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1.
Angew Chem Int Ed Engl ; 59(46): 20666-20671, 2020 Nov 09.
Article in English | MEDLINE | ID: mdl-32790246

ABSTRACT

Herein we present a new viologen-based radical-containing metal-organic framework (RMOF) Gd-IHEP-7, which upon heating in air undergoes a single-crystal-to-single-crystal transformation to generate Gd-IHEP-8. Both RMOFs exhibit excellent air and water stability as a result of favorable radical-radical interactions, and their long-lifetime radicals result in wide spectral absorption in the range 200-2500 nm. Gd-IHEP-7 and Gd-IHEP-8 show excellent activity toward solar-driven nitrogen fixation, with ammonia production rates of 128 and 220 µmol h-1 g-1 , respectively. Experiments and theoretical calculations indicate that both RMOFs have similar nitrogen fixation pathways. The enhanced catalytic efficiency of Gd-IHEP-8 versus Gd-IHEP-7 is attributed to intermediates stabilized by enhanced hydrogen bonding.

2.
EMBO J ; 32(10): 1365-80, 2013 May 15.
Article in English | MEDLINE | ID: mdl-23511975

ABSTRACT

Direct phosphorylation of GluA1 by PKC controls α-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA) receptor (AMPAR) incorporation into active synapses during long-term potentiation (LTP). Numerous signalling molecules that involved in AMPAR incorporation have been identified, but the specific PKC isoform(s) participating in GluA1 phosphorylation and the molecule triggering PKC activation remain largely unknown. Here, we report that the atypical isoform of PKC, PKCλ, is a critical molecule that acts downstream of phosphatidylinositol 3-kinase (PI3K) and is essential for LTP expression. PKCλ activation is required for both GluA1 phosphorylation and increased surface expression of AMPARs during LTP. Moreover, p62 interacts with both PKCλ and GluA1 during LTP and may serve as a scaffolding protein to place PKCλ in close proximity to facilitate GluA1 phosphorylation by PKCλ. Thus, we conclude that PKCλ is the critical signalling molecule responsible for GluA1-containing AMPAR phosphorylation and synaptic incorporation at activated synapses during LTP expression.


Subject(s)
Isoenzymes/metabolism , Long-Term Potentiation/physiology , Protein Kinase C/metabolism , Animals , Gene Knockdown Techniques , Glutamic Acid/metabolism , Heat-Shock Proteins/genetics , Heat-Shock Proteins/metabolism , Hippocampus/metabolism , In Vitro Techniques , Isoenzymes/genetics , Male , Phosphatidylinositol 3-Kinases/metabolism , Phosphorylation , Protein Kinase C/genetics , Rats , Rats, Sprague-Dawley , Receptors, AMPA/metabolism , Sequestosome-1 Protein , Signal Transduction , Synapses/metabolism
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