p53 and its 14 kDa C-terminal domain recognize primary DNA damage in the form of insertion/deletion mismatches
Article Abstract:
Electron microscopy and gel retardation studies indicate that p53 protein and its 14kDa C-terminal can recognize and bind to insertion/deletion mismatches (IDL) in DNA and form very stable complexes. The progress of a tumor can be recognized by the fact that the cell cannot detect and repair DNA damage. The complexes formed by p53 with IDL mismatches in DNA have a half-life of over two hours indicating that p53 probably binds other proteins to the site and provides a signal for the damage.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Increasing the complexity of coactivation in nuclear receptor signaling
Article Abstract:
A series of coactivators that associates with nuclear receptors have been isolated. The nuclear receptors, which are indistinguishable from other eukaryotic factors regulating transcription, bind selectively to DNA. An RNA coactivator for steroid receptors was also determined. It works through the N-terminal AF1 domain and may possibly function as an RNA. However, several concerns still remain about nuclear receptor coactivation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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Dynamic nuclear pore complexes: Life on the edge
Article Abstract:
Nuclear pore complex (NPC) proteins play active roles in translocation, and that transport is also controlled by dynamic changes in NPC composition and architecture. A review seeks to re-evaluate the understanding of nucleocytoplasmic exchange and to envision the NPC as an ever-changing portal with the potential to regulate crucial cellular functions locally and globally.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
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