Dual roles for ATP in the regulation of phase separated protein aggregates in oocyte nucleoli

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Dual roles for ATP in the regulation of phase separated protein aggregates in oocyte nucleoli

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im Juli 2018 veröffentlichter wissenschaftlicher Artikel

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scientific article published on 17 July 2018

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wetenschappelijk artikel

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наукова стаття, опублікована в липні 2018

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Dual roles for ATP in the regu ...... aggregates in oocyte nucleoli

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Dual roles for ATP in the regu ...... aggregates in oocyte nucleoli

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Dual roles for ATP in the regu ...... aggregates in oocyte nucleoli

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Dual roles for ATP in the regu ...... aggregates in oocyte nucleoli

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Dual roles for ATP in the regu ...... aggregates in oocyte nucleoli

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Dual roles for ATP in the regu ...... aggregates in oocyte nucleoli

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P1476

Dual roles for ATP in the regu ...... tes in Xenopus oocyte nucleoli

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P2093

Elizabeth H Peuchen

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Michael H Hayes

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Norman J Dovichi

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P2860

Nucleolar proteome dynamics

Spatiotemporal quantification of subcellular ATP levels in a single HeLa cell during changes in morphology.

The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains.

ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling

The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels

Universal sample preparation method for proteome analysis

Andromeda: a peptide search engine integrated into the MaxQuant environment

GO::TermFinder--open source software for accessing Gene Ontology information and finding significantly enriched Gene Ontology terms associated with a list of genes

P31

scholarly article

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10.7554/ELIFE.35224

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English

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Daniel L Weeks

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2018-07-17T00:00:00Z

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P698

30015615

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6050040

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