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Rat ceruloplasmin : A new labile copper binding site and zinc/copper mosaic. / Samygina, V. R.; Sokolov, A. V.; Bourenkov, G.; Schneider, T. R.; Anashkin, V. A.; Kozlov, S. O.; Kolmakov, N. N.; Vasilyev, V. B.

в: Metallomics, Том 9, № 12, 01.12.2017, стр. 1828-1838.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Samygina, VR, Sokolov, AV, Bourenkov, G, Schneider, TR, Anashkin, VA, Kozlov, SO, Kolmakov, NN & Vasilyev, VB 2017, 'Rat ceruloplasmin: A new labile copper binding site and zinc/copper mosaic', Metallomics, Том. 9, № 12, стр. 1828-1838. https://doi.org/10.1039/c7mt00157f

APA

Samygina, V. R., Sokolov, A. V., Bourenkov, G., Schneider, T. R., Anashkin, V. A., Kozlov, S. O., Kolmakov, N. N., & Vasilyev, V. B. (2017). Rat ceruloplasmin: A new labile copper binding site and zinc/copper mosaic. Metallomics, 9(12), 1828-1838. https://doi.org/10.1039/c7mt00157f

Vancouver

Samygina VR, Sokolov AV, Bourenkov G, Schneider TR, Anashkin VA, Kozlov SO и пр. Rat ceruloplasmin: A new labile copper binding site and zinc/copper mosaic. Metallomics. 2017 Дек. 1;9(12):1828-1838. https://doi.org/10.1039/c7mt00157f

Author

Samygina, V. R. ; Sokolov, A. V. ; Bourenkov, G. ; Schneider, T. R. ; Anashkin, V. A. ; Kozlov, S. O. ; Kolmakov, N. N. ; Vasilyev, V. B. / Rat ceruloplasmin : A new labile copper binding site and zinc/copper mosaic. в: Metallomics. 2017 ; Том 9, № 12. стр. 1828-1838.

BibTeX

@article{fe5e1c8d2d634808b31611ae48608b90,
title = "Rat ceruloplasmin: A new labile copper binding site and zinc/copper mosaic",
abstract = "Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acute-phase protein and a free radical scavenger. The structural organization of Cp causes its sensitivity to proteolysis and ROS (reactive oxygen species), which can alter some of the important Cp functions. Elucidation of the orthorhombic crystal structure of rat Cp at 2.3 {\AA} resolution revealed the basis for stronger resistance of rat Cp to proteolysis and a new labile copper binding site. The presence of this site appears as a very rare and distinctive feature of rat Cp as was shown by sequence alignment of ceruloplasmin, hephaestin and zyklopen in the Deuterostomia taxonomic group. The trigonal crystal form of rat Cp at 3.2 {\AA} demonstrates unexpected partial substitution of copper by zinc.",
author = "Samygina, {V. R.} and Sokolov, {A. V.} and G. Bourenkov and Schneider, {T. R.} and Anashkin, {V. A.} and Kozlov, {S. O.} and Kolmakov, {N. N.} and Vasilyev, {V. B.}",
year = "2017",
month = dec,
day = "1",
doi = "10.1039/c7mt00157f",
language = "English",
volume = "9",
pages = "1828--1838",
journal = "Metallomics",
issn = "1756-5901",
publisher = "Royal Society of Chemistry",
number = "12",

}

RIS

TY - JOUR

T1 - Rat ceruloplasmin

T2 - A new labile copper binding site and zinc/copper mosaic

AU - Samygina, V. R.

AU - Sokolov, A. V.

AU - Bourenkov, G.

AU - Schneider, T. R.

AU - Anashkin, V. A.

AU - Kozlov, S. O.

AU - Kolmakov, N. N.

AU - Vasilyev, V. B.

PY - 2017/12/1

Y1 - 2017/12/1

N2 - Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acute-phase protein and a free radical scavenger. The structural organization of Cp causes its sensitivity to proteolysis and ROS (reactive oxygen species), which can alter some of the important Cp functions. Elucidation of the orthorhombic crystal structure of rat Cp at 2.3 Å resolution revealed the basis for stronger resistance of rat Cp to proteolysis and a new labile copper binding site. The presence of this site appears as a very rare and distinctive feature of rat Cp as was shown by sequence alignment of ceruloplasmin, hephaestin and zyklopen in the Deuterostomia taxonomic group. The trigonal crystal form of rat Cp at 3.2 Å demonstrates unexpected partial substitution of copper by zinc.

AB - Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acute-phase protein and a free radical scavenger. The structural organization of Cp causes its sensitivity to proteolysis and ROS (reactive oxygen species), which can alter some of the important Cp functions. Elucidation of the orthorhombic crystal structure of rat Cp at 2.3 Å resolution revealed the basis for stronger resistance of rat Cp to proteolysis and a new labile copper binding site. The presence of this site appears as a very rare and distinctive feature of rat Cp as was shown by sequence alignment of ceruloplasmin, hephaestin and zyklopen in the Deuterostomia taxonomic group. The trigonal crystal form of rat Cp at 3.2 Å demonstrates unexpected partial substitution of copper by zinc.

UR - http://www.scopus.com/inward/record.url?scp=85038350445&partnerID=8YFLogxK

U2 - 10.1039/c7mt00157f

DO - 10.1039/c7mt00157f

M3 - Article

C2 - 29177316

AN - SCOPUS:85038350445

VL - 9

SP - 1828

EP - 1838

JO - Metallomics

JF - Metallomics

SN - 1756-5901

IS - 12

ER -

ID: 42247651