Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Venus”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 199 records · Page 11Linked to original sources
PubMed1990

["The Venus of Pest"--expedition of an anatomical beauty].

The Semmelweis-Museum in Budapest, Hungary, has a small collection of anatomical wax models. Studying the correspondence of the Austrian emperor Joseph II., then King of Hungary with representatives of the Hungarian administration, we were able to find out the origin of these models, their transportation to Hungary and their large significance in anatomical teaching at the end of the 18th century in Hungary. These models are the result of a long-lasting cooperation between artists and anatomists, particularly in Italy. Their artistic climax is reached during the second term of the 18th century, reflecting the complex interaction of contemporary sociocultural trends i.e. popularization of results of scientific research, traits of enlightenment combined with an artistic hyperidealistic typization as known from classical antiquity and sponsored financially as a means of imperial representation. The aim of the study was to point to the eminent importance of this collection as a monument of cultural heritage.

Anatomy↗
PubMed1970

Water on Venus?

Explore the source record for details and available documents.

Astronomical Phenomena↗
PubMedDate not supplied

The birth of Venus.

Explore the source record for details and available documents.

Aphrodisiacs↗
PubMed1982

Hinge-bending in L-arabinose-binding protein. The "Venus's-flytrap" model.

Theoretical conformational energy calculations show that large changes in the width of the binding-site cleft in the L-arabinose-binding protein involve only modest changes in the protein internal energy. Solvation energy changes associated with such variations of the cleft width and with protein-ligand interactions are estimated to be significantly larger than the internal energy changes. These results indicate that the binding-site cleft is open in the unliganded protein and is induced to close upon ligation. This picture is consistent with experimental data on the structure and binding kinetics of the L-arabinose-binding protein and provides a physical framework for interpreting such data.

Bacterial Proteins↗