M
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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Journal ArticleDOI
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.
Michael B. Yaffe,Katrin Rittinger,Stefano Volinia,Paul R. Caron,Alastair Aitken,Henrik Leffers,Steven J. Gamblin,Stephen J. Smerdon,Lewis C. Cantley,Lewis C. Cantley +9 more
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
Manuel Stucki,Julie A. Clapperton,Duaa H. Mohammad,Michael B. Yaffe,Stephen J. Smerdon,Stephen P. Jackson +5 more
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.
Michael S.Y. Huen,Robert A. Grant,Isaac A. Manke,Kay Minn,Xiaochun Yu,Michael B. Yaffe,Junjie Chen +6 more
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
Peggy P. Hsu,Seong A. Kang,Jonathan Rameseder,Yi Zhang,Kathleen Ottina,Kathleen Ottina,Daniel Lim,Timothy R. Peterson,Yongmun Choi,Nathanael S. Gray,Michael B. Yaffe,Jarrod A. Marto,David M. Sabatini +12 more
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.