About: Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods
Creator	Ban, Nenad Bieri, Philipp Damoc, Eugen Franc, Vojtech Itten, Martin Makarov, Alexander Tamara, Sem Fort, Kyle Heck, Albert Van De Waterbeemd, Michiel
Source	PMC
abstract	Biomolecular mass spectrometry has matured strongly over the past decades and has now reached a stage where it can provide deep insights into the structure and composition of large cellular assemblies. Here, we describe a three-tiered hybrid mass spectrometry approach that enables the dissection of macromolecular complexes in order to complement structural studies. To demonstrate the capabilities of the approach, we investigate ribosomes, large ribonucleoprotein particles consisting of a multitude of protein and RNA subunits. We identify sites of sequence processing, protein post-translational modifications, and the assembly and stoichiometry of individual ribosomal proteins in four distinct ribosomal particles of bacterial, plant and human origin. Amongst others, we report extensive cysteine methylation in the zinc finger domain of the human S27 protein, the heptameric stoichiometry of the chloroplastic stalk complex, the heterogeneous composition of human 40S ribosomal subunits and their association to the CrPV, and HCV internal ribosome entry site RNAs.
has issue date	2018-06-27(xsd:dateTime)
bibo:doi	10.1038/s41467-018-04853-x
bibo:pmid	29950687
has license	cc-by
sha1sum (hex)	5278efe68b31540a1a68ecf36528c7dd4a5fa14d
schema:url	https://doi.org/10.1038/s41467-018-04853-x
resource representing a document's title	Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods
has PubMed Central identifier	PMC6021402
has PubMed identifier	29950687
schema:publication	Nat Commun
resource representing a document's body	covid:5278efe68b31540a1a68ecf36528c7dd4a5fa14d#body_text
is schema:about of	named entity 'PROVIDE' named entity 'CYSTEINE' named entity 'HERE' named entity 'ORDER' named entity 'COMPLEX' named entity 'PARTICLES' named entity 'LARGE' named entity 'STALK' named entity 'STAGE' named entity 'PARTICLES' named entity 'DISSECTION' named entity 'RIBONUCLEOPROTEIN' named entity 'RIBOSOMAL' named entity 'STOICHIOMETRY' named entity 'DESCRIBE' named entity 'RIBOSOMAL' named entity 'USING' named entity 'LIFE' named entity 'MASS SPECTROMETRY' named entity 'METHODS' named entity 'HYBRID' named entity 'INSIGHTS' named entity 'WHERE' named entity 'RIBOSOMAL PROTEINS' named entity 'STUDIES' named entity 'MULTITUDE' named entity 'EXTENSIVE' named entity 'IDENTIFY' named entity 'MASS SPECTROMETRY' named entity 'DEEP' named entity 'RIBOSOMES' named entity 'METHYLATION' named entity 'THEIR' named entity 'ASSOCIATION' named entity 'CELLULAR' named entity 'REPORT' named entity 'HETEROGENEOUS' named entity 'S27' named entity '40S' named entity 'BACTERIAL' named entity 'HUMAN ORIGIN' named entity 'COMPLEMENT' named entity 'HUMAN' named entity 'HCV' named entity 'INVESTIGATE' named entity 'PROTEIN' named entity 'COMPOSITION' named entity 'PLANT' named entity 'ZINC FINGER DOMAIN' named entity 'STRUCTURE' named entity 'CRPV' named entity 'STRUCTURAL' named entity 'ASSEMBLY' named entity 'INDIVIDUAL' named entity 'APPROACH' named entity 'ENABLES' named entity 'PROTEIN ' named entity 'PROTEIN POST-TRANSLATIONAL MODIFICATIONS' named entity 'COMPLEXES' named entity 'DISSECTING' named entity 'RNA' named entity 'SITES' named entity 'SEQUENCE PROCESSING' named entity 'HYBRID' named entity 'INTERNAL RIBOSOME ENTRY SITE' named entity 'DISTINCT' named entity 'ADVANCED' named entity 'PAST' named entity 'mass spectrometry' named entity 'protein' named entity '40S' named entity 'CrPV'

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