Open Biology is celebrating five years of publishing high impact open access biology at the molecular and cellular level. As we commemorate this milestone, we take a look back at the journal's achievments over the past five years.
We would like to thank our authors, referees, Editorial Board members, and readers for their unwavering support over the past five years. We look forward to continuing the journey with you!
To celebrate Open Biology turning five years old, our editors each highlight the story of a paper that has had a significant impact on cell biology research. The selected papers represent many of the subject areas covered by the journal.
Labile disulfide bonds are common at the leucocyte cell surface - Clive Metcalfe, Peter Cresswell, Laura Ciaccia, Benjamin Thomas and A. Neil Barclay (2011)
Inside a protein, disulfide bonds contribute to structural integrity, whereas at the surface they can influence molecular function by being ‘redox-labile’. Metcalfe et al developed a proteomics-based method, with which they systematically screened the surface proteins of leukocytes for the presence of such labile disulfide bonds. This method is a valuable addition to the immunologist’s tool-box.
PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
Chandana Kondapalli, Agne Kazlauskaite, Ning Zhang, Helen I. Woodroof, David G. Campbell, Robert Gourlay, Lynn Burchell, Helen Walden, Thomas J. Macartney, Maria Deak, Axel Knebel, Dario R. Alessi and Miratul M. K. Muqit (2012)
In recent years several genes have been found to cause Parkinson’s disease but the function of these genes is still under question. This article describes the discovery of the function and target for the one of these genes called PINK1. PINK1 is a special enzyme called a kinase and the authors found that it targets another Parkinson’s linked protein called Parkin. The findings reveal that PINK1 switches on the function of Parkin and suggests that failure to switch Parkin on leads to Parkinson’s disease. The work importantly indicated that designing drugs to switch Parkin on may have the potential to treat Parkinson’s disease patients.
TRPC3 and TRPC6 are essential for normal mechanotransduction in subsets of sensory neurons and cochlear hair cells - Kathryn Quick, Jing Zhao, Niels Eijkelkamp, John E. Linley, Francois Rugiero, James J. Cox, Ramin Raouf, Martine Gringhuis, Jane E. Sexton, Joel Abramowitz, Ruth Taylor, Andy Forge, Jonathan Ashmore, Nerissa Kirkwood, Corné J. Kros, Guy P. Richardson, Marc Freichel, Veit Flockerzi, Lutz Birnbaumer, John N. Wood (2012)
When the channel proteins, TRPC3 and TRP6, are genetically knocked out, mice lose touch sensitivity in the skin and the ability to detect high frequency sound in the cochlear. The paper by Quick et al showed that re-expression of these same two proteins causes the cells to become mechanosensitive indicating that these two proteins transduce mechanical pressure in both touch sensation and hearing. This study makes the link, for the first time, that common proteins underlie touch and hearing.
The structure of Plasmodium yoelii merozoite surface protein 119 and implications for malaria vaccine design - Rachel D. Curd, Berry Birdsall, Madhusudan Kadekoppala, Solabomi A. Ogun, Geoffrey Kelly and Anthony A. Holder (2014)
Malaria is caused by a parasite, and a vaccine to prevent the disease may be based on merozoite surface protein 1 located on the form of this parasite in the blood. Using a mouse model, this paper showed that antibodies providing protection against malaria may bind to MSP1 and binding can be disrupted by structural changes to MSP1. Importantly, a change to one small part of MSP1 abolished protection against malaria following vaccination with the protein, highlighting the crucial role of this region as a target of the protective response that will need to be induced by an MSP1-based malaria vaccine.
A decision underlies phototaxis in an insect - Axel E. Gorostiza, Julien Colomb and Björn Brembs (2016)
Flies, such as Drosophila, move towards a source of light exhibiting a behaviour known as phototaxis. This strong behavioural response is commonly used in the design of behavioural tests in many genetic studies and has long been viewed as a hard-wired preference. The paper by Axel et al provides compelling new evidence that overturns this view. They show in walking flies that the phototaxic response is dependent on the ability to fly. If flight is compromised temporarily, the flies’ preference for light is reversed. Photopreference, they show, is differentially controlled by separate dopamine and octopamine neural circuits. The work indicates that active decision-making is involved even in behaviours that appear to be innate. [sign up for alerts]
"We published one paper this year with Open Biology and were so impressed by the professional and rapid assessment of our manuscript that we decided to submit a second paper just a few months later. In both cases, our experiences were extremely positive and we sincerely believe that Open Biology is destined to become one of the most read and interesting biology journals. It simply ticks all the boxes: fast and fair review process handled by highly qualified scientific editors, efficient and friendly editorial staff, very quick turnaround time from submission to publication, full open access at a reasonable fee, and useful and informative metrics after publication. All this from the oldest scientific publisher in the world! We strongly encourage other scientists to try Open Biology; you will not be disappointed."
Dr. Pier Paolo D'Avino, University of Cambridge
A journal run by scientists for scientists
"Over the past five years, Open Biology has gone from strength to strength and continues to demonstrate the Society’s support for open access publishing and bring attention to the dynamic field of cell biology.
Run by scientists for scientists, it offers a valuable opportunity for all levels of researchers to participate more actively in the publishing process and make their findings widely accessible. I look forward to the journal's continued success."
- Sir Venki Ramakrishnan, Royal Society President