Browse
Submit Data
Databases
API
Help

Dataset Information

324 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Thermal proteome profiling of JQ1

ABSTRACT: Goal of this experiment was the identification of proteins affected in their thermal stability by JQ1.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte

SUBMITTER: Maria Faelth Savitski

LAB HEAD: Marcus Bantscheff

PROVIDER: PXD008638 | Pride | 2018-05-02

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	01263_F1_R1_P0124030B02_TMT10.raw.gz	Raw
	01263_F1_R1_P0124030B03_TMT10.raw.gz	Raw
	01263_F1_R1_P0124030B04_TMT10.raw.gz	Raw
	01263_F1_R1_P0124030B05_TMT10.raw.gz	Raw
	01263_F1_R1_P0124030B06_TMT10.raw.gz	Raw

Items per page:

1 - 5 of 124

Publications

Multiplexed Proteome Dynamics Profiling Reveals Mechanisms Controlling Protein Homeostasis.

Savitski Mikhail M MM Zinn Nico N Faelth-Savitski Maria M Poeckel Daniel D Gade Stephan S Becher Isabelle I Muelbaier Marcel M Wagner Anne J AJ Strohmer Katrin K Werner Thilo T Melchert Stephanie S Petretich Massimo M Rutkowska Anna A Vappiani Johanna J Franken Holger H Steidel Michael M Sweetman Gavain M GM Gilan Omer O Lam Enid Y N EYN Dawson Mark A MA Prinjha Rab K RK Grandi Paola P Bergamini Giovanna G Bantscheff Marcus M

Cell 20180315 1

Protein degradation plays important roles in biological processes and is tightly regulated. Further, targeted proteolysis is an emerging research tool and therapeutic strategy. However, proteome-wide technologies to investigate the causes and consequences of protein degradation in biological systems are lacking. We developed "multiplexed proteome dynamics profiling" (mPDP), a mass-spectrometry-based approach combining dynamic-SILAC labeling with isobaric mass tagging for multiplexed analysis of ...[more]

PMID: 29551266

Similar Datasets

2 Dimensional Thermal proteome profiling of JQ1

Project description:Goal of this experiment was the identification of proteins affected dose dependently in their thermal stability by JQ1.

2018-05-02 | PXD008626 | Pride

Thermal proteome profiling of Jurkat cells

Project description:Determine melting temperature of proteins in Jurkats

2018-05-02 | PXD008639 | Pride

Nonionic surfactants can modify the thermal stability of globular and membrane proteins interfering with the thermal proteome profiling principles to identify protein targets

Project description:The membrane proteins are essential targets to understand cellular function. The unbiased identification of membrane protein targets is still the bottleneck for a system- level understanding of cellular response to stimuli or perturbations. It has been suggested to enrich the soluble proteome with membrane proteins by introducing nonionic surfactants in the solubilization solution. This strategy was aiming to simultaneous identify the globular and membrane protein targets by thermal proteome profiling principles. However, the thermal shift assay would surpass the cloud point temperature from the nonionic surfactants most frequently utilized for membrane protein solubilization. It is expected that around the cloud point temperature, the surfactant micelles would suffer structural modifications altering the proteome solubility. Here, we show that the presence of nonionic surfactants can alter protein thermal stability from a mixed globular, and membrane proteome. In the presence of surfactant micelles, the changes in protein solubility analyzed after the thermal shift assay are affected by the thermal dependent modification of the micelles size, and their interaction with proteins. We demonstrate that the introduction of nonionic surfactants for the solubilization of membrane proteins is not compatible with the principles of target identification by thermal proteome profiling methodologies. Our results lead to explore thermal-independent strategies for membrane protein solubilization to assure confident membrane protein target identification. The proteome-wide thermal shift methods have already shown their capability to elucidate mechanism of actions from pharma, biomedicine, analytical chemistry, or toxicology and finding strategies, free from surfactants, to identify membrane protein targets would be the next challenge.

2023-03-20 | PXD037153 | Pride

Protocol for performing and analyzing TPP-TR and TPP-CCR experiments

Project description:Explore the effect of Panobinostat on the thermal stability of the proteins of the K562 cell line proteome.

