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Structural determinants of water permeation through aquaporin-1

TLDR
An atomic model of human red cell AQP1 is described, providing a possible molecular explanation to a longstanding puzzle in physiology—how membranes can be freely permeable to water but impermeable to protons.
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STIM1 Clusters and Activates CRAC Channels via Direct Binding of a Cytosolic Domain to Orai1

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A Virulence Locus of Pseudomonas aeruginosa Encodes a Protein Secretion Apparatus

TLDR
HSI-I likely contributes to the pathogenesis of P. aeruginosa in CF patients and is detected in pulmonary secretions of cystic fibrosis patients and Hcp1-specific antibodies in their sera, suggesting that the apparatus functions during chronic infections.
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Global Conformational Rearrangements in Integrin Extracellular Domains in Outside-In and Inside-Out Signaling

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Latent TGF-β structure and activation

TLDR
Crystals of dimeric porcine proTGF-β1 reveal a ring-shaped complex, a novel fold for the pro domain, and show how the prodomain shields the growth factor from recognition by receptors and alters its conformation.
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Multiple associated proteins regulate proteasome structure and function.

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The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis

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Molecular model for a complete clathrin lattice from electron cryomicroscopy

TLDR
Analysis of coats with distinct diameters shows an invariant pattern of contacts in the neighbourhood of each vertex, allowing assembly and uncoating to be controlled by events at a few specific sites.
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Structural Basis for dsRNA Recognition, Filament Formation, and Antiviral Signal Activation by MDA5

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Neurodegenerative disease: Amyloid pores from pathogenic mutations

TLDR
It is shown that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloids diseases.
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