Literature DB >> 8528769

Structure, function, and membrane integration of defensins.

S H White1, W C Wimley, M E Selsted.   

Abstract

Defensins comprise a structural class of small cationic peptides that exert broad-spectrum antimicrobial activities through membrane permeabilization. Their predominantly beta-sheet structure, stabilized by three disulfide bonds, distinguishes them from other antimicrobial peptides which typically form amphiphilic helices. Defensins bind to membranes electrostatically and subsequently form apparently multimeric pores. Recent structural and biophysical studies are beginning to provide insights into the process of permeabilization.

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Year:  1995        PMID: 8528769     DOI: 10.1016/0959-440x(95)80038-7

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  107 in total

1.  The mouse secretome: functional classification of the proteins secreted into the extracellular environment.

Authors:  Sean M Grimmond; Kevin C Miranda; Zheng Yuan; Melissa J Davis; David A Hume; Ken Yagi; Naoko Tominaga; Hidemasa Bono; Yoshihide Hayashizaki; Yasushi Okazaki; Rohan D Teasdale
Journal:  Genome Res       Date:  2003-06       Impact factor: 9.043

Review 2.  Mammalian antibiotic peptides.

Authors:  P Síma; I Trebichavský; K Sigler
Journal:  Folia Microbiol (Praha)       Date:  2003       Impact factor: 2.099

3.  Multidimensional signatures in antimicrobial peptides.

Authors:  Nannette Y Yount; Michael R Yeaman
Journal:  Proc Natl Acad Sci U S A       Date:  2004-04-26       Impact factor: 11.205

4.  High-throughput discovery of broad-spectrum peptide antibiotics.

Authors:  Ramesh Rathinakumar; William C Wimley
Journal:  FASEB J       Date:  2010-04-21       Impact factor: 5.191

5.  Diversity in antistaphylococcal mechanisms among membrane-targeting antimicrobial peptides.

Authors:  S P Koo; A S Bayer; M R Yeaman
Journal:  Infect Immun       Date:  2001-08       Impact factor: 3.441

6.  The α-defensin salt-bridge induces backbone stability to facilitate folding and confer proteolytic resistance.

Authors:  Håkan S Andersson; Sharel M Figueredo; Linda M Haugaard-Kedström; Elina Bengtsson; Norelle L Daly; Xiaoqing Qu; David J Craik; André J Ouellette; K Johan Rosengren
Journal:  Amino Acids       Date:  2012-10       Impact factor: 3.520

7.  A molecular dynamics study of the bee venom melittin in aqueous solution, in methanol, and inserted in a phospholipid bilayer.

Authors:  Alice Glättli; Indira Chandrasekhar; Wilfred F van Gunsteren
Journal:  Eur Biophys J       Date:  2005-12-02       Impact factor: 1.733

8.  Rational combinatorial design of pore-forming beta-sheet peptides.

Authors:  Joshua M Rausch; Jessica R Marks; William C Wimley
Journal:  Proc Natl Acad Sci U S A       Date:  2005-07-14       Impact factor: 11.205

9.  Rattusin, an intestinal α-defensin-related peptide in rats with a unique cysteine spacing pattern and salt-insensitive antibacterial activities.

Authors:  Amar A Patil; Andre J Ouellette; Wuyuan Lu; Guolong Zhang
Journal:  Antimicrob Agents Chemother       Date:  2013-02-04       Impact factor: 5.191

10.  Role of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5.

Authors:  Sang-Ho Park; Hyung-Eun Kim; Chi-Man Kim; Hee-Jeong Yun; Eung-Chil Choi; Bong-Jin Lee
Journal:  Biochem J       Date:  2002-11-15       Impact factor: 3.857

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