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861 results for “Collagen”
Dataset for: "Dynamical properties of solid and hydrated collagen: Insight from nuclear magnetic resonance relaxometry"
<p>The dataset contains a full set of 1H magnetization curves (1H magnetization versus time) for solid and hydrated collagen and collagen-based artificial tissues.</p> <p>DOI of article: <a href="https://doi.org/10.1063/5.0191409" target="_blank" rel="noopener">https://doi.org/10.1063/5.0191409</a></p> <p>This research was funded by the National Science Centre, Poland, Grant No. 2021/43/B/NZ5/01602.</p>
Supplementary Data to "Disparate regulation of Smad3 phosphorylation and collagen gene transcription by full-length IL-33"
<p>These are Supplementary Figures for the article "Disparate regulation of Smad3 phosphorylation and collagen transcription by full-length IL-33"</p>
MALDI-TOF-MS reference spectra and sequence data for domesticated equids (horse and donkey) collagen for Zooarchaeology by Mass Spectrometry (ZooMS)
<p>MALDI-TOF-MS spectra of extracted collagen from modern reference and archaeological bone samples to develop markers for Zooarchaeology by Mass Spectrometry (ZooMS) to distinguish between Equus species. For each sample digestions were done in both trypsin and chymotrypsin separately. Information about the species of the samples can be found in 'sample metadata.csv' file. Information on the extraction and digestion protocol can be found in the associated manuscript. The sequence data contains alignments of the proteins COL1A1 and COL1A2 for available Equus collagen protein sequences. More information on these files can be found in the corresponding manuscript to this dataset.<br> </p>
Data from: Preserved collagen reveals species identity in archaeological marine turtle bones from Caribbean and Florida sites
Advancements in molecular science are continually improving our understanding of marine turtle biology and evolution. However, there are still considerable gaps in our understanding, such as past marine turtle distributions, which can benefit from advanced zooarchaeological analyses. Here we apply collagen fingerprinting to 130 archaeological marine turtle bone samples up to 2500 years old from the Caribbean and Florida's Gulf Coast for faunal identification, finding the vast majority of samples (88%) to contain preserved collagen despite deposition in the tropics. All samples can be identified to species-level with the exception of the Kemp's ridley (Lepidochelys kempii) and olive ridley (L. olivacea) turtles, which can be separated to genus level, having diverged from one another only ~5 million years ago. Additionally, we identify a single homologous peptide that allows the separation of archaeological green turtle samples, Chelonia spp., into two distinct groups, which potentially signifies a difference in genetic stock. The majority of the archaeological samples are identified as green turtle (Chelonia spp.; 63%), with hawksbill (Eretmochelys imbricata; 17%) and ridley turtles (Lepidochelys spp.; 3%) making up smaller proportions of the assemblage. There were no molecular identifications of the loggerhead turtle (Caretta caretta) in the assemblage despite 9% of the samples being morphologically identified as such, highlighting the difficulties in relying on morphological identifications alone in archaeological remains. Finally, we present the first marine turtle molecular phylogeny using collagen (I) amino acid sequences and find our analyses match recent phylogenies based on nuclear and mitochondrial DNA. Our results highlight the advantage of using collagen fingerprinting to supplement morphological analyses of turtle bones and support the usefulness of this technique for assessing their past distributions across the Caribbean and Florida's Gulf Coast, especially in these tropical environments where DNA preservation may be poor.
