<filename>doc/presentation/TEST.bib
@article{Waddington1959,
abstract = {THE battle, which raged for so long between the theories of evolution supported by geneticists on one hand and by naturalists on the other, has in recent years gone strongly in favour of the former. Few biologists now doubt that genetical investigation has revealed at any rate the most important categories of hereditary variation; and the classical 'naturalist' theory-the inheritance of acquired characters-has been very generally relegated to the background because, in the forms in which it has been put forward, it has required a type of hereditary variation for the existence of which there was no adequate evidence.},
author = {Waddington, <NAME>},
doi = {10.1038/1831654a0},
isbn = {0201483645},
issn = {0028-0836},
journal = {Nature},
keywords = {Genetics},
pages = {1654--1655},
pmid = {13666847},
title = {{Canalization of development and genetic assimilation of acquired characters.}},
volume = {183},
year = {1959}
}
@article{Moitra,
abstract = {The way in which proteins attain and maintain their final form is of fundamental importance. Recent work has focused on the role of a set of ubiquitous proteins, termed chaperonins, in the assembly of phage and multisubunit proteins. The range of chaperonin action is unknown; they could interact with most cellular polypeptides or have a limited subset of protein partners. Included in the chaperonin family is the essential heat-shock regulated Escherichia coli groEL gene product. Over-expression of the groE operon in E. coli causes enhanced assembly of heterologously expressed ribulose bisphosphate carboxylase subunits and suppresses the heat-sensitive mutant phenotype of several dnaA alleles. It has been inferred that suppression of heat-sensitive mutations is confined to dnaA alleles and that this confinement could reflect an interaction between the groE operon products and a dnaA protein aggregate at the replication origin. We now report that multiple copies of the groE operon suppress mutations in genes encoding several diverse proteins. Our data indicate a general role for the groE operon products, the GroEL and GroES proteins, in the folding-assembly pathways of many proteins.},
author = {{<NAME>}, <NAME> and Gatenby, <NAME> and LaRossa, <NAME>},
issn = {0028-0836},
journal = {Nature},
pages = {451--453},
pmid = {2573840},
title = {{Demonstration by genetic suppression of interaction of GroE products with many proteins.}},
volume = {342},
year = {1989}
}
