Differential dimerization and association among resistin family proteins with implications for functional specificity
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چکیده
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Differential association of cellular proteins with family protein-tyrosine kinases.
We have sought to identify candidate substrates for src family protein-tyrosine kinases potentially important for transformation. Transfected NIH/3T3 cells, each overexpressing a normal or activated version of the fyn, fgr, or src translational product, were examined using antibody to phosphotyrosine as a probe. Expression of each cDNA induced similar but distinct patterns of tyrosine phosphory...
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Resistin is a peptide hormone secreted by adipocytes. Cysteine residues comprise eleven of 94 (12%) amino acids in resistin. The arrangement of these cysteines is unique to resistin and its recently discovered family of tissue-specific secreted proteins, which have been independently termed resistin-like molecules (RELMs) and the FIZZ (Found in Inflammatory Zone) family. Here we show that resis...
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چکیده ندارد.
Functional Specificity among Ribosomal Proteins Regulates Gene Expression
Duplicated genes escape gene loss by conferring a dosage benefit or evolving diverged functions. The yeast Saccharomyces cerevisiae contains many duplicated genes encoding ribosomal proteins. Prior studies have suggested that these duplicated proteins are functionally redundant and affect cellular processes in proportion to their expression. In contrast, through studies of ASH1 mRNA in yeast, w...
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Saposins are small, heat-stable glycoprotein activators of lysosomal glycosphingolipid hydrolases that derive from a single precursor, prosaposin, by proteolytic cleavage. Three of these saposins (B, C, and D) share common structural features including a lack of tryptophan, a single glycosylation sequence, the presence of three conserved disulfide bonds, and a common multiamphipathic helical bu...
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ژورنال
عنوان ژورنال: Journal of Endocrinology
سال: 2002
ISSN: 0022-0795,1479-6805
DOI: 10.1677/joe.0.1750499