PLoS ONE (eISSN-1932-6203) is an international, peer-reviewed, open-access, online publication from the Public Library of Science (PLoS). PLoS ONE welcomes reports on primary research from any scientific discipline. PLoS ONE will launch later in 2006.
PLoS ONE is run as a partnership between its in-house PLoS staff and international Advisory and Editorial Boards, ensuring fast, fair, and professional peer review. To contact the Managing Editor, Christopher Surridge, or the Publications Assistant, Lindsay King, please e-mail plosone [at] plos.org.
PLoS ONE Now Accepting Submissions
Save 40% on the Publication Fee
September 13, 2006
Dear Colleague,
PLoS ONE, the open-access online forum for the publication of primary research from all areas of science and medicine, wants to publish your work.
You can send your research to us today and be one of the very first authors to publish in PLoS ONE, a publication that even before its launch has been described in the blogosphere as "nothing short of a revolution in scientific communication" and "a journal, but not as we know it".
Publishing in PLoS ONE...
... is community led
This will be your forum―by the people, for the people. It's your chance to speed up scientific progress by participating in online discussion and debate of the research that you feel passionate about.
... is about freedom for the author
You get as much space as you need to tell your story.
Your work is freely accessible to anyone anywhere with an internet connection
You retain your copyright
... is affordable
The publication fee is US$1250 per paper. But for papers submitted between now and launch, it's only US$750.
... and is rewarding
Submit your work
Save 40% on the post-launch publication fee.
Sign up for content alerts
First 200 get a free laser pointer.
The Dark Side of EGFP: Defective Polyubiquitination
http://www.plosone.org/article/fetchArticle.action?articleURI=info%3Adoi%2F10.1371%2Fjournal.pone.0000054
Enhanced Green Fluorescent Protein (EGFP) is the most commonly used live cell reporter despite a number of conflicting reports that it can affect cell physiology. Thus far, the precise mechanism of GFP-associated defects remained unclear. Here we demonstrate that EGFP and EGFP fusion proteins inhibit polyubiquitination, a posttranslational modification that controls a wide variety of cellular processes, like activation of kinase signalling or protein degradation by the proteasome. As a consequence, the NF-κB and JNK signalling pathways are less responsive to activation, and the stability of the p53 tumour suppressor is enhanced in cell lines and in vivo. In view of the emerging role of polyubiquitination in the regulation of numerous cellular processes, the use of EGFP as a live cell reporter should be carefully considered.
Prion Protein in Milk
http://www.plosone.org/article/fetchArticle.action?articleURI=info%3Adoi%2F10.1371%2Fjournal.pone.0000071
Background
Prions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmission is possible. The low concentration of the proteinaceous agent in body fluids and its long incubation time complicate epidemiologic analysis and estimation of spreading and thus the risk of human infection. This situation is particularly unsatisfactory for food and pharmaceutical industries, given the lack of sensitive tools for monitoring the infectious agent.
Methodology/Principal Findings
We have developed an adsorption matrix, Alicon PrioTrap?, which binds with high affinity and specificity to prion proteins. Thus we were able to identify prion protein (PrPC)?the precursor of prions (PrPSc)?in milk from humans, cows, sheep, and goats. The absolute amount of PrPC differs between the species (from ?g/l range in sheep to ng/l range in human milk). PrPC is also found in homogenised and pasteurised off-the-shelf milk, and even ultrahigh temperature treatment only partially diminishes endogenous PrPC concentration.
Conclusions/Significance
In view of a recent study showing evidence of prion replication occurring in the mammary gland of scrapie infected sheep suffering from mastitis, the appearance of PrPC in milk implies the possibility that milk of TSE-infected animals serves as source for PrPSc.
PLoS ONE beta, a new way of communicating peer-reviewed science and medicine, is now launched.
Before your first visit, I want to let you know about the inherent challenges of this project and the philosophy that compels PLoS to confront them.
We want to speed up scientific progress and believe that scientific debate is as important as the investigation itself. PLoS ONE is a forum where research can be both shared and commented upon - we are launching it as a beta website so that the whole scientific community can help us develop the features.
What makes the site beta? Not the content, which features peer-reviewed research from hundreds of authors across a diverse range of scientific disciplines. It's the additional tools and functionality surrounding these papers that will be continually refined and developed in response to user feedback.
It is this union of continually evolving user tools provided by the Topaz publishing platform and extensive content that will make PLoS ONE a success.
The first beta release of PLoS ONE features tools that allow users to annotate articles and participate in discussion threads. Our goal is to spark lively discussion online and we'd like to invite you to participate. Future updates will include user ratings for both papers and the comments made about them, personalized content alerts and much more.
We will be watching with interest to see how our new platform and software responds to high volumes of traffic and encourage you to give your feedback on your first experience via the site itself.
To stay involved:
Sign up for content alerts
First 100 people receive a PLoS ONE t-shirt (first come, first served).
Submit your work
Visit the PLoS ONE Journal Management System to upload your article.
Thanks so much for your early support. It really has made the world of difference to know that you and more than 4,000 of your peers have been behind us from the start.
E-Cadherin-Coated Plates Maintain Pluripotent ES Cells without Colony Formation
http://www.plosone.org/article/fetchArticle.action?articleURI=info%3Adoi%2F10.1371%2Fjournal.pone.0000015
Embryonic stem (ES) cells cultured on gelatin-coated plates or feeder layers form tight aggregated colonies by the E-cadherin-mediated cell-cell adhesions. Here we show that murine ES cells do not make cell-cell contacts or form colonies when cultured on the plate coated with a fusion protein of E-cadherin and IgG Fc domain. The cells in culture retain all ES cell features including pluripotency to differentiate into cells of all three germ layers and germ-line transmission after extended culture. Furthermore, they show a higher proliferative ability, lower dependency on LIF, and higher transfection efficiency than colony-forming conditions. Our results suggest that aggregated colony formation might inhibit diffusion of soluble factors and increase cell-cell communication, which may result in a heterogeneous environment within and between surrounding cells of the colony. This method should enable more efficient and scalable culture of ES cells, an important step towards the clinical application of these cells.
The HA tag is cleaved and loses immunoreactivity during apoptosis
Nature Methods - 4, 107 - 108 (2007)
http://www.nature.com/nmeth/journal/v4/n2/full/nmeth0207-107.html