Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Józef Ba Tran"'
Publikováno v:
Cell Communication and Signaling, Vol 21, Iss 1, Pp 1-19 (2023)
Abstract Background Nucleobindin-2 (Nucb2) is a multidomain protein that, due to its structure, participates in many physiological processes. It was originally identified in several regions of the hypothalamus. However, more recent studies have redef
Externí odkaz:
https://doaj.org/article/97793ee850894980bc7cf3f6587558c0
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 19, p 11140 (2022)
The metal binding at protein–protein interfaces is still uncharted territory in intermolecular interactions. To date, only a few protein complexes binding Zn(II) in an intermolecular manner have been deeply investigated. The most notable example of
Externí odkaz:
https://doaj.org/article/2263576df960470db44508ad6938d95d
Autor:
Marek Łuczkowski, Michał Padjasek, Józef Ba Tran, Lars Hemmingsen, Olga Kerber, Jelena Habjanič, Eva Freisinger, Artur Krężel
Publikováno v:
Chemistry – A European Journal. 28
Autor:
Marek Łuczkowski, Michał Padjasek, Józef Ba Tran, Lars Hemmingsen, Olga Kerber, Jelena Habjanič, Eva Freisinger, Artur Krężel
Publikováno v:
Luczkowski, M, Padjasek, M, Tran, J B, Hemmingsen, L, Kerber, O, Habjanic, J, Freisinger, E & Krezel, A 2022, ' An Extremely Stable Interprotein Tetrahedral Hg(Cys) 4 Core Forms in the Zinc Hook Domain of Rad50 Protein at Physiological pH ', Chemistry: A European Journal, vol. 28, no. 66, e202202738 . https://doi.org/10.1002/chem.202202738
In nature, thiolate-based systems are the primary targets of divalent mercury (Hg-II) toxicity. The formation of Hg(Cys)(x) cores in catalytic and structural protein centers mediates mercury's toxic effects and ultimately leads to cellular damage. Mu
Autor:
Józef Ba Tran, Artur Krężel
Publikováno v:
Journal of Proteome Research
InterMetalDB is a free-of-charge database and browser of intermolecular metal binding sites that are present on the interfaces of macromolecules forming larger assemblies based on structural information deposited in Protein Data Bank (PDB). It can be
Publikováno v:
Trends in biochemical sciences. 46(1)
The presence of Zn2+ at protein–protein interfaces modulates complex function, stability, and introduces structural flexibility/complexity, chemical selectivity, and reversibility driven in a Zn2+-dependent manner. Recent studies have demonstrated
Publikováno v:
Journal of inorganic biochemistry. 204
Metal ions are essential elements present in biological systems able to facilitate many cellular processes including proliferation, signaling, DNA synthesis and repair. Zinc ion (Zn(II)) is an important cofactor for numerous biochemical reactions. Co