In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid
sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the …

Exposure of cells to conditions of environmental stress—including heat shock, oxidative
stress, heavy metals, or pathologic conditions, such as ischemia and reperfusion …

The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …

The products of the Escherichia coli dnaK, dnaJ, and grpE heat shock genes have been
previously shown to be essential for bacteriophage lambda DNA replication at all …

The DNA binding activity of p53 is required for its tumor suppressor function; we show here
that this activity is cryptic but can be activated by cellular factors acting on a C-terminal …

The chaperone protein network controls both initial protein folding and subsequent
maintenance of proteins in the cell. Although the native structure of a protein is principally …

▪ Abstract A mechanism for regulating gene expression at the level of transcription utilizes an
antagonist of the sigma transcription factor known as the anti-sigma (anti-σ) factor. The …

A putative Z‐DNA binding protein, named zuotin, was purified from a yeast nuclear extract
by means of a Z‐DNA binding assay using [32P] poly (dG‐m5dC) and [32P] oligo (dG …

Pelham previously proposed that the hsp70 family of heat shock proteins could prevent the
formation and/or allow the dissolution of protein aggregates created during stress …

SUMMARY Simian virus 40 (SV40) is a small DNA tumor virus that has been extensively
characterized due to its relatively simple genetic organization and the ease with which its …