C
Carl W. Schmid
Researcher at University of California, Davis
Publications - 102
Citations - 8705
Carl W. Schmid is an academic researcher from University of California, Davis. The author has contributed to research in topics: Alu element & Gene. The author has an hindex of 48, co-authored 102 publications receiving 8524 citations. Previous affiliations of Carl W. Schmid include University of California, Berkeley.
Papers
More filters
Journal ArticleDOI
Molecular weights of homogeneous coliphage DNA's from density-gradient sedimentation equilibrium
Carl W. Schmid,John E. Hearst +1 more
TL;DR: The concentration distributions at sedimentation equilibrium are studied as a function of DNA concentration for T7, T5 and T4 coliphage DNA's and the results extrapolated to infinite dilution to obtain molecular weights for these DNA's.
Journal ArticleDOI
RNA polymerase III promoter and terminator elements affect Alu RNA expression
TL;DR: Results show that Alu expression may be regulated at multiple levels and can respond to cis-acting elements, and a terminator resembling the terminator for the 7SL RNA gene has no effect on in vitro Alu template activity, but increases expression in vivo in a position independent manner.
Journal ArticleDOI
Phylogenetic evidence for multiple Alu source genes.
TL;DR: A member of the young PV Alu sub-family is detected in chimpanzee DNA showing that the PV subfamily is not specific to human DNA, and provides phylogenetic evidence for the existence of multiple Alu source genes.
Journal ArticleDOI
Density‐gradient sedimentation equilibrium of DNA and the effective density gradient of several salts
Carl W. Schmid,John E. Hearst +1 more
TL;DR: In this article, the authors compared various treatments of sedimentation equilibrium on a theoretical and an experimental basis and paid particular attention to the polyelectrolyte nature of the problem and the choice of a neutral component.
Journal ArticleDOI
Zinc-induced secondary structure transitions in human sperm protamines.
TL;DR: The data support a model in which protamine adopts a folded structure in the presence of zinc, and propose that a zinc-modulated structure is physiologically significant considering the relatively high levels of zinc in human sperm.