Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive Plus
ORGANISM(S): Bordetella Pertussis (strain Tohama I / Atcc Baa-589 / Nctc 13251) Bacteria
DISEASE(S): Pertussis
SUBMITTER: Ivo Fabrik
LAB HEAD: Prof. Peter Sebo, PhD.
PROVIDER: PXD016384 | Pride | 2020-07-19
REPOSITORIES: Pride
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20190726_IF027_WT_1_AcK_01.raw | Raw | |||
20190726_IF027_WT_1_WCLD_01.raw | Raw | |||
20190726_IF027_WT_2_AcK_01.raw | Raw | |||
20190726_IF027_WT_2_WCLD_01.raw | Raw | |||
20190726_IF027_WT_4_AcK_01.raw | Raw |
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Journal of proteome research 20200731 9
Post-translational modifications of proteins enable swift physiological adaptation of cells to altered growth conditions and stress. Aside from protein phosphorylation, acetylation on ε-amino groups of lysine residues (<i>N</i>-ε-lysine acetylation) represents another important post-translational modification of proteins. For many bacterial pathogens, including the whooping cough agent <i>Bordetella pertussis</i>, the role and extent of protein acetylation remain to be defined. We expressed in < ...[more]