Steven L. McKnight
University of Texas Southwestern Medical Center
178 Papers
3.1K Citations
Steven L. McKnight is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Gene & Transcription (biology). The author has an hindex of 87, co-authored 175 publications. Previous affiliations of Steven L. McKnight include Baylor University Medical Center & Fred Hutchinson Cancer Research Center.
Chat about Author
Papers
The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
TL;DR: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
3.5K
A Conserved Family of Prolyl-4-Hydroxylases That Modify HIF
TL;DR: In cultured mammalian cells, inappropriate accumulation of HIF caused by forced expression of the HIF-1α subunit under normoxic conditions was attenuated by coexpression of HPH, indicating that HPH is an essential component of the pathway through which cells sense oxygen.
2.6K
Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
Masato Kato,Tina W. Han,Shanhai Xie,Kevin Y. Shi,Xinlin Du,Leeju C. Wu,Hamid Mirzaei,Elizabeth J. Goldsmith,Jamie Longgood,Jimin Pei,Jimin Pei,Nick V. Grishin,Douglas E. Frantz,Jay W. Schneider,She Chen,Lin Li,Michael R. Sawaya,David Eisenberg,Robert Tycko,Steven L. McKnight +19 more
TL;DR: It is discovered that exposure of cell or tissue lysates to a biotinylated isoxazole (b-isox) chemical precipitated hundreds of RNA-binding proteins with significant overlap to the constituents of RNA granules, offering a framework for understanding the function of LC sequences as well as an organizing principle for cellular structures that are not membrane bound.
2K
Regulated expression of three C/EBP isoforms during adipose conversion of 3T3-L1 cells.
TL;DR: The temporal pattern of expression of these three C/EBP isoforms during adipocyte differentiation may reflect the underpinnings of a regulatory cascade that controls the process of terminal cell differentiation.
Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells.
TL;DR: EPAS1 expression is limited to the endothelium of mouse embryos and is capable of specifically activating the transcription of the endothelial tyrosine kinase gene Tie-2, raising the possibility that EPAS1 may represent an important regulator of vascularization, perhaps involving the regulation of endothelial cell gene expression in response to hypoxia.