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gprotein
Recently, the small Gprotein Rho has attracted much attention.
      
Gprotein-coupled receptors (GPCRs) represent one of the most important categories of membrane proteins that play important roles in signaling pathways.
      
Cometabolism with methyl tert-butyl ether, (MTBE), gave maximum degradation rates of 49, 12, 32 and 0?mg?gprotein-1?h-1, respectively.
      
Biomass yieldin relation to light energy was determined as gprotein per mol of photons (400-700 nm).
      
Antecedent ethanolincreased FAT 18 hr after SO from 0.105 0.048 μg/gprotein to 0.258 ± 0.054 and AP lasting 18 hrfrom 0.331 ± 0.072 to 0.695 ± 0.110.
      
Although present in different tissues, Pins and Pinsrelated proteins may mediate their functions by regulating Gprotein activity.
      
BX 471 demonstrated a greater than 10,000 fold selectivity for CCR1 compared with 28 Gprotein coupled receptors.
      
Cdc42 is a Gprotein that is only active in the GTP-bound form.
      
Different Gprotein subunit genes apparently take over the function of suppressing conidiation in different species.
      
Differences in Gprotein activation by mu and delta opioid, and cannabinoid, receptors in rat striatum.
      
Endothelins exert their physiological effects via two specific Gprotein coupled receptors termed ETA and ETB.
      
Evidence against Gprotein involvement in the effect of nociceptin on T-currents.
      
It is not uncommon that the physiological roles of Gprotein coupled receptors differ between rodents and humans.
      
It allows the adaptor and small Gprotein-dependent steps involved in GLUT4 vesicle formation and regulation to be studied in a cell-free system.
      
Interestingly, they are not closer to the adenosine receptor than to other Gprotein-coupled receptors.
      
Information on the Gprotein interactions with these four major inhibitory sites is limited.
      
In all cases, blots were reprobed with cDNA specific for a different Gprotein mRNA to eliminate any variation due to electrophoresis or blotting.
      
In the present study, we investigated the Gprotein pharmacology associated with mGluR8 activity.
      
Little is known about the transcriptional control of Gprotein a-subunit genes or the mechanisms that regulate the turnover of their transcripts.
      
Muscarinic agonists modulate Nand L-type Ca2 channels in these neurons through two distinct Gprotein-mediated mechanisms.
      
 

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