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34 results for “trypsin”

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zenodo44/100

X-ray diffraction images of bovine trypsin crystals recorded at the FemtoMAX beamline of Max IV synchrotron facility

<p>The deposition concerns bovine trypsin diffraction images in two wedges. Each image is&nbsp;recorded on a still crystal and&nbsp;separated by 0.1 deg rotation. The x4.tar.gz archive contains summed intensities from individual snapshots at the same orientation, whereas&nbsp;x4_single.tar.gz archive contains single snapshots/orientation.&nbsp;</p>

opencc-by-4.0Nov 2020View details →
zenodo44/100

Radiofrequency ultrasound signals from bovine cartilage samples degraded with trypsin and collagenase

The folder Repository_RF_data contains the radiofrequency (RF) data acquired with an ArtUS EXT-1H system (Telemed, Italy) equipped with a 192 elements linear probe L15-7H40-A5 working in the frequency range 7.5-15 MHz, in the matlab format ".mat". Data were collected at 15 MHz, with a sampling rate of 40 MHz, adjusting the focus in the middle of the samples. The analysed samples were bovine cartilage samples, divided in three groups: - Control group: cartilage sample without any chemical treatment. - Trypsin group: cartilage samples immersed in a trypsin solution for 4h. - Collagenase group: cartilage samples immersed in a collagenase solution for 24h. The folder Repository_RF_data includes 2 matlab variables: - trypsin.mat = data acquired from 6 samples before and after the trypsin treatment - collagenase.mat = data acquired from 6 samples before and after the collagenase treatment Each variable is a TxN cell, where T is the time point of evaluation and N is the number of samples. The first row of each variable corresponds to the time zero of treatment, that is the control group; while the second row includes measurement at the final time point of treatment (4h for trypsin an 24h for collagenase). In particular, a single RF frame was acquired for all the analyses. Each recorded RF frame resulted in a matrix in which the columns (57) represented the number of RF scanning lines in a specific RF window, while the rows (727) constituted the number of samples in a single scanning line. For the details, see the articles published on Annual International Conference of the IEEE Engineering in Medicine and Biology Society: Sorriento A, Cafarelli A, Valenza G, Ricotti L. Ex-vivo quantitative ultrasound assessment of cartilage degeneration. Annu Int Conf IEEE Eng Med Biol Soc. 2021 Nov;2021:2976-2980. doi: 10.1109/EMBC46164.2021.9630198. PMID: 34891870.

opencc-by-4.0Mar 2022View details →
zenodo36/100

Representative structures for Trypsin-Benzamidine conformation-space network

<p>These structures were used for the analysis presented in the paper "Multiple Ligand Unbinding Pathways and Ligand-Induced Destabilization Revealed by WExplore" published in Biophysical Journal, 112, February 28, 2017.  There is a tar ball (allframes.tgz) containing 4000 structures in PDB format, as well as a PDF file of the network with labels for each of the 4000 states (network_labels.pdf).  Unpack the tar ball with: "tar xzf allframes.tgz".</p> <p> </p>

opencc-by-4.0Jan 2017View details →
zenodo36/100

Raw data to: Biochemical Analyses of Cystatin-C Dimers and Cathepsin-B reveals a Trypsin-Driven Feedback Mechanism in Acute Pancreatitis

<p>This repository contains the initial structures, full conformational ensembles sampled using the TIGER2hPE replica-exchange MD simulation technique, and clusters resulting from subsequent ccPCA analysis, to extract major complex structures between proteins. Also attached are the initial structures of mCTSB and mCST3 predicted by AlphaFold2.</p> <table> <tbody> <tr> <td> <p><strong>Simulation Nr.</strong></p> </td> <td> <p><strong>Components simulated<br></strong></p> </td> </tr> <tr> <td> <p><strong>1</strong></p> </td> <td> <p>CTSB</p> </td> </tr> <tr> <td> <p><strong>2</strong></p> </td> <td> <p>CTSB</p> </td> </tr> <tr> <td> <p><strong>3</strong></p> </td> <td> <p>CTSB + mCST3</p> </td> </tr> <tr> <td> <p><strong>4</strong></p> </td> <td> <p>CTSL + mCST3</p> </td> </tr> <tr> <td> <p><strong>5</strong></p> </td> <td> <p>CTSB + mCST3-R71</p> </td> </tr> <tr> <td> <p><strong>6</strong></p> </td> <td> <p>CTSB + mCST3-R45</p> </td> </tr> <tr> <td> <p><strong>7</strong></p> </td> <td> <p>CTSB + dCST3-R45</p> </td> </tr> <tr> <td> <p><strong>8</strong></p> </td> <td> <p>CTSB + dCST3-R28</p> </td> </tr> </tbody> </table>

