Browsing by Author "Bitter, Wilbert"

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    ProVision: A web based platform for rapid analysis of proteomics data processed by MaxQuant
    (2020-07) Gallant, James; Heunis, Tiaan; Sampson, Samantha Leigh; Bitter, Wilbert
    Proteomics is a powerful tool for protein expression analysis and is becoming more readily available to researchers through core facilities or specialised collaborations. However, one major bottleneck for routine implementation and accessibility of this technology to the wider scientific community is the complexity of data analysis. To this end, we have created ProVision, a free open-source web-based analytics platform that allows users to analyse data from two common proteomics relative quantification workflows, namely label-free and tandem mass tag-based experiments. Furthermore, ProVision allows the freedom to interface with the data analysis pipeline while maintaining a user-friendly environment and providing default parameters for fast statistical and exploratory data analysis. Finally, multiple customisable quality control, differential expression plots as well as enrichments and protein-protein interaction prediction can be generated online in one platform. Availability and implementation: Quick start and step-by-step tutorials as well as tutorial data is fully incorporated in the web application. This application is available online at https://provision.shinyapps.io/provision/ for free use. The source code is available at https://github.com/JamesGallant/ProVision under the GPL version 3.0 license.
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    Systematic genetic nomenclature for type VII secretion systems
    (Public Library of Science, 2009) Bitter, Wilbert; Houben, Edith N. G.; Bottai, Darria; Brodin, Priscille; Brown, Eric J.; Cox, Jeffery S.; Derbyshire, Keith; Fortune, Sarah M.; Gao, Lian-Yong; Liu, Jun; Van Pittius, Nicolaas C. Gey; Pym, Alexander S.; Rubin, Eric J.; Sherman, David R.; Cole, Stewart T.; Brosch, Roland
    Mycobacteria, such as the etiological agent of human tuberculosis, Mycobacterium tuberculosis, are protected by an impermeable cell envelope composed of an inner cytoplasmic membrane, a peptidoglycan layer, an arabinogalactan layer, and an outer membrane. This second membrane consists of covalently linked, tightly packed long-chain mycolic acids [1,2] and noncovalently bound shorter lipids involved in pathogenicity [3–5]. To ensure protein transport across this complex cell envelope, mycobacteria use various secretion pathways, such as the SecA1-mediated general secretory pathway [6,7], an alternative SecA2-operated pathway [8], a twin-arginine translocation system [9,10], and a specialized secretion pathway variously named ESAT-6-, SNM-, ESX-, or type VII secretion [11–16]. The latter pathway, hereafter referred to as type VII secretion (T7S), has recently become a large and competitive research topic that is closely linked to studies of host–pathogen interactions of M. tuberculosis [17] and other pathogenic mycobacteria [16]. Molecular details are just beginning to be revealed [18–22] showing that T7S systems are complex machineries with multiple components and multiple substrates. Despite their biological importance, there has been a lack of a clear naming policy for the components and substrates of these systems. As there are multiple paralogous T7S systems within the Mycobacteria and orthologous systems in related bacteria, we are concerned that, without a unified nomenclature system, a multitude of redundant and obscure gene names will be used that will inevitably lead to confusion and hinder future progress. In this opinion piece we will therefore propose and introduce a systematic nomenclature with guidelines for name selection of new components that will greatly facilitate communication and understanding in this rapidly developing field of research.