Publications by authors named "Monireh Goodarzifard"
Article Synopsis
- Nuclear receptors rely on coactivator proteins for gene transcription, primarily binding to the conserved LXXLL peptide motif found in many coactivators.
- Recent findings reveal a new and more complex PXLXXLLXXP binding motif that improves our understanding of how these interactions work.
- Studies using molecular modeling and X-ray crystallography have identified the critical role of flanking prolines in the α-helix structure, which can inform the design of new drugs to modulate nuclear receptor-coactivator interactions.
Cytotoxic T lymphocytes (CTLs) kill target cells through the polarized release of lytic molecules from secretory lysosomes. Loss of munc13-4 function inhibits this process and causes familial hemophagocytic lymphohistiocytosis type 3 (FHL3). munc13-4 binds rab27a, but the necessity of the complex remains enigmatic, because studies in knockout models suggest separate functions.
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