Ontology type: schema:ScholarlyArticle
2014-01
AUTHORSMarija Brgles, Tihana Kurtović, Lidija Kovačič, Igor Križaj, Miloš Barut, Maja Lang Balija, Günter Allmaier, Martina Marchetti-Deschmann, Beata Halassy
ABSTRACTIn order to perform their function, proteins frequently interact with other proteins. Various methods are used to reveal protein interacting partners, and affinity chromatography is one of them. Snake venom is composed mostly of proteins, and various protein complexes in the venom have been found to exhibit higher toxicity levels than respective components separately. Complexes can modulate envenomation activity of a venom and/or potentiate its effect. Our previous data indicate that the most toxic components of the Vipera ammodytes ammodytes (Vaa) venom isolated so far-ammodytoxins (Atxs)-are contributing to the venom's toxicity only moderately; therefore, we aimed to explore whether they have some interacting partner(s) potentiating toxicity. For screening of possible interactions, immuno-affinity chromatography combined with identification by mass spectrometry was used. Various chemistries (epoxy, carbonyldiimidazole, ethylenediamine) as well as protein G functionality were used to immobilize antibodies on monolith support, a Convective Interaction Media disk. Monoliths have been demonstrated to better suit the separation of large biomolecules. Using such approach, several proteins were indicated as potential Atx-binding proteins. Among these, the interaction of Atxs with a Kunitz-type inhibitor was confirmed by far-Western dot-blot and surface plasmon resonance measurement. It can be concluded that affinity chromatography on monolithic columns combined with mass spectrometry identification is a successful approach for screening of protein interactions and it resulted with detection of the interaction of Atx with Kunitz-type inhibitor in Vaa venom for the first time. More... »
PAGES293-304
http://scigraph.springernature.com/pub.10.1007/s00216-013-7453-5
DOIhttp://dx.doi.org/10.1007/s00216-013-7453-5
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/24217948
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"name": "pubmed_id",
"type": "PropertyValue",
"value": [
"24217948"
]
},
{
"name": "nlm_unique_id",
"type": "PropertyValue",
"value": [
"101134327"
]
},
{
"name": "doi",
"type": "PropertyValue",
"value": [
"10.1007/s00216-013-7453-5"
]
},
{
"name": "dimensions_id",
"type": "PropertyValue",
"value": [
"pub.1046504211"
]
}
],
"sameAs": [
"https://doi.org/10.1007/s00216-013-7453-5",
"https://app.dimensions.ai/details/publication/pub.1046504211"
],
"sdDataset": "articles",
"sdDatePublished": "2019-04-10T17:32",
"sdLicense": "https://scigraph.springernature.com/explorer/license/",
"sdPublisher": {
"name": "Springer Nature - SN SciGraph project",
"type": "Organization"
},
"sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000001_0000000264/records_8672_00000515.jsonl",
"type": "ScholarlyArticle",
"url": "http://link.springer.com/10.1007%2Fs00216-013-7453-5"
}
]Download the RDF metadata as: json-ld nt turtle xml License info
JSON-LD is a popular format for linked data which is fully compatible with JSON.
curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/s00216-013-7453-5'
N-Triples is a line-based linked data format ideal for batch operations.
curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/s00216-013-7453-5'
Turtle is a human-readable linked data format.
curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/s00216-013-7453-5'
RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/s00216-013-7453-5'
This table displays all metadata directly associated to this object as RDF triples.
321 TRIPLES
21 PREDICATES
83 URIs
32 LITERALS
20 BLANK NODES