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    Biochemistry

    [ASAP] Mo-, V-, and Fe-Nitrogenases Use a Universal Eight-Electron Reductive-Elimination Mechanism To Achieve N2 Reduction

    Biochemistry
    DOI: 10.1021/acs.biochem.9b00468

    …read more

    Source:: <a href=http://feedproxy.google.com/~r/acs/bichaw/~3/JYXkI1OJnn8/acs.biochem.9b00468 target="_blank" title="[ASAP] Mo-, V-, and Fe-Nitrogenases Use a Universal Eight-Electron Reductive-Elimination Mechanism To Achieve N2 Reduction” rel=nofollow>ACS Biochemistry

          

    [ASAP] Three-Dimensional Protein Structure Determination Using Pseudocontact Shifts of Backbone Amide Protons Generated by Double-Histidine Co2+-Binding Motifs at Multiple Sites

    Biochemistry
    DOI: 10.1021/acs.biochem.9b00404

    …read more

    Source:: <a href=http://feedproxy.google.com/~r/acs/bichaw/~3/Tx1gGC67FbU/acs.biochem.9b00404 target="_blank" title="[ASAP] Three-Dimensional Protein Structure Determination Using Pseudocontact Shifts of Backbone Amide Protons Generated by Double-Histidine Co2+-Binding Motifs at Multiple Sites” rel=nofollow>ACS Biochemistry

          

    Pharmacological targeting of the unfolded protein response for disease intervention

    Nature Chemical Biology, Published online: 18 July 2019; doi:10.1038/s41589-019-0326-2

    Hetz et al. discuss recent advances in the identification and optimization of small molecules targeting the unfolded protein response and the application of these small molecules in cancers, neurodegeneration and metabolic diseases. …read more

    Source:: Nature Biochemistry

          

    Specificity for latent C termini links the E3 ubiquitin ligase CHIP to caspases

    Nature Chemical Biology, Published online: 18 July 2019; doi:10.1038/s41589-019-0322-6

    The C termini sequences recognized by E3 ubiquitin ligase CHIP were identified via a peptide library screen. Caspase cleavage caused the exposure of aspartic acid at the C termini of Tau and caspase-6 that made them accessible to CHIP. …read more

    Source:: Nature Biochemistry

          

    A programmable DNA-origami platform for studying lipid transfer between bilayers

    Nature Chemical Biology, Published online: 18 July 2019; doi:10.1038/s41589-019-0325-3

    Use of DNA-origami nanostructures to study lipid transfer between closely apposed membrane bilayers supports a model where phospholipids are transferred by extended synaptotagmin 1 between the endoplasmic reticulum and plasma membrane through a shuttle mechanism. …read more

    Source:: Nature Biochemistry

          

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