Fig 1: (A) Western blotting of Hsp90, Hsp70, ARFIP1, PNN, NAP1L1, ECSH1 and PTGES3, after treatment for 36 h. Each blot is the representative result of three independent experiments. (B) Quantitative data of (A). *p < 0.01, **p < 0.01 compared with control group.
Fig 2: Sanger sequencing of putatively pathogenic variants in six candidate genes and corresponding structural mapping. (A) Sanger sequencing validated the existence of putatively pathogenic genetic variants in six genes from four families. (B) Structures of RyR2, ATP2A2, PLXNB2, and NAP1L1 are shown. Structural mapping of the mutation T357I onto the structure of ATP2A2. T357 forms four hydrogen bonds with K352, G354, and D600, whereas only one is left after changing to I357. The variant p.N1551S (located in the SPRY3) and p.R137W (located in the NTD) are indicated on the structure of RyR2. Structural mapping of the mutation E54G onto the structure of NAP1L1, and this mutation changes a negatively charged residue to a non-charged residue. Structural mapping of the variant p.R463Q and p.D1573E onto the structure of PLXNB2. R463Q and D1573E are located on the extracellular and intracellular sides, respectively. The reference structures were downloaded from the PDB and AlphaFold protein structure databases. All the figures were prepared using PyMOL.
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