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

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1.

Research article   Open Access Highly Accessed

Experience-dependent persistent expression of zif268 during rest is preserved in the aged dentate gyrus

Ali Gheidi, Erin Azzopardi, Allison A Adams, Diano F Marrone BMC Neuroscience 2013, 14:100 (13 September 2013)

Abstract | Full text | PDF | PubMed

2.

Research article   Open Access

Development of a case-mix funding system for adults with combined vision and hearing loss

Dawn M Guthrie, Jeffrey W Poss BMC Health Services Research 2013, 13:137 (15 April 2013)

Abstract | Full text | PDF | PubMed

3.

Research article   Open Access Highly Accessed

Auditory-motor adaptation to frequency-altered auditory feedback occurs when participants ignore feedback

Dwayne Keough, Colin Hawco, Jeffery A Jones BMC Neuroscience 2013, 14:25 (9 March 2013)

Abstract | Full text | PDF | PubMed

4.

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

5.

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.

6.

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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