Micro-CT image of cell-populated collagen scaffold in the aqueous environment (contrasted with PTA)
<p>A dataset of the collagen scaffold populated with the 3T3 cells scanned in the aqueous environment using Bruker Skyscan 1276 machine (Bruker, Belgium). </p><p><strong>Scaffold production</strong></p><p>The processes of obtaining and working with collagen scaffolds were conducted in an isolated environment under sterile conditions. The collagen sponge matrix was manufactured at the Center for Collagen Innovation within the Institute of Regenerative Medicine at Sechenov University and provided to us for experimental purposes. In order to obtain the collagen, the authors utilized animal-derived materials sourced from the tendons of large horned cattle. To do this, the tendons were cleaned of excess tissues, cut into pieces with a thickness of 0.5-1 cm, and sequentially treated for 12 hours in a 0.5 M NaCl solution. Subsequently, the mass was homogenized in a 0.83 M acetic acid solution. The resulting suspension was hydrolyzed with 0.24% pepsin for 2 days, after which 1 M NaOH was added to adjust the pH to 7.5, halting the hydrolysis process. The suspension was precipitated with a 12% NaCl solution, the resulting precipitate was redissolved in 0.02 M acetic acid, and then dialyzed. To obtain collagen porous matrices (sponges), the obtained solution was neutralized using 0.1 M NaOH until a pH of 7-7.5 was reached, and the resulting suspension was lyophilized at -40°C for 2 days.</p><p>Subsequently, the collagen matrix was cut into cubes with sides measuring 0.5 cm. These cubes were placed in 15 ml test tubes filled with 70% ethyl alcohol for sterilization. The test tubes were then placed on a shaker and left in the refrigerator at +4°C for 24 hours. Afterward, the collagen matrices were removed from the alcohol and rinsed five times with 0.9% NaCl.</p><p>Following the alcohol rinse to confirm the absence of toxicity, an elution test, adapted following the ISO 10993 protocol, was conducted. To obtain collagen cube extracts, they were incubated in a cell culture medium at a volume of 1 ml per sample for 24 hours at 37°C. The 3T3 cell culture was passaged, with 5000 cells seeded in each well of a 96-well plate. After 24 hours, the cells were treated with extract at a volume of 200 µl per well and left in the incubator at 37°C for 24 hours. The following day, extracts were collected, and AlamarBlue reagent (Invitrogen, Waltham, MA, USA) was added according to the manufacturer's instructions to assess the metabolic activity of the cells. Serial dilutions of sodium dodecyl sulfate (SDS) were used as the positive control. Fluorescence intensity was measured using a Victor Nivo spectrofluorimeter (PerkinElmer, Waltham, Massachusetts, USA) at an excitation wavelength of 530 nm and an emission wavelength of 590 nm.</p><p><strong>Cell seeding</strong></p><p>After confirming the absence of cytotoxic effects, collagen sponges were seeded with the NIH 3T3 cell line at a density of 50,000 cells per sample (cubes of collagen sponge measuring 0.5 cm per side). </p><p><strong>Staining technique</strong></p><p>Fixed specimens in 10% formalin with PBS were washed after 24 hours with distilled water and after that placed in 3% phosphotungstic acid dissolved in distilled water for 24 hours and kept on the rotary shaker at room temperature. After staining, samples were washed and stored in distilled water at 5 °C. </p><p><strong>Image acquisition and reconstruction</strong></p><p>A plastic tube filled with distilled water containing the contrasted sample was placed on the sample holder in a SkyScan 1276 micro-CT (Bruker, Kontich, Belgium) and were scanned at 3 μm voxel resolution with 70 kV voltage and 200 uA source power and an aluminum filter with 1 mm of thickness. The rotation was set to 360° around the vertical axis of the sample, with two middle frames for each 0.2° angle step.</p><p>After scanning, the data were reconstructed using Bruker's NRecon software. During reconstruction, the ring artifact reduction value was set to 20% and the beam hardening correction value to 30%. After that, samples were exported as a series of 16-bit TIFF images which could be opened in the specialized software. </p>
MALDI-TOF spectra of archaeological (Oncorhynchus) and modern (Salmo salar) bone collagen