opencc-by-4.0Sep 2024View details →
zenodo36/100

Raw diffraction images of 5-Chlorotryptamine-bound trypsin

<p>Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting these long chains of amino acids into smaller pieces.&nbsp;</p> <p>We used datasets to investigate the protocol of detecting polymorphs using Hierarchical clustering (Acta D., submitted). All diffraction data were collected at BL32XU, SPring-8, using an automated data collection system&nbsp;<em>ZOO</em>. Data were acquired from four crystals of 5-Chlorotryptamine-bound trypsin. All datasets were collected using a continuous helical scan scheme for 360&ordm; oscillation with the following experimental parameters; Beam size: 10 &micro;m &times; 15 &micro;m, Wavelength: 1.0000 &Aring;, Total dose/crystal: 10 MGy, Detector: EIGER X 9M (DECTRIS Co. Ltd.). All crystals belonged to space group P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub>&nbsp;with unit cell parameters roughly corresponding to a=54.5, b=58.6, c=66.6 &Aring;.</p>

opencc-by-4.0Oct 2023View details →
zenodo36/100

Raw diffraction images of 4-Methoxybenzamidine-bound trypsin

<p>Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting these long chains of amino acids into smaller pieces.&nbsp;</p> <p>We used datasets to investigate the protocol of detecting polymorphs using Hierarchical clustering (Acta D., submitted). All diffraction data were collected at BL32XU, SPring-8, using an automated data collection system&nbsp;<em>ZOO</em>. Data were acquired from four crystals of 4-Methoxybenzamidine -bound trypsin. All datasets were collected using a continuous helical scan scheme for 360&ordm; oscillation with the following experimental parameters; Beam size: 10 &micro;m &times; 15 &micro;m, Wavelength: 1.0000 &Aring;, Total dose/crystal: 10 MGy, Detector: EIGER X 9M (DECTRIS Co. Ltd.). All crystals belonged to space group P212121 with unit cell parameters roughly corresponding to a=54.6, b=58.6, c=66.7 &Aring;.</p>

opencc-by-4.0Oct 2023View details →
ClinicalTrials.gov36/100

Alpha-1 Anti-Trypsin (AAT) Treatment in Acute Myocardial Infarction

ClinicalTrials.gov study NCT01936896. IPD Sharing: Not stated. Countries: 1. Publications: 1.

restrictedIPD-UNDECIDEDFeb 2026View details →
ClinicalTrials.gov36/100

Comparing Trypsin-Chymotrypsin and Naproxen Sodium for Post-endodontic Treatment Pain

ClinicalTrials.gov study NCT06562816. IPD Sharing: NO. Countries: 1. Publications: 6.

closedIPD-NOFeb 2026View details →
ClinicalTrials.gov36/100

Efficacy of Trypsin-Chymotrypsin On Post-operative Pain After Single Visit Root Canal Treatment

ClinicalTrials.gov study NCT05479747. IPD Sharing: NO. Countries: 1. Publications: 1.

closedIPD-NOFeb 2026View details →
zenodo32/100

Raw diffraction images of a crystal of Bovine trypsin collected by Direct Data Collection (DDC) using the ESRF RoboDiff goniometer

<p>In order to demonstrate the data collection capabilities of the RoboDiff diffraction data were collected from a crystal of Bovine trypsin to demonstrate the suitability of the beamline MASSIF-1 and RoboDiff for standard data collection.</p>

opencc-zeroMay 2016View details →
zenodo32/100

Dataset DOE of non-ionic aqueous micellar extraction of trypsin inhibitors and isoflavones from soybean meal

<p>Design of Experiments data from the work &quot;Non-ionic aqueous micellar extraction of trypsin inhibitors and isoflavones from soybean meal: process optimization&quot;</p>

opencc-by-4.0Jun 2022View details →
zenodo32/100

Fig. 2 in Molecular cloning of the trypsin inhibitor from the skin secretion of the Madagascan Tomato Frog, Dyscophus guineti (Microhylidae), and insights into its potential defensive role

Fig. 2 Reverse phase HPLC chromatogram of the skin secretion from Dyscophus guineti (a). For the fraction in (a) marked with an arrow, a clear inhibition of trypsin activity was observed (b)

opennotspecifiedFeb 2013View details →
zenodo32/100

Rosetta Loop Modeling Data for "A Systematic Approach for Evaluating the Role of Surface-Exposed Loops in Trypsin-like Serine Proteases: Analysis of the 170 loop in Coagulation Factor VIIa"

<p>Rosetta Loop Modeling data for the publication &quot;A Systematic Approach for Evaluating the Role of Surface-Exposed Loops in Trypsin-like Serine Proteases: Analysis of the 170 loop in Coagulation Factor VIIa.&quot;&nbsp;See the included readme.txt for more details. Please cite the paper if you use these data.</p>

opencc-by-4.0Sep 2021View details →
zenodo32/100

Molecular dynamics dataset of Trypsin-Benzamidine

<p>This dataset contains all-atom molecular dynamics trajectories of&nbsp;Trypsin-Benzamidine. All details regarding the molecular dynamics setup are given in references [1, 2]. The dataset consists of two parts&nbsp;and comes with a time step of&nbsp;100 ps.</p> <p><strong>long-trajs.tar</strong>:&nbsp;cumulative of 100 &micro;s of MD data in trajectories of 48 x 2 &micro;s and 4 x 1 &micro;s. Generated&nbsp;and used in&nbsp;[1].</p> <p><strong>gpugrid-trajs.tar</strong>: cumulative of 49.5 &micro;s&nbsp;of MD data in trajectories of 495 x 100 ns. Generated for [2] and used in [1, 2].</p> <p>[1]&nbsp;Plattner, N.; No&eacute;, F. Protein Conformational Plasticity and Complex Ligand-Binding Kinetics Explored by Atomistic Simulations and Markov Models.&nbsp;<em>Nature Communications</em>&nbsp;<strong>2015</strong>,&nbsp;<em>6</em>, 7653.&nbsp;<a href="https://doi.org/10.1038/ncomms8653">https://doi.org/10.1038/ncomms8653</a>.&nbsp;</p> <p>[2] Buch, I.; Giorgino, T.; De Fabritiis, G. Complete Reconstruction of an Enzyme-Inhibitor Binding Process by Molecular Dynamics Simulations.&nbsp;<em>Proc. Natl. Acad. Sci. U.S.A.</em>&nbsp;<strong>2011</strong>,&nbsp;<em>108</em>&nbsp;(25), 10184&ndash;10189.&nbsp;<a href="https://doi.org/10.1073/pnas.1103547108">https://doi.org/10.1073/pnas.1103547108</a>.</p>

opencc-by-4.0Sep 2023View details →
ClinicalTrials.gov32/100

Study to Investigate the Mechanism of Action of an Oral Enzyme Treatment With Bromelain, Trypsin and Rutoside Versus Placebo in Subjects With OsTeoarthritis

ClinicalTrials.gov study NCT05038410. IPD Sharing: Not stated. Countries: 1. Publications: 1.

restrictedIPD-UNDECIDEDFeb 2026View details →
ClinicalTrials.gov32/100

Healing Potentiality of Trypsin and Alpha Chemo Trypsin in Mandibular Molars With Chronic Apical Abscess

ClinicalTrials.gov study NCT06164509. IPD Sharing: NO. Countries: 1. Publications: 2.

closedIPD-NOFeb 2026View details →
ClinicalTrials.gov32/100

How Secreted-embryo-derived Trypsin Initiates, Maintains and Terminates Ca2+ Signals in Uterine Epithelial Cells

ClinicalTrials.gov study NCT04865367. IPD Sharing: NO. Countries: 1. Publications: 15.

closedIPD-NOFeb 2026View details →
ClinicalTrials.gov32/100

Epigenetic Regulation of Immunity in Alpha-1 Anti-trypsin Deficiency

ClinicalTrials.gov study NCT02691611. IPD Sharing: NO. Countries: 1. Publications: 33.

closedIPD-NOFeb 2026View details →
zenodo28/100

Fig. 3 in Molecular cloning of the trypsin inhibitor from the skin secretion of the Madagascan Tomato Frog, Dyscophus guineti (Microhylidae), and insights into its potential defensive role

Fig. 3 MALDI-TOF mass spectrum of the protease inhibitor-containing fraction

opennotspecifiedFeb 2013View details →
zenodo28/100

Raw diffraction images of apo-trypsin

<p>Trypsin is an enzyme in the first section of the small intestine that starts the degestion of protein molecules by cutting these long chains of amino acids into smaller pieces.</p> <p>We used datasets to investigate the protocol of detecting polymorphs using Hierarchical clustering (Acta D., submitted). All diffraction data were collected at BL32XU, SPring-8, using an automated data collection system&nbsp;<em>ZOO</em>. Data were acquired from four crystals for apo-form, 4-Methoxybenzamidine(benzamidine)-bound, and 5-Chlorotryptamine(tryptamine)-bound trypsin crystals, respectively. All datasets were collected using a continuous helical scan scheme for 360&ordm; oscillation with the following experimental parameters; Beam size: 10 &micro;m &times; 15 &micro;m, Wavelength: 1.0000 &Aring;, Total dose/crystal: 10 MGy, Detector: EIGER X 9M (DECTRIS Co. Ltd.). All crystals belonged to the space group P212121 with the unit cell parameters roughly corresponding to a=54.5, b=58.4, 66.8&nbsp;&Aring;.</p>

opencc-by-4.0Oct 2023View details →

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