p47phox molecular activation for assembly of the neutrophil NADPH oxidase complex
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F10%3A00354237" target="_blank" >RIV/61388971:_____/10:00354237 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
p47phox molecular activation for assembly of the neutrophil NADPH oxidase complex
Original language description
Paper describes mechanism of molecular activation of p47phox, one part of the NADPH oxidase complex. P47phox is a modular multidomain protein that is known to undergo process of activation via phosphorylation. Due to the modular nature and its size it isimpossible to solve the structure of autoinhibited and activated form by NMR or crystallography. Therefore we used hydrogen/deuterium exchange coupled to mass spectrometry to describe the structural differences between the two forms. We show that the protein undergoes opening upon activation and described the key regions involved in the interaction in the auto-inhibited state
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Biological Chemistry
ISSN
0021-9258
e-ISSN
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Volume of the periodical
285
Issue of the periodical within the volume
37
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
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UT code for WoS article
000281594000063
EID of the result in the Scopus database
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