Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

NAMPT translocates to the nucleus following interaction with GAPDH to sustain NAD synthesis

ABSTRACT: Cross-Linking LC-MS analysis of NAMPT-GAPDH complex

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

SUBMITTER: Armando Genazzani

PROVIDER: MSV000084426 | MassIVE | Mon Oct 07 03:19:00 BST 2019

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Enhanced protein-protein interaction network construction promoted by in vivo cross-linking

Project description:Chemical cross-linking coupled with mass spectrometry has emerged as a powerful strategy which enables global profiling of protein interactome with direct interaction interfaces in complex biological systems. The alkyne-tagged enrichable cross-linkers are preferred to improve the coverage of low-abundance cross-linked peptides, combined with click chemistry for biotin conjugation to allow the cross-linked peptides enrichment. Herein, together with in vivo chemical cross-linking by alkyne-tagged cross-linker, we explored the click chemistry-based enrichment approaches on protein and peptide level with three cleavable click chemistry ligands, respectively. By comparison, the approach of protein-based click chemistry conjugation with acid-cleavable tag was demonstrated to permit the most cross-linked peptides identification. The advancement of this strategy enhanced the proteome-wide cross-linking analysis, constructing a 5,518 protein-protein interactions network among 1,871 proteins with wide abundance distribution in cell. Therefore, all these results demonstrated a guideline value of our work for efficient cross-linked peptides enrichment, thus facilitated the in-depth profiling of protein interactome for functional analysis.

2022-07-15 | PXD035355 | JPOST Repository

Analysis of the structure of the MTA1 complex using chemical cross-linking mass spectrometry

Project description:Analysis of the structure of the MTA1 complex using chemical cross-linking mass spectrometry

2022-11-30 | PXD038459 |

Enhanced protein-protein interaction network construction promoted by in vivo cross-linking with acid-cleavable click chemistry enrichment

Project description:Chemical cross-linking coupled with mass spectrometry has emerged as a powerful strategy which enables global profiling of protein interactome with direct interaction interfaces in complex biological systems. The alkyne-tagged enrichable cross-linkers are preferred to improve the coverage of low-abundance cross-linked peptides, combined with click chemistry for biotin conjugation to allow the cross-linked peptides enrichment. However, a systematic evaluation on the efficiency of click approaches (protein-based or peptide-based) and diverse cleavable click chemistry ligands (acid, reduction, photo) for cross-linked peptides enrichment and release is lacking. Herein, together with in vivo chemical cross-linking by alkyne-tagged cross-linker, we explored the click chemistry-based enrichment approaches on protein and peptide level with three cleavable click chemistry ligands, respectively. By comparison, the approach of protein-based click chemistry conjugation with acid-cleavable tag was demonstrated to permit the most cross-linked peptides identification. The advancement of this strategy enhanced the proteome-wide cross-linking analysis, constructing a 5,518 protein-protein interactions network among 1,871 proteins with wide abundance distribution in cell. Therefore, all these results demonstrated a guideline value of our work for efficient cross-linked peptides enrichment, thus facilitated the in-depth profiling of protein interactome for functional analysis.

2022-07-14 | PXD035317 | JPOST Repository

HeLa mRNA interactome

Project description:Pull-down of poly(A)-mRNA cross linked proteins using two cross-linking methods (conventional cross-linking and PAR-cross-linking) to identify all mRNA-binding proteins (GO:0003729). The provided data is quantitative proteomic data for comparison of cross-linking and control samples.

2012-08-14 | E-MTAB-869 | biostudies-arrayexpress

In planta chemical crosslinking and mass spectrometry analysis of protein structure and interaction in Arabidopsis

Project description:Mass spectrometry analysis in combination with the site-specific chemical cross-linking has emerged as a powerful method in study of three-dimensional structure of protein complex and in mapping of protein-protein interactions (PPIs). Even though in vitro cross-linking experiments have been widely applied to investigate the specific interactions of a bait protein and its targets, the measurement of in vivo protein tertiary structure and PPIs has been problematic and strenuous due to the dynamic nature of the biological systems and a lower number of cross-linked peptides that can be isolated via MudPIT (Multidimensional Protein Identification Technology) for mass spectrometry analysis. Using Arabidopsis thaliana as a model multicellular eukaryotic organism, we have attempted to develop an improved in vivo chemical cross-linking and mass spectrometry (or IPXL-MS) workflow, which aims at optimizing the in vivo cross-linking conditions, establishing of a MudPIT procedure for enrichment of cross-linked peptides, and developing an integrated software program to identify the in planta chemical cross-linked peptides, by which three pairs of in vivo cross-linked peptides of high-confidence has been identified twice from two independent biological replicates. This work has demarked a beginning of alternative proteomic approach in study of in vivo protein tertiary structure and PPIs in higher plants. This in vivo cross-linking approach may be applied into other model multicellular organisms, such as mouse, for molecular systems biological research.

2016-06-28 | PXD003658 | Pride

GNPS - Systematic analysis of NDUFAF6 in complex I assembly and mitochondrial disease

Project description:Cross-linking AE-MS dataset for NDUFAF6 interactions

2024-03-08 | MSV000094276 | GNPS

Dam1 complex-microtubule interaction

Project description:we used cross-linking mass spectrometry to determine the molecular architecture of the Dam1 complex alone and bound to microtubules. Our data provide a map of the subunit arrangement of the Dam1 complex. Analysis of the Dam1 complex assembled around microtubules reveals that the Spc34 and Ask1 subunits are likely involved in self -assembly whereas the Duo1 and Dam1 subunits both interact with microtubules. We also demonstrate that the C termini of Dam1 and Duo1 provide the microtubule binding properties to the Dam1 complex. Our data provides key information on the organization of the Dam1 complex around microtubules.

2016-03-01 | PXD003678 | Pride

Molecular view of ER membrane remodeling by the Sec61/TRAP translocon

Project description:Cross-linking mass spectrometry of the sheep Sec61-TRAP complex

| MSV000090438 | MassIVE

Molecular Architecture of the Yeast Mediator Complex

Project description:Cross-linking MS data from the yeast Mediator complex. Cross-linking was performed using either BS3 or 1:1 mix of d0:d12 DSS. Includes unfractionated, SEC enriched, high pH reverse phase fractionated, DDA and inclusion list generated files.

2015-08-13 | MSV000079237 | MassIVE

TMEM175-LAMP1 crosslinking proteomics

Project description:Raw data of cross linking sites mapping of TMEM175-LAMP1 complex.

2023-04-10 | MSV000091672 | MassIVE