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Michael B. Yaffe

Researcher at Massachusetts Institute of Technology

Publications -  405
Citations -  45104

Michael B. Yaffe is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Phosphorylation & DNA damage. The author has an hindex of 102, co-authored 379 publications receiving 41663 citations. Previous affiliations of Michael B. Yaffe include Beth Israel Deaconess Hospital & Women's College, Kolkata.

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Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs

TL;DR: Scansite identifies short protein sequence motifs that are recognized by modular signaling domains, phosphorylated by protein Ser/Thr- or Tyr-kinases or mediate specific interactions with protein or phospholipid ligands, allowing segments of biological pathways to be constructed in silico.
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The structural basis for 14-3-3:phosphopeptide binding specificity.

TL;DR: It is shown that the 14-3-3 dimer binds tightly to single molecules containing tandem repeats of phosphoserine motifs, implicating bidentate association as a signaling mechanism with molecules such as Raf, BAD, and Cbl.
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MDC1 Directly Binds Phosphorylated Histone H2AX to Regulate Cellular Responses to DNA Double-Strand Breaks

TL;DR: It is shown that MDC1/NFBD1-gammaH2AX complex formation regulates H2AX phosphorylation and is required for normal radioresistance and efficient accumulation of DNA-damage-response proteins on damaged chromatin.
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RNF8 Transduces the DNA-Damage Signal via Histone Ubiquitylation and Checkpoint Protein Assembly.

TL;DR: This study implicates RNF8 as a novel DNA-damage-responsive protein that integrates protein phosphorylation and ubiquitylation signaling and plays a critical role in the cellular response to genotoxic stress.
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The mTOR-Regulated Phosphoproteome Reveals a Mechanism of mTORC1-Mediated Inhibition of Growth Factor Signaling

TL;DR: It is found that the phosphorylation response to insulin is largely mTOR dependent and that mTOR exhibits a unique preference for proline, hydrophobic, and aromatic residues at the +1 position.