled receptors.
      
Other studies have demonstrated cell-specific effects of Gi protein deletion.
      
Our finding of PTK-Lyn activation with burn could be interpreted to result from either a Gi protein-independent or Gilinked signal pathway.
      
PT ADP ribosylates the G subunit of Gi protein and thus inactivates it.
      
Pertussis toxin pretreatment failed to increase cAMP in PC hearts, excluding a role for Gi protein.
      
Recent studies by Kirsch et a17 have indicated that KATP can be opened by A,-activation via a Gi protein coupled mechanism.
      
Stimulation of Gs and inhibition of Gi protein functions by minimally oxidized LDL.
      
This suggests that a pertussis toxin-sensitive Gi protein-dependent mechanism might be involved.
      
This effect involves the interaction of SRIF-specific, Gi protein-linked receptors with adenylyl cyclase.
      
This result indicates that a Gi protein is implicated in the antimitogenic pathway activated by the somatostatin analogue.
      
Thus, the cCCR1 is functionally expressed as a Gi protein-coupled receptor in the HEK293 cell line.
      
This is in agreement with our observations of the Gi protein being up-regulated by the inverse agonist.
      
Thus the cytoplasmic domain of NPR-C can directly activate the Gi protein and inhibit adenylyl cyclase.
      
Thus, the link between cAMP levels and ATP release is similar, but differences depending on Gi protein activation or subtypes may exist.
      
The Gi protein composition of Ltk cells may be more limited than that of HEK293 and HeLa cells.
      
These results demonstrate that 2-ARs in transgenic adipocytes are coupled to Gi protein.
      
 

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