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Click-chemistry approach to study mycoloylated proteins: Evidence for PorB and PorC porins mycoloyla...

Click-chemistry approach to study mycoloylated proteins: Evidence for PorB and PorC porins mycoloyla...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1868609276

Click-chemistry approach to study mycoloylated proteins: Evidence for PorB and PorC porins mycoloylation in Corynebacterium glutamicum

About this item

Full title

Click-chemistry approach to study mycoloylated proteins: Evidence for PorB and PorC porins mycoloylation in Corynebacterium glutamicum

Publisher

United States: Public Library of Science

Journal title

PloS one, 2017-02, Vol.12 (2), p.e0171955-e0171955

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Protein mycoloylation is a recently identified, new form of protein acylation. This post-translational modification consists in the covalent attachment of mycolic acids residues to serine. Mycolic acids are long chain, α-branched, β-hydroxylated fatty acids that are exclusively found in the cell envelope of Corynebacteriales, a bacterial order that...

Alternative Titles

Full title

Click-chemistry approach to study mycoloylated proteins: Evidence for PorB and PorC porins mycoloylation in Corynebacterium glutamicum

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1868609276

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1868609276

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0171955

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