id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-298736-9bvyp21d	Gerold, Gisa	Decoding protein networks during virus entry by quantitative proteomics	2016-06-15		.txt	text/plain	12159	626	38	In the past decade mass spectrometry based proteomics methods have reached sensitivities and high throughput compatibilities of genomics methods and now allow the reliable quantitation of proteins in complex samples from limited material. Since then technological developments like antibody based affinity purification (AP), mass spectrometry (MS) of proteins, DNA mediated transformation and molecular cloning led to the discovery of dozens of receptors for human pathogenic viruses (Fig. 1) . While transcriptomics can reveal long-term alterations of the cellular state, virus entry usually occurs within minutes and typically relies on rapid changes of protein conformation, localization, interactions and post-translational modifications (PTM). Of note, high resolution proteomics can not only reveal transient interactions of VAP with enzymes, but also has the potential to identify proteolytic cleavage sites and redox modifications in VAPs. It is conceivable that virus induced protein interactions during entry not only serve to promote the virus uptake pathway, but can also help cloak viruses and lead to immune evasion.	./cache/cord-298736-9bvyp21d.txt	./txt/cord-298736-9bvyp21d.txt