2019-05-24 | PXD013774 | Pride

Coral thermal tolerance: tuning gene expression to resist thermal stress

Project description:Thermal history plays a role in the response of corals to subsequent heat stress. Prior heat stress can have a profound impact on later thermal tolerance, but the mechanism for this plasticity is not clear. The understanding of gene expression changes behind physiological acclimatization is critical in forecasts of coral health in impending climate change scenarios. Acropora millepora fragments were preconditioned to sublethal bleaching threshold stress for a period of 10 days; this prestress conferred bleaching resistance in subsequent thermal challenge, in which non-preconditioned coral bleached. Using microarrays, we analyze the transcriptomes of the coral host, comparing the bleaching-resistant preconditioned treatment to non-preconditioned and control treatments. This experiment compared host gene expression of Acropora millepora across control, non-preconditioned, and preconditioned treatments. Fragments were sampled prior to preconditioning (Day 4), following 10 days of thermal preconditioning (Day 20), and after two (Day 23), four (Day 25), and eight days (Day 29) of 31M-BM-0C thermal challenge. The analysis implements 45 arrays, representing 5 sampling points of three treatments (n=3).

2012-11-29 | E-GEOD-41435 | biostudies-arrayexpress

Multiplexed proteome dynamics profiling of HSP90 inhibitor 17-AAG

Project description:Investigation of proteostatic effects of HSP90 inhibition by 17-AAG and differentiation of maturation state dependent HSP90 requirements of proteins.

2018-04-05 | PXD008633 | Pride

Multiplexed proteome dynamics profiling of Estradiol and SERMs

Project description:Investigation of proteostatic effects of Estradiol, raloxifen and GW7604 in MCF7 cells.

2018-05-02 | PXD008636 | Pride

Thermal proteome profiling of sponge whole-body movement

Project description:Sponges (Porifera) are early-branching Metazoa who do not possess muscles or neurons, however are able to undergo a whole-body movement that involves the closure of their canal system and collapse of an epithelial tent. In this study we profile proteomic responses of the freshwater sponge Spongilla lacustris during nitric oxide (NO) and agitation induced movements to elucidate the early evolution of coordination. Specifically, we measure condition-dependent changes in protein thermal stability and abundance using Thermal proteome profiling (TPP). These changes are the result of proteins undergoing stabilizing or destabilizing conformational changes broadly caused by e.g. the binding or dissociation of small molecules to the proteins, the formation or loss of protein-protein interactions or a change in post-translational modifications.

2024-01-04 | PXD044169 | Pride

De novo mapping of the apicomplexan Ca2+-responsive proteome: temperature range thermal profiling experiment

Project description:Apicomplexan parasites cause persistent mortality and morbidity worldwide through diseases including malaria, toxoplasmosis, and cryptosporidiosis. Ca2+ signaling pathways have been repurposed in these eukaryotic pathogens to regulate parasite-specific cellular processes governing the transition between the replicative and lytic phases of the infectious cycle. Despite the presence of conserved Ca2+-responsive proteins, little is known about how specific signaling elements interact to impact pathogenesis. We mapped the Ca2+-responsive proteome of the model apicomplexan T. gondii via time-resolved phosphoproteomics and thermal proteome profiling. The waves of phosphoregulation following PKG activation and stimulated Ca2+ release corroborate known physiological changes but identify specific molecular components in these pathways. Thermal profiling of parasite extracts identified many expected Ca2+-responsive proteins, such as parasite Ca2+-dependent protein kinases. Our approach also identified numerous Ca2+-responsive proteins that are not predicted to bind Ca2+, yet are critical components of the parasite signaling network. We characterized protein phosphatase 1 (PP1) as a Ca2+-responsive enzyme that relocalized to the parasite apex upon Ca2+ store release. Conditional depletion of PP1 revealed that the phosphatase regulates Ca2+ uptake to promote parasite motility. PP1 may thus be partly responsible for Ca2+-regulated serine/threonine phosphatase activity in apicomplexan parasites.

2022-10-15 | PXD033713 | Pride