The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain.
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چکیده
منابع مشابه
wuthering heights and the concept of marality/a sociological study of the novel
to discuss my point, i have collected quite a number of articles, anthologies, and books about "wuthering heights" applying various ideas and theories to this fantastic story. hence, i have come to believe that gadamer and jauss are rightful when they claim that "the individaul human mind is the center and origin of all meaning," 3 that reading literature is a reader-oriented activity, that it ...
15 صفحه اولThe rapamycin-binding domain of the protein kinase mammalian target of rapamycin is a destabilizing domain.
Rapamycin is an immunosuppressive drug that binds simultaneously to the 12-kDa FK506- and rapamycin-binding protein (FKBP12, or FKBP) and the FKBP-rapamycin binding (FRB) domain of the mammalian target of rapamycin (mTOR) kinase. The resulting ternary complex has been used to conditionally perturb protein function, and one such method involves perturbation of a protein of interest through its m...
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The Forkhead box M1 (FoxM1) transcription factor is critical for expression of the genes essential for G(1)/S transition and mitotic progression. To explore the cell cycle regulation of FoxM1, we examined the phosphorylation profile of FoxM1. Here, we show that the phosphorylated status and the activity of FoxM1 increase as cells progress from S to G(2)/M phases. Moreover, dephosphorylation of ...
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پژوهش حاضر ارائه ی توصیفی است از نظام آوایی گویش لری شهر اندیمشک، واقع در شمال غربی استان خوزستان. چهارچوب نظری این پژوهش، انگاره ی پسازایشی جزءمستقل می باشد. این پایان نامه شامل موارد زیر است: -توصیف آواهای این گویش به صورت آواشناسی سنتی و در قالب مختصه های زایشی ممیز، همراه با آوانوشته ی تفصیلی؛ -توصیف نظام آوایی گویش لری و قواعد واجی آن در چهارچوب انگاره ی پسازایشی جزءمستقل و معرفی برهم کن...
A novel p53 phosphorylation site within the MDM2 ubiquitination signal: I. phosphorylation at SER269 in vivo is linked to inactivation of p53 function.
p53 is a thermodynamically unstable protein containing a conformationally flexible multiprotein docking site within the DNA-binding domain. A combinatorial peptide chip used to identify the novel kinase consensus site RXSΦ(K/D) led to the discovery of a homologous phosphorylation site in the S10 β-strand of p53 at Ser(269). Overlapping peptide libraries confirmed that Ser(269) was a phosphoacce...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 1995
ISSN: 0261-4189
DOI: 10.1002/j.1460-2075.1995.tb00212.x