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Structural and Histone Binding Ability Characterizations of Human PWWP Domains

Overview of attention for article published in PLOS ONE, June 2011
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Title
Structural and Histone Binding Ability Characterizations of Human PWWP Domains
Published in
PLOS ONE, June 2011
DOI 10.1371/journal.pone.0018919
Pubmed ID
Authors

Hong Wu, Hong Zeng, Robert Lam, Wolfram Tempel, Maria F. Amaya, Chao Xu, Ludmila Dombrovski, Wei Qiu, Yanming Wang, Jinrong Min

Abstract

The PWWP domain was first identified as a structural motif of 100-130 amino acids in the WHSC1 protein and predicted to be a protein-protein interaction domain. It belongs to the Tudor domain 'Royal Family', which consists of Tudor, chromodomain, MBT and PWWP domains. While Tudor, chromodomain and MBT domains have long been known to bind methylated histones, PWWP was shown to exhibit histone binding ability only until recently.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 184 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 3 2%
United States 2 1%
Denmark 2 1%
Netherlands 1 <1%
Canada 1 <1%
Unknown 175 95%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 55 30%
Researcher 30 16%
Student > Master 19 10%
Student > Bachelor 16 9%
Student > Doctoral Student 10 5%
Other 24 13%
Unknown 30 16%
Readers by discipline Count As %
Agricultural and Biological Sciences 57 31%
Biochemistry, Genetics and Molecular Biology 48 26%
Chemistry 22 12%
Medicine and Dentistry 7 4%
Pharmacology, Toxicology and Pharmaceutical Science 5 3%
Other 13 7%
Unknown 32 17%