PXD067225

PXD067225 is an original dataset announced via ProteomeXchange.

Title	Effect of heat-shock on total, poly-ubiquitylated, and insoluble proteomes of human IMR-90 fibroblasts in different proliferation states
Description	Cellular stress responses are crucial for survival in sub-optimal conditions, and almost invar-iably involve proteome-wide alterations at the levels of protein abundance, post-translational modification with poly-ubiquitin chains (poly-ubiquitylation), and solubility. However, most of our understanding of human cell stress responses at the protein level stems from experi-ments in rapidly-dividing cell culture models. Here, we used primary human diploid lung fibro-blasts (IMR-90) in proliferating, contact-inhibited quiescent, or doxorubicin-induced senes-cent states, to explore their responses to a severe heat-shock (44 degrees Celsius for 2 hours) at the total, poly-ubiquitylated, and insoluble proteome levels.
HostingRepository	PRIDE
AnnounceDate	2025-10-08
AnnouncementXML	Submission_2025-10-08_10:34:28.256.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Harvey Johnston
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2025-08-11 14:58:43	ID requested
⏵ 1	2025-10-08 10:34:28	announced

10.1101/2025.09.07.674107;

submitter keyword: Human, LC-MSMS, Proteostasis, Quiescence, Insoluble, Lung, Stress, Senescence, Heat-Shock, Fibroblast, Ubiquitin, Aggregate

Rahul Samant
contact affiliation	Signalling ISP, Babraham Institute, Cambridge, UK
contact email	rahul.samant@babraham.ac.uk
lab head
Harvey Johnston
contact affiliation	The Babraham Institute
contact email	harvey.johnston@babraham.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD067225
     1. Label: PRIDE project
     2. Name: Effect of heat-shock on total, poly-ubiquitylated, and insoluble proteomes of human IMR-90 fibroblasts in different proliferation states