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Member - Wilfrid Laurier University Library

Wilfrid Laurier University Library Wilfrid Laurier University is a mid-sized Ontario university with a reputation for excellence in teaching, scholarship and research.

http://www.wlu.ca/

Research staff and students at Wilfrid Laurier University Library:

Do you realize that you can now publish in journals published by BioMed Central, Chemistry Central and SpringerOpen without directly paying any article-processing charges? Payment of your article-processing charges is covered by Wilfrid Laurier University Library's Prepay Membership. Read more information about publishing your articles with us.



Work published with BioMed Central, Chemistry Central and SpringerOpen by researchers at Wilfrid Laurier University Library

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1.

Research   Open Access

Public awareness of income-related health inequalities in Ontario, Canada

Ketan Shankardass, Aisha Lofters, Maritt Kirst, Carlos Quiñonez International Journal for Equity in Health 2012, 11:26 (21 May 2012)

Abstract | Full text | PDF | PubMed

2.

Methodology   Open Access

Reproducible hairy root transformation and spot-inoculation methods to study root symbioses of pea

Scott R Clemow, Lindsey Clairmont, Lene H Madsen, Frédérique C Guinel Plant Methods 2011, 7:46 (15 December 2011)

Abstract | Full text | PDF | PubMed | Cited on BioMed Central |  Editor’s summary

The authors describe a set of tools that should greatly facilitate investigations of both the mycorrhizal and rhizobial symbioses with pea. The tools include an improved transformation method and techniques for targeted inoculation of roots with the symbiont to enable the processes involved in establishing the symbiosis to be studied in more detail.

3.

Research article   Open Access Highly Accessed

The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains

Lynn GL Richardson, Masoud Jelokhani-Niaraki, Matthew D Smith BMC Biochemistry 2009, 10:35 (30 December 2009)

Abstract | Full text | PDF | PubMed |  Editor’s summary

The variable N-terminal acidic domains of the Toc159 chloroplast preprotein receptor family in Arabidopsis are intrinsically disordered, which may facilitate interactions with transit peptides, and explain how these receptors serve to import a wide variety of proteins into chloroplasts.

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