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Bernhard M. Mayr
Researcher at Salk Institute for Biological Studies
Publications - 5
Citations - 3007
Bernhard M. Mayr is an academic researcher from Salk Institute for Biological Studies. The author has contributed to research in topics: CREB & ATF/CREB. The author has an hindex of 5, co-authored 5 publications receiving 2846 citations.
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Journal ArticleDOI
Transcriptional regulation by the phosphorylation-dependent factor CREB
Bernhard M. Mayr,Marc Montminy +1 more
TL;DR: The transcription factor CREB functions in glucose homeostasis, growth-factor-dependent cell survival, and has been implicated in learning and memory, and how is specificity achieved in these signalling pathways?
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Distinct effects of cAMP and mitogenic signals on CREB-binding protein recruitment impart specificity to target gene activation via CREB
TL;DR: The studies indicate that the relative effects of cAMP and mitogen/stress signals on CREB⋅CBP complex formation impart selectivity to gene activation through CREB phosphorylated at Ser-133.
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Identification of small-molecule antagonists that inhibit an activator: coactivator interaction.
Jennifer L. Best,Carlos A. Amezcua,Bernhard M. Mayr,Lawrence Flechner,Christopher M. Murawsky,Beverly M. Emerson,Tsaffrir Zor,Kevin H. Gardner,Marc Montminy +8 more
TL;DR: The ability of small molecules to interfere with second-messenger signaling cascades by inhibiting specific protein-protein interactions in the nucleus is demonstrated by identifying several compounds that bind to different surfaces on KIX.
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Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators.
TL;DR: NMR and biochemical analyses are used to study the interactions of KIX with the trans activation domain from the constitutive activator c-Myb and with the kinase-inducible transactivation domain (KID) from CREB to obtain insights into the mechanism by which the KIX domain of CBP can recognize the transactivation domains of many different transcription factors.
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Glutamine rich and basic region/leucine zipper (bZIP) domains stabilize cAMP-response element-binding protein (CREB) binding to chromatin.
TL;DR: A novel mechanism by which the family of glutamine-rich activators promotes cellular gene expression is suggested by examining the dynamics of cAMP-response element-binding protein (CREB) binding to chromatin in live cells using fluorescence recovery after photobleaching (FRAP).