The Membrane-Bound Structure and Topology of a Human α-Defensin Indicate a Dimer Pore Mechanism for Membrane Disruption-Reference-Cited by-同舟云学术

The Membrane-Bound Structure and Topology of a Human α-Defensin Indicate a Dimer Pore Mechanism for Membrane Disruption

Published:2010-10-26 Issue:45 Volume:49 Page:9770-9782
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Zhang Yuan¹,Lu Wuyuan²,Hong Mei¹

Affiliation:

1. Department of Chemistry, Iowa State University, Ames, Iowa 50011, United States

2. Institute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi101512j

Reference75 articles.

1. Defensins: antimicrobial peptides of innate immunity

2. Reconstruction of the Conserved β-Bulge in Mammalian Defensins Using d-Amino Acids

3. Primary structures of three human neutrophil defensins.

4. Antibiotic proteins of human polymorphonuclear leukocytes.

5. Defensins. Natural peptide antibiotics of human neutrophils.

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