<p>SPECIES INFORMATION<br> csv containing information about the samples that links the information about the species and files</p> <p><br> MALDI TOF-MS</p> <p>MALDI Spectra from a Bruker Ultraflex II range m/z 800-3500<br> Three technical replicates were averaged in mMass<br> Each of these spectra a tab delimited .txt file are uploaded</p> <p><br> SEQUENCE DATA<br> An aligned FASTA file containing the bovine reference collagen sequence and both versions of S. salar and O. mykiss sequences. The sequences are concatenated with COL1A1, COL1A2, and COL1A3 for the two fish and COL1A1, COL1A2, COL1A1 for bovine.</p> <p>Three annotated gff files containing the sequence from version 1 of S. salar annotated with the locations of the published mammal markers and the biomarkers presented in this paper. Each gff file corresponds to one of the three collagen proteins COL1A1, COL1A2, and COL1A3.</p>
2D and 3D Segmentation of uncertain local collagen fiber orientations in SHG microscopy
<p><strong>General</strong></p> <p>This dataset consists out of multiple Second Harmonic Generation (SHG) microscopy scans of collagen fibers in mice bones. Some mices are diseased with osteogenesis imperfecta (brittle bone).</p> <p>We used this data to investigate the segmentation of uncertain local collagen fiber orientations. The corresponding paper "2D and 3D Segmentation of uncertain local collagen fiber orientations in SHG microscopy" is accepted at GCPR 2019.</p> <p><strong>Abstract</strong></p> <p>Collagen fiber orientations in bones, visible with Second Harmonic Generation (SHG) microscopy, represent the inner structure and its alteration due to influences like cancer. While analyses of these orientations are valuable for medical research, it is not feasible to analyze the needed large amounts of local orientations manually. Since we have uncertain borders for these local orientations only rough regions can be segmented instead of a pixel-wise segmentation. We analyze the effect of these uncertain borders on human performance by a user study. Furthermore, we compare a variety of 2D and 3D methods such as classical approaches like Fourier analysis with state-of-the-art deep neural networks for the classification of local fiber orientations. We present a general way to use pretrained 2D weights in 3D neural networks, such as Inception-ResNet-3D a 3D extension of Inception-ResNet-v2. In a 10 fold cross-validation our two stage segmentation based on Inception-ResNet-3D and transferred 2D ImageNet weights achieves a human comparable accuracy.</p> <p><strong>Links</strong></p> <p>A preprint of the paper is available at <a href="https://arxiv.org/abs/1907.12868">https://arxiv.org/abs/1907.12868</a>.</p> <p>The final publication is available at Springer via <a href="https://doi.org/10.1007/978-3-030-33676-9_26">https://doi.org/10.1007/978-3-030-33676-9_26</a></p> <p>The source code is available at <a href="https://github.com/Emprime/uncertain-fiber-segmentation">https://github.com/Emprime/uncertain-fiber-segmentation</a>.</p> <p><strong>Data description</strong></p> <p>Please read the accompanying paper for more information about the dataset. Please see the source code for more information about the usage of the data.</p> <ul> <li>shg-ce-de: contains the enhanced and denoised scans as image slices, the scans are sorted by mice (wt wildtyp, het ill mice), scan location and individual scan</li> <li>shg-masks: contains the ground truth masks for the three different classes (similar - Green, dissimilar - Red, not of interest - blue)</li> <li>shg-featues: contains the input and gt for the second stage of the proposed two stage segmentation</li> <li>shg-cross-splits: contains the 10 random splits for the 10 fold cross validation</li> <li>logs-prediction: contains the 10 tensorboard logs, weights and predictions for the 10 fold cross validations</li> </ul>
Perturbations in fatty acid metabolism and collagen production infer pathogenicity of a novel MBTPS2 variant in Osteogenesis imperfecta
<p>(i) PCR-sequencing: Chromatograms were generated by PCR-sequencing of a region within exon 4 of MBTPS2 using DNA extracted from a healthy control and the proband's fibroblasts</p> <p>(ii) Gene expression was quantified by qRT-PCR using RNA extracted from fibroblasts. Transcript levels of each gene of interest was calculated using the 2^-deltaCt method with normalization to the average Ct values of endogenous control genes GAPDH, IPO8 and TBP.</p> <p>(iii) Cellular fatty acid content was quantified by GC-MS/MS. Each table represents one technical replicate. Absolute values of each fatty acid are listed in the tables; relative ratios of various fatty acids are calculated at the bottom of each table. </p> <p>(iv) Immunocytochemistry images of ECM proteins (COL1 = collagen type I; COL4 = collagen type IV; COL5 = collagen type V; a2b1 = integrin a2b1) and binding of collagen-hybridising peptide (R-CHP).</p>
Early Clinical Outcomes of High-Purity Type I Collagen as a Biologic Reinforcement in Selected Hernia Repair Scenarios
ClinicalTrials.gov study NCT07360691. IPD Sharing: YES. Countries: 1. Publications: 7.
