Editing Chaperone (protein) (section)

==History==
The investigation of chaperones has a long history.<ref>{{cite journal | vauthors = Ellis RJ | title = Discovery of molecular chaperones | journal = Cell Stress & Chaperones | volume = 1 | issue = 3 | pages = 155–60 | date = September 1996 | pmid = 9222600 | pmc = 248474 }}</ref> The term "molecular chaperone" appeared first in the literature in 1978, and was invented by [[Ron Laskey]] to describe the ability of a nuclear protein called [[nucleoplasmin]] to prevent the aggregation of folded histone proteins with DNA during the assembly of nucleosomes.<ref>{{cite journal | vauthors = Laskey RA, Honda BM, Mills AD, Finch JT | title = Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA | journal = Nature | volume = 275 | issue = 5679 | pages = 416–20 | date = October 1978 | pmid = 692721 | doi = 10.1038/275416a0 | bibcode = 1978Natur.275..416L | s2cid = 2535641 }}</ref> The term was later extended by [[R. John Ellis]] in 1987 to describe proteins that mediated the post-translational assembly of protein complexes.<ref>{{cite journal | vauthors = Ellis J | title = Proteins as molecular chaperones | journal = Nature | volume = 328 | issue = 6129 | pages = 378–9 | year = 1987 | pmid = 3112578 | doi = 10.1038/328378a0 | bibcode = 1987Natur.328..378E | s2cid = 4337273 }}</ref> In 1988, it was realised that similar proteins mediated this process in both prokaryotes and eukaryotes.<ref>{{cite journal | vauthors = Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ | display-authors = 6 | title = Homologous plant and bacