Molecular dynamic simulations suggest that metabolite-induced post-translational modifications alter the behavior of the fibrinogen coiled-coil domain

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023736%3A_____%2F21%3A00013234" target="_blank" >RIV/00023736:_____/21:00013234 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.3390/metabo11050307" target="_blank" >https://doi.org/10.3390/metabo11050307</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/metabo11050307" target="_blank" >10.3390/metabo11050307</a>

Result language
angličtina
Original language name
Molecular dynamic simulations suggest that metabolite-induced post-translational modifications alter the behavior of the fibrinogen coiled-coil domain
Original language description
Fibrinogen is an abundant blood plasma protein that, inter alia, participates in blood coagulation. It polymerizes to form a fibrin clot that is among the major components of the thrombus. Fibrinogen reactions with various reactive metabolites may induce post‐translational modifications (PTMs) into the protein structure that affect the architecture and properties of fibrin clots. We reviewed the previous literature to find the positions of PTMs of fibrinogen.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30205 - Hematology

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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