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Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1

Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_umu_166031

Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1

About this item

Full title

Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2011-01, Vol.469 (7330), p.419-423

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Human β-defensin 1 shows its true colours
Defensins are key effector molecules of innate immunity, protecting the host from infectious microbes and shaping the composition of the microbiota at mucosal surfaces. Human β-defensin 1 (hBD-1) is one of the most prominent peptides of its class and is expressed by virtually all human epithelial sites,...

Alternative Titles

Full title

Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_swepub_primary_oai_DiVA_org_umu_166031

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_umu_166031

Other Identifiers

ISSN

0028-0836,1476-4687

E-ISSN

1476-4687

DOI

10.1038/nature09674