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Iain D. C. Fraser

Researcher at National Institutes of Health

Publications -  106
Citations -  12775

Iain D. C. Fraser is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Innate immune system & Signal transduction. The author has an hindex of 44, co-authored 100 publications receiving 11362 citations. Previous affiliations of Iain D. C. Fraser include Howard Hughes Medical Institute & California Institute of Technology.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Regulation of NMDA Receptors by an Associated Phosphatase-Kinase Signaling Complex

TL;DR: Yotiao is a scaffold protein that physically attaches PP1 and PKA to NMDA receptors to regulate channel activity and targeting of these enzymes near the substrate is proposed to enhance phosphorylation-dependent modulation.
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Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif.

TL;DR: Computer-aided analysis of secondary structure, performed on four RII-anchoring protein sequences, suggests that anchoring proteins interact with RII alpha via an amphipathic helix binding motif.
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NF-κB Signaling in Macrophages: Dynamics, Crosstalk, and Signal Integration.

TL;DR: This review of recent research on the dynamics of NF-κB signaling focuses on how these dynamics vary in different cell types, while discussing why these characteristics may be important and how new techniques and technologies should allow for appropriate control of innate immune responses.
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Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain.

TL;DR: The cloning of a cDNA which encodes a 1015-amino acid segment of Ht 31 is described and the nanomolar affinity constant and the different patterns of RII-anchoring proteins in each tissue suggest that the type II alpha PKA holoenzyme may be specifically targeted to different locations in each type of cell.