Regenerative Collagen Scaffold for Breast Volume Restoration in Breast-Conserving Surgery
ClinicalTrials.gov study NCT07219316. IPD Sharing: YES. Countries: 1. Publications: 5.
Evaluation of High-Purity Type I Collagen Biologic Wrap to Improve Function After Extensor Tendon Repair of the Hand
ClinicalTrials.gov study NCT07335653. IPD Sharing: YES. Countries: 1. Publications: 7.
Vision Restoration With a Collagen Crosslinked Boston Keratoprosthesis Unit
ClinicalTrials.gov study NCT02863809. IPD Sharing: NO. Countries: 1. Publications: 1.
Data from: Preserved collagen reveals species identity in archaeological marine turtle bones from Caribbean and Florida sites
Open the record for dataset details and reuse information.
MALDI-TOF-MS archaeological spectra and for African bovid collagen for Zooarchaeology by Mass Spectrometry (ZooMS) from Zambia
<p>The MALDI data for archaeological samples from Zambia. The spectra are all in the folder in .mzml format. The samples are labeled the same as in the corresponding manuscript. The modern African bovid spectra that were used to determine markers can be found at Zenodo doi:10.5281/zenodo.3964709.</p>
Quality control for modern bone collagen stable carbon and nitrogen isotope measurements
<p><strong>(1)</strong> Isotopic analyses of collagen, the main protein preserved in sub fossil bone and tooth, has long provided a powerful tool for the reconstruction of ancient diets and environments. Although isotopic studies of contemporary ecosystems have typically focused on more accessible tissues (e.g., muscle, hair), there is growing interest in the potential for analyses of collagen because it is often available in hard tissue archives (e.g., scales, skin, bone, tooth), allowing for enhanced long-term retrospective studies. The quality of measurements of the stable carbon and nitrogen isotopic compositions of ancient samples are subject to robust and well-established criteria for detection of contaminants and digenesis. Among these quality control (QC) criteria, the most widely utilized is the atomic C:N ratio (C:N<sub>Atomic</sub>), which for ancient samples has an acceptable range between 2.9 and 3.6. While this QC criterion was developed for ancient materials, it has increasingly being applied to collagen from modern tissues.</p> <p><strong>(2)</strong> Here we use a large survey of published collagen amino acid compositions (n<em> </em>= 436) from 193 vertebrate species as well as recent experimental isotopic evidence from 413 modern collagen extracts to demonstrate that the C:N<sub>Atomic</sub> range used for ancient samples is not suitable for assessing collagen quality of modern and archived historical samples.</p> <p><strong>(3) </strong>For modern tissues, collagen C:N<sub>Atomic</sub> falling outside 3.00–3.30 for fish and 3.00–3.28 for mammals and birds can produce systematically skewed isotopic compositions and may lead to significant interpretative errors. These findings are followed by a review of protocols for improving C:N<sub>Atomic</sub> criteria for modern collagen extracts.</p> <p><strong>(4)</strong> Given the tremendous conservation and environmental policy-informing potential that retrospective isotopic analyses of collagen from contemporary and archived vertebrate tissues have for addressing pressing questions about long-term environmental conditions and species behaviours, it is critical that QC criteria tailored to modern tissues are established.</p>
Ectopical expression of bacterial collagen-like protein supports its role as adhesin in host-parasite coevolution
<div> <div> <div> <div> <p>For a profound understanding of antagonistic coevolution, it is necessary to identify the coevolving genes. The bacterium Pasteuria and its host, the microcrustacean Daphnia, are a well-characterized paradigm for co-evolution, but the underlying genes remain largely unknown. A genome-wide association study suggested a Pasteuria collagen-like protein 7 (Pcl7) as a candidate mediating parasite attachment and driving its coevolution with the host. Since Pasteuria ramosa cannot currently be genetically manipulated, we used Bacillus thuringiensis to express a fusion protein of a Pcl7 carboxy- terminus from