Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Ivan Stambolic"'
Autor:
Danijela Apostolovic, Ivan Stambolic, Dragana Stanic-Vucinic, Jelena Vesic, Tanja Cirkovic Velickovic, Miloš Milčić
Publikováno v:
Food Chemistry
2S albumins of peanuts are seed storage proteins, highly homologous in structure and described as major elicitors of anaphylactic reactions to peanut (allergens Ara h 2 and Ara h 6). Epigallocatechin-3-gallate (EGCG) is the most biologically potent p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75156cf963e4267c40032227bc63152a
https://doi.org/10.1016/j.foodchem.2015.04.001
https://doi.org/10.1016/j.foodchem.2015.04.001
Publikováno v:
Physical chemistry chemical physics : PCCP. 19(17)
LOV (light-, oxygen- or voltage-sensitive) domains act as photosensory units of many prokaryotic and eukaryotic proteins. Upon blue light excitation they undergo a photocycle via the excited triplet state of their flavin chromophore yielding the flav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f5e9d0b77100d7563ce85cf718d9b68
https://pubmed.ncbi.nlm.nih.gov/28271102
https://pubmed.ncbi.nlm.nih.gov/28271102
Autor:
Miloš Milčić, Marina Atanaskovic-Markovic, Danijela Apostolovic, Miljan Simonović, Ivan Stambolic, Jana Ognjenovic, Jelena Vesic, Tanja Cirkovic Velickovic, Marija Stojadinovic
Publikováno v:
Food Chemistry
Polyphenols, the potent plant secondary metabolites, have beneficial effects on human health, but the mechanism(s) by which these effects are exerted is not well understood. Here, we present the detailed analysis of the interactions between the major
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1deebf8f67e4a3fe716fa4bfe8944331
https://doi.org/10.1016/j.foodchem.2014.05.005
https://doi.org/10.1016/j.foodchem.2014.05.005
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 82:2018-2040
Devising analysis tools for elucidating the regulatory mechanism of complex enzymes has been a challenging task for many decades. It generally requires the determination of the structural-dynamical information of protein solvent systems far from equi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3cce7bc285ffa2395240c39da57fb8de
https://doi.org/10.1002/prot.24556
https://doi.org/10.1002/prot.24556
Autor:
Sofija P. Sovilj, Vladislava M. Jovanović, Dalibor M. Stanković, Ivan Stambolic, Branka Petković, Dragan Manojlović, Miloš Milčić
Publikováno v:
Electrochimica Acta
The complexation reactions between octaazamacrocyclic ligand N,N',N '',N'"-tetrakis(2-pyridylmethyl)-1,4,8,11-tetraazacyclotetradecane (tpmc) and Co2+, Ni2+, Zn2+ and Cu2+ metal cations have been studied conductometrically in acetonitrile and aqueous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6511767e25049b135841274e8552d72
https://doi.org/10.1016/j.electacta.2012.11.100
https://doi.org/10.1016/j.electacta.2012.11.100
Publikováno v:
Proteins. 82(9)
Devising analysis tools for elucidating the regulatory mechanism of complex enzymes has been a challenging task for many decades. It generally requires the determination of the structural-dynamical information of protein solvent systems far from equi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::197bb84518e19627ccdaba2071bf67dd
https://pubmed.ncbi.nlm.nih.gov/24623633
https://pubmed.ncbi.nlm.nih.gov/24623633
Autor:
Ivan Stambolic, Matthias Ruckenbauer, Hans Lischka, Adelia J. A. Aquino, Mario Barbatti, Bernhard Sellner
Publikováno v:
The journal of physical chemistry. A. 114(33)
The internal conversion and hot ground-state dynamics of trans- and cis-azomethane starting in the S(1) state have been investigated by nonadiabatic ab initio surface hopping dynamics using MCSCF-GVB-CAS and MRCISD methods and by determining energy m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4779e161e2eda3db51900629276eecbc
https://pubmed.ncbi.nlm.nih.gov/20450202
https://pubmed.ncbi.nlm.nih.gov/20450202