Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.581057
In vitro pull down assays indicated that the interaction of ERalpha with MPG was direct and occurred through the DNA and ligand binding domains and the hinge region of the receptor . 0.581057^^^
Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
The interaction of human alpha 1 acid glycoprotein ( AAG ) with a corticosteroid was studied using nitroxide labeled deoxycorticosterone and electron spin resonance ( ESR ) spectroscopy . ^^^ The ESR spectra of the spin labeled steroid in the presence of AAG could be used to characterize the ligand protein interaction at equilibrium without the need of a separation between bound and free species . ^^^ The ESR spectra width could be used to define a polar character for the spin label environment in the steroid binding site of AAG and to calculate an apparent rotational correlation time of 2 . 8 10 10 ( 8 ) sec for the steroid protein complex in aqueous solution at 20 degrees C . ^^^
Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
Despite extensive searching in exons 1 through 8 , we found no deletions / insertions and only two missense mutations in codons 69 [ AAC ( Asn ) > AAG ( Lys ) ] and 396 [ ATG ( Met ) > GTG ( Val ) ] of the same ER negative tumor . ^^^
Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
Endoplasmic reticulum ( ER ) stress in the budding yeast Saccharomyces cerevisiae triggers Ca2+ influx through a plasma membrane channel composed of Cch 1 and Mid 1 . ^^^
Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
The yeast Mid 1 protein with an apparent molecular mass of 100 kDa is required for Ca2+ influx stimulated by the mating pheromone and by a capacitative calcium entrylike mechanism acting in response to Ca2+ depletion from the endoplasmic reticulum ( ER ) and functions as a stretch activated Ca2+ permeable channel when expressed in mammalian cells . ^^^ In this study , we examined a possible intracellular localization of this protein by indirect fluorescence microscopy and found that Mid 1 is present in the ER membrane as well as the plasma membrane . ^^^ Intracellular fluorescence images for Mid 1 were the same as those for the ER marker protein Sec 71 but quite different from those of the Golgi protein Ypt 1 . ^^^ The protein level and modification of Mid 1 in the plasma membrane and the ER membrane were unchanged by the mating pheromone . ^^^
Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
The truncated protein containing the region from H 1 to H 3 ( Mid 1 ( 1 360 ) GFP ) localized normally in the plasma and endoplasmic reticulum ( ER ) membranes and complemented the low viability and Ca ( 2+ ) uptake activity of the mid 1 mutant , whereas Mid 1 ( 1 133 ) GFP containing the region from H 1 to H 2 did not . ^^^ The region from H 1 to H 3 is required for the localization of Mid 1 in the plasma and ER membranes . ^^^
Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
An ESR study was first performed to validate in vitro the specific antioxidant properties of carnosine and MPG . ^^^
Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
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Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
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Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
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Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
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Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
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Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
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Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
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Interacting proteins: P29372 and P03372 Pubmed SVM Score :0.0
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