How open science helps researchers succeed
- National Autonomous University of Mexico, Mexico
- National Institutes of Health, United States
- University of California, Davis, United States
- Laura and John Arnold Foundation, United States
- BioMed Central, United Kingdom
- CrossRef, United Kingdom
- University of Texas at Austin, United States
- Center for Open Science, United States
- University of California, Berkeley, United States
- Mozilla Foundation, United States
- Gesmer Updegrove LLP, United States
- Washington State University, United States
Abstract
Open access, open data, open source, and other open scholarship practices are growing in popularity and necessity. However, widespread adoption of these practices has not yet been achieved. One reason is that researchers are uncertain about how sharing their work will affect their careers. We review literature demonstrating that open research is associated with increases in citations, media attention, potential collaborators, job opportunities, and funding opportunities. These findings are evidence that open research practices bring significant benefits to researchers relative to more traditional closed practices.
Article and author information
Author details
Reviewing Editor
- Peter Rodgers, eLife, United Kingdom
Publication history
- Received: April 8, 2016
- Accepted: July 4, 2016
- Accepted Manuscript published: July 7, 2016 (version 1)
- Version of Record published: July 29, 2016 (version 2)
Copyright
© 2016, McKiernan et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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How open science helps researchers succeed
eLife 5:e16800.
https://doi.org/10.7554/eLife.16800
Further reading
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Researchers can benefit from making their research findings freely available online.
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- Biochemistry and Chemical Biology
- Cell Biology
Dystroglycan (DG) requires extensive post-translational processing and O-glycosylation to function as a receptor for extracellular matrix (ECM) proteins containing laminin-G-like (LG) domains. Matriglycan is an elongated polysaccharide of alternating xylose (Xyl) and glucuronic acid (GlcA) that binds with high-affinity to ECM proteins with LG-domains and is uniquely synthesized on α-dystroglycan (α-DG) by like-acetylglucosaminyltransferase-1 (LARGE1). Defects in the post-translational processing or O-glycosylation of α-DG that result in a shorter form of matriglycan reduce the size of α-DG and decrease laminin binding, leading to various forms of muscular dystrophy. Previously, we demonstrated that Protein O-Mannose Kinase (POMK) is required for LARGE1 to generate full-length matriglycan on α-DG (~150-250 kDa) (Walimbe et al., 2020). Here, we show that LARGE1 can only synthesize a short, non-elongated form of matriglycan in mouse skeletal muscle that lacks the DG N-terminus (α-DGN), resulting in a ~100-125 kDa α-DG. This smaller form of α-DG binds laminin and maintains specific force but does not prevent muscle pathophysiology, including reduced force production after eccentric contractions or abnormalities in the neuromuscular junctions. Collectively, our study demonstrates that α-DGN, like POMK, is required for LARGE1 to extend matriglycan to its full mature length on α-DG and thus prevent muscle pathophysiology.
