iron-sulfur cluster co-chaperone protein HscB isoform X1 [Homo sapiens - Protein

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Structural characterization of the human DjC20/HscB cochaperone in solution. [Biochim Biophys Acta Proteins ...]
Structural characterization of the human DjC20/HscB cochaperone in solution.
Coto ALS, Pereira AA, Oliveira SD, Moritz MNO, Franco da Rocha AM, Dores-Silva PR, da Silva NSM, de Araújo Nogueira AR, Gava LM, Seraphim TV, et al. Biochim Biophys Acta Proteins Proteom. 2024 Jan 1; 1872(1):140970. Epub 2023 Oct 21.
Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20. [Metallomics. 2016]
Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20.
Maio N, Rouault TA. Metallomics. 2016 Oct 1; 8(10):1032-1046.
Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain. [J Biol Chem. 2008]
Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain.
Bitto E, Bingman CA, Bittova L, Kondrashov DA, Bannen RM, Fox BG, Markley JL, Phillips GN Jr. J Biol Chem. 2008 Oct 31; 283(44):30184-92. Epub 2008 Aug 19.

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