W
William Dowhan
Researcher at University of Texas Health Science Center at Houston
Publications - 171
Citations - 15799
William Dowhan is an academic researcher from University of Texas Health Science Center at Houston. The author has contributed to research in topics: Cardiolipin & Membrane protein. The author has an hindex of 70, co-authored 169 publications receiving 14687 citations. Previous affiliations of William Dowhan include University of Melbourne & University of Texas System.
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Journal ArticleDOI
MOLECULAR BASIS FOR MEMBRANE PHOSPHOLIPID DIVERSITY: Why Are There So Many Lipids?
TL;DR: The wide range of processes in which specific involvement of phospholipids has been documented explains the need for diversity inospholipid structure and why there are so many membrane lipids.
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Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane.
TL;DR: It is reported here that in a crd1Δ strain of yeast (null in expression of CL synthase) ∼90% of complexes III and IV were observed as individual homodimers; only the supercomplex was observed with CRD1wild type cells, indicating that CL plays a central role in higher order organization of components of the respiratory chain of mitochondria.
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The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins
TL;DR: This work defines the stimulation of SecA ATPase by lipid as "SecA/lipid ATPase", and indicates that liposome-bound SecA protein recognizes both leader and mature domains, suggesting an underlying unity of mechanism.
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An essential role for a phospholipid transfer protein in yeast Golgi function.
TL;DR: It is established for the first time an in vivo function for a phospholipid transfer protein, namely a role in the compartment-specific stimulation of protein secretion, in yeast.
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Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange.
TL;DR: Cardiolipin (CL)-specific fluorescent dye 10-N-nonyl-acridine orange (NAO) was used to visualize CL distribution in Escherichia coli cells of different phospholipid compositions and revealed NAO-binding domains in the plane of the cell membrane.