Proteomics

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Comparative interactome analysis of Nematostella vectensis Hsp70 isoforms reveals unique clientome remodeling upon heat stress.


ABSTRACT: Comparative interactome analysis of Nematostella vectensis Hsp70 isoforms reveals unique clientome remodeling upon heat stress. Three isoforms of nvHSP70 (A, B, and D) were IP'd from either Heat Shock conditions (HS) or non-Heat Shock (UN) and their interactomes were compared. Mass Spec was run on a Q-Exactive (Orbitrap).

INSTRUMENT(S): Q Exactive

ORGANISM(S): Nematostella Vectensis Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Donald Wolfgeher  

LAB HEAD: Andrew W. Truman

PROVIDER: PXD012144 | Pride | 2019-06-25

REPOSITORIES: Pride

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Publications

Dynamic remodeling of the interactomes of Nematostella vectensis Hsp70 isoforms under heat shock.

Knighton Laura E LE   Nitika   Waller Shawn J SJ   Strom Owen O   Wolfgeher Donald D   Reitzel Adam M AM   Truman Andrew W AW  

Journal of proteomics 20190621


Heat shock protein 70s (Hsp70s) are a highly conserved class of molecular chaperones that fold a large proportion of the proteome. Nematostella vectensis (Nv) is an estuarine sea anemone that has emerged as a model species to characterize molecular responses to physiological stressors due to its exposure to diverse, extreme abiotic conditions. Previous transcriptional data has shown dramatic differences among expression profiles of three NvHsp70 isoforms (NvHsp70A, B and D) under stress but it i  ...[more]

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