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xxhashdeep (v4.5)
No full textThis is md5deep, a set of cross-platform tools to compute hashes, or message digests, for any number of files while optionally recursively digging through the directory structure. It can also take a list of known hashes and display the filenames of input files whose hashes either do or do not match any of the known hashes. This version supports MD5, SHA-1, SHA-256, Tiger Whirlpool and xxHash hashes. It includes the option -R to not follow symlinks implemented by https://github.com/s-d-adamsThis release adds xxHash to hashdeep and ups some limits for faster execution
Insights into the structure and oxidation stability of Ln-doped UN spent fuel-based materials
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Specific alterations of plant species on extracellular enzyme activities and potential microbial nutrient limitation in post-fire forest soils of eastern Tibetan plateau
No full textEffect of rainfall event on water-dispersible colloids in a hyper-arid Atacama alluvial fan
No full textRadial oxygen loss of Typha latifolia outperforms microbial effects in heavy metal(loid) stabilization
No full textOff-pathway oligomers of α-synuclein and Aβ inhibit secondary nucleation of α-synuclein amyloid fibrils
No full textα-Synuclein (αSyn) is a key culprit in the pathogenesis of synucleinopathies such as Parkinson’s Disease (PD), in which it forms not only insoluble aggregates called amyloid fibrils but also smaller, likely more detrimental species termed oligomers. This property is shared with other amyloidogenic proteins such as the Alzheimer’s Disease-associated amyloid-β (Aβ). We previously found an intriguing interplay between off-pathway Aβ oligomers and Aβ fibrils, in which the oligomers interfere with fibril formation via inhibition of secondary nucleation by blocking secondary nucleation sites on the fibril surface. Here, using ThT aggregation kinetics and atomic force microscopy (AFM), we tested if the same interplay applies to αSyn fibrils. Both homotypic (i.e. αSyn) and heterotypic (i.e. Aβ) off-pathway oligomers inhibited αSyn aggregation in kinetic assays of secondary nucleation. Initially soluble, kinetically trapped Aβ oligomers co-precipitated with αSyn(1–108) fibrils. The resulting co-assemblies were imaged as clusters of curvilinear oligomers by AFM. The results indicate that off-pathway oligomers have a general tendency to bind amyloid fibril surfaces, also in the absence of sequence homology between fibril and oligomer. The interplay between off-pathway oligomers and amyloid fibrils adds another level of complexity to the homo- and hetero-assembly processes of amyloidogenic proteins
Combined Mutational and Spectroscopic Study on the Calcium-Related Kinetic Effects on the VirChR1 Photocycle
No full textThe viral rhodopsin 1 subfamily consists of microbial rhodopsins, such as VirChR1, with a light-gated cation channeling functionality, which is inhibited by calcium. For VirChR1, S14, E54, and N225 have been proposed as key residues for calcium binding. They form a highly conserved SEN-triad in channelrhodopsins near the functionally important central gate. Here, we present a time-resolved UV/vis spectroscopic study on the VirChR1 variants S14A, E54A, and N225A in a calcium-dependent manner. Comparison with the calcium-associated effects observed for the wild type shed light on the role of the respective residues for the calcium interaction. While S14A shows less pronounced, yet similar, signals, indicative of a reduced calcium affinity, E54A exhibits nearly calcium-independent photocycle kinetics, highlighting its crucial role for calcium binding. The N225A variant shows altered photocycle kinetics, in both the absence and presence of calcium, demonstrating its critical role in the formation of the functionally important central gate in VirChR1
input4MIPs.CMIP7.FZJ.FZJ-CMIP-ozone-1-2
No full textCMIP7 Forcing Datasets (input4MIPs). This dataset FZJ-CMIP-ozone-1-2 is part of input4MIPs under dataset_category: '['ozone']'. More information about the dataset can be found at the following links: https://input4mips-cvs.readthedocs.io/en/latest/dataset-overviews/ozone https://input4mips-controlled-vocabularies-cvs.readthedocs.io/en/stable/database-views/input4MIPs_source-id_CMIP7.html https://input4mips-controlled-vocabularies-cvs.readthedocs.io/en/stable/dataset-overviews/ The dataset is available at: https://esgf-node.ornl.gov/search/input4mips/?mip_era=CMIP7&activity_id=input4MIPs&institution_id=FZJ&source_id=FZJ-CMIP-ozone-1-