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Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate a...

Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate a...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_4eb1898661044a6890c551d0a05b51d3

Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate

About this item

Full title

Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2021-10, Vol.12 (1), p.5808-5808, Article 5808

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The nucleotides diadenosine triphosphate (Ap
3
A) and diadenosine tetraphosphate (Ap
4
A) are formed in prokaryotic and eukaryotic cells. Since their concentrations increase significantly upon cellular stress, they are considered to be alarmones triggering stress adaptive processes. However, their cellular roles remain elusive. To eluci...

Alternative Titles

Full title

Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_4eb1898661044a6890c551d0a05b51d3

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_4eb1898661044a6890c551d0a05b51d3

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-021-26075-4

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