P. ramosa and the amino-terminal domain of a B. thuringiensis collagen-like protein (CLP). Mutant B. thuringiensis (Pcl7-Bt) spores but not wild-type B. thuringiensis (WT-Bt) spores, attached to the same site of susceptible hosts as P. ramosa. Furthermore, Pcl7-Bt spores attached readily to susceptible host genotypes, but only slightly to resistant host genotypes. These findings indicated that the fusion protein was properly expressed and folded and demonstrated that indeed the C-terminus of Pcl7 mediates attachment in a host genotype-specific manner. These results provide strong evidence for the involvement of a CLP in the coevolution of Daphnia and P. ramosa and open new avenues for genetic epidemiological studies of host–parasite interactions.</p> </div> </div> </div> </div>
HT1080WT cells embedded in 3D collagen type I matrices - manual annotations for cell instance segmentation and tracking
<p>Human fibrosarcoma HT1080WT (ATCC) cells at low cell densities embedded in 3D collagen type I matrices [1]. The time-lapse videos were recorded every 2 minutes for 16.7 hours and covered a field of view of 1002 pixels × 1004 pixels with a pixel size of 0.802 μm/pixel The videos were pre-processed to correct frame-to-frame drift artifacts, resulting in a final size of 983 pixels × 985 pixels pixels.</p> <p><em>Hasini Jayatilaka, Anjil Giri, Michelle Karl, Ivie Aifuwa, Nicholaus J Trenton, Jude M Phillip, Shyam Khatau, and Denis Wirtz. EB1 and cytoplasmic dynein mediate protrusion dynamics for efficient 3-dimensional cell migration. FASEB J., 32(3):1207–1221, 2018. ISSN 0892-6638. doi: 10.1096/fj.201700444RR.</em></p> <p>Further information about how to use this data is given in <a href="http://github.com/esgomezm/microscopy-dl-suite-tf">https://github.com/esgomezm/microscopy-dl-suite-tf</a></p> <p><strong>This dataset is provided together with the following preprint and if you use it, we would like to kindly ask you to cite it properly:</strong></p> <p><a href="https://arxiv.org/abs/2112.08817">Estibaliz Gómez-de-Mariscal, Hasini Jayatilaka, Özgün Çiçek, Thomas Brox, Denis Wirtz, Arrate Muñoz-Barrutia, *Search for temporal cell segmentation robustness in phase-contrast microscopy videos*, arXiv 2021 (arXiv:2112.08817)</a></p>
Dipolar Relaxation of Water Protons in the Vicinity of a Collagen-Like Peptide: Input Files for Simulation
<p>Input files to run the simulations in the paper</p> <p>Journal: The Journal of Physical Chemistry B<br> Title: Dipolar relaxation of water protons in the vicinity of a collagen-like peptide<br> Authors: Jouni Karjalainen, Henning Henschel, Mikko J. Nissi, Miika T. Nieminen, Matti Hanni<br> DOI: 10.1021/acs.jpcb.2c00052</p>
Novel stereological method for estimation of cell counts in 3D collagen scaffolds
<p>Dataset provides all images used for cell number evaluation. The used macros are the part of Supplementary of the article.</p>
Monitoring of neoadjuvant chemotherapy through time domain diffuse optics: Breast tissue composition changes and collagen discriminative potential
<p>This dataset serves as a comprehensive resource containing the raw data, analyses, and various tools utilized to produce the findings that are presented in our paper titled ‘<strong>Monitoring of neoadjuvant chemotherapy through time domain diffuse optics: breast tissue composition changes and collagen discriminative potential</strong>’. </p> <p>The aim of this clinical study is to test broad spectral range (635-1060 nm) time domain diffuse optical spectroscopy to monitor the response of breast cancer patients to neoadjuvant chemotherapy. Preliminary results from patients on changes in hemoglobin, water, lipids, collagen concentrations, and scattering parameters due to the therapy are presented. In these initial results, we hypothesize that collagen could be a possible biomarker to distinguish complete and partial responders.</p>
ScienceDex guides
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These curated guides explain access requirements, typical timelines, costs, and reuse considerations for widely used research datasets.
Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.
International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.