DR-NTU (Data)

Metrics

987,948 Downloads

Deposit, archive and share your final research data in DR-NTU (Data)

DR-NTU (Data) is for research data deposit. For research paper deposits, please use DR-NTU.

Mission: DR-NTU (Data) curates, stores, preserves, makes available and enables the download of digital data generated by the NTU research community. The repository develops and provides guidance for managing, sharing, and reusing research data to promote responsible data sharing in support of open science and research integrity.

Who can deposit? NTU faculty, research staff and students.

What can be deposited? Final, non-sensitive research data from projects carried out at NTU. The uploaded content must not infringe upon the copyrights or other intellectual property rights, and must be void of all identifiable information.

How to deposit?

Useful links: FAQs | Collection Guidelines | NTU Research Data Management | General terms of use and Privacy policy

FAIR Datasets

NIE Data Repository (Harvested)

Asian School of the Environment (ASE)

College of Computing and Data Science (CCDS)

Earth Observatory of Singapore (EOS)

Graduate College

Lee Kong Chian School of Medicine

Nanyang Business School (NBS)

School of Art, Design and Media (ADM)

School of Biological Sciences (SBS)

School of Chemistry, Chemical Engineering and Biotechnology (CCEB)

School of Civil and Environmental Engineering (CEE)

School of Electrical and Electronic Engineering (EEE)

School of Humanities

School of Materials Science and Engineering (MSE)

School of Mechanical and Aerospace Engineering (MAE)

School of Physical and Mathematical Sciences (SPMS)

School of Social Sciences (SSS)

S. Rajaratnam School of International Studies

Wee Kim Wee School of Communication and Information (WKWSCI)

Featured Dataverses

In order to use this feature you must have at least one published dataverse.

Publish Dataverse

Are you sure you want to publish your dataverse? Once you do so it must remain published.

Publish Dataverse

This dataverse cannot be published because the dataverse it is in has not been published.

Delete Dataverse

Are you sure you want to delete your dataverse? You cannot undelete this dataverse.

961 to 970 of 73,600 Results

20210610 Confocal Sedimentation controls.tif Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction TIFF Image - 6.1 MB - MD5: 2f8a033ca5b4db1b35292782a7c6ec70
20210610 Confocal Sedimentation with EPYC1-GFP.tif Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction TIFF Image - 6.1 MB - MD5: 9862b8f0c39480e61c0c1a11a2f47244
20211229 ATPase Assay data JB R25 R26 R43 R38 R20 R30.xlsx Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction MS Excel Spreadsheet - 166.7 KB - MD5: 614ca7353d0d9cfd11fa2403e626e495
20211229 ATPase assay R25 R26 R43 R38 R20 R30.txt Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction Plain Text - 27.9 KB - MD5: 9b3ab43ae1e702f4d82e68c4663bf4f5
20220217 Triple component LLPS salt sensitivity rerun 20220214 B1-B7.tab Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction Tabular Data - 1.5 KB - 20 Variables, 10 Observations - UNF:6:+ZB1XbmVTnLbZ4v+aRyfsg==
20220217 Triple component LLPS salt sensitivity rerun 20220214 B1-B7.tif Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction TIFF Image - 10.8 MB - MD5: 7d2372f687afe4a570a0414caea826f0
20220217 Triple component LLPS salt sensitivity rerun 20220214 B1-B7.tif (RGB)_16bit_invert.scn Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction Unknown - 3.7 MB - MD5: 5e3085ef34fa872b0c16b525d014b050
20220217 Triple component LLPS salt sensitivity rerun 20220214 B1-B7.tif (RGB)_16bit_invert.tif Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction TIFF Image - 3.6 MB - MD5: 62bc7c60766f19eb68023e1f768196a2
20220309 CrRca and EPYC1 salt sensitivity repeat 20220303 lo-bind tubes A1-A7_16bit_invert.scn Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction Unknown - 2.2 MB - MD5: 4b1173921f97b1e6ed562f954bf24895
20220309 CrRca and EPYC1 salt sensitivity repeat 20220303 lo-bind tubes A1-A7_16bit_invert.tab Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction Tabular Data - 916 B - 9 Variables, 15 Observations - UNF:6:FQcn9sA5UoaZCPDCO6q6SQ==

20210610 Confocal Sedimentation controls.tif

Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction

TIFF Image - 6.1 MB -

20210610 Confocal Sedimentation with EPYC1-GFP.tif

Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction

TIFF Image - 6.1 MB -

20211229 ATPase Assay data JB R25 R26 R43 R38 R20 R30.xlsx

Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction

MS Excel Spreadsheet - 166.7 KB -

20211229 ATPase assay R25 R26 R43 R38 R20 R30.txt

Dec 5, 2025 - Data for: Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction

Plain Text - 27.9 KB -