[This corrects the article DOI: 10.1371/journal.pone.0043569.].
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5861629 | PMC |
http://dx.doi.org/10.1371/annotation/ebea4bd5-2b96-4842-b110-2f7c156e5060 | DOI Listing |
Purpose: The long scan times of quantitative MRI techniques make motion artifacts more likely. For MR-Fingerprinting-like approaches, this problem can be addressed with self-navigated retrospective motion correction based on reconstructions in a singular value decomposition (SVD) subspace. However, the SVD promotes high signal intensity in all tissues, which limits the contrast between tissue types and ultimately reduces the accuracy of registration.
View Article and Find Full Text PDFIt is well known that activation of NMDA receptors can trigger long-term synaptic depression (LTD) and that a morphological correlate of this functional plasticity is spine retraction and elimination. Recent studies have led to the surprising conclusion that NMDA-induced spine shrinkage proceeds independently of ion flux and requires the initiation of protein synthesis, highlighting an unappreciated contribution of mRNA translation to non-ionotropic NMDAR signaling. Here we used NMDA-induced spine shrinkage in slices of mouse hippocampus as a readout to investigate this novel modality of synaptic transmission.
View Article and Find Full Text PDFIntrinsically disordered arginine-glycine (RG) repeat domains are enriched in multilayered biomolecular condensates such as the nucleolus. nucleolar RG repeats are dispensable for nucleolar accumulation and instead contribute to the organization of sub-nucleolar compartments. The sufficiency of RG repeats to facilitate sub-nucleolar compartmentalization is unclear.
View Article and Find Full Text PDFConnections between the mechanical properties of DNA and biological functions have been speculative due to the lack of methods to measure or predict DNA mechanics at scale. Recently, a proxy for DNA mechanics, cyclizability, was measured by loop-seq and enabled genome-scale investigation of DNA mechanics. Here, we use this dataset to build a computational model predicting bias-corrected intrinsic cyclizability, with near-perfect accuracy, solely based on DNA sequence.
View Article and Find Full Text PDFFungal highly reducing polyketide synthases (hrPKSs) are remarkable multidomain enzymes that catalyse the biosynthesis of a diverse range of structurally complex compounds. During biosynthesis, the ketosynthase (KS) and acyltransferase (AT) domains of the condensing region are visited by the acyl carrier protein (ACP) domain during every cycle, catalysing chain priming and elongation reactions. Despite their significance, our comprehension of how these steps contribute to biosynthetic fidelity remains poorly understood.
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