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The Journal of Biological Chemistry logoLink to The Journal of Biological Chemistry
. 2009 Dec 18;284(51):35996. doi: 10.1074/jbc.A708704200

Mechanism of small heat shock protein function in vivo. A knock-in mouse model demonstrates that the R49C mutation in αA-crystallin enhances protein insolubility and cell death.

Jing-hua Xi, Fang Bai, Julia Gross, R Reid Townsend, A Sue Menko, Usha P Andley
PMCID: PMC2791027

VOLUME 283 (2008) PAGES 5801–5814

On page 5802, in the right column, lines 22–24 from the top, the corrected sentence is as follows: “First generation offspring that inherited the targeted allele with neomycin were subsequently backcrossed into C57BL/6J (for at least three generations).” In the right column, line 19 from the bottom, the corrected sentence is as follows: “Some of these mice were further genotyped to exclude the presence of a deletion mutation in the gene for lens phakinin (CP49), which is characteristic of the 129 strain from which the ES cells were derived.”

On page 5807, in the left column, lines 8–10 from the top, the corrected sentence is as follows: “Fig. 2 shows the MS and fragmentation spectra of the predicted peptide from a combined endopeptidase digest (LysC + GluC + trypsin) of the wild type αA-crystallin from lenses derived from mice prior to Cre mating.” In the left column, lines 8–11 from the bottom, the corrected sentence is as follows: “αA-R49C homozygous eyes weighed 60–70% less than eyes of wild type and heterozygous littermates.”

On page 5809, Fig. 4 is being withdrawn because it contained erroneous data.

These additions and corrections do not result in any change in the conclusions of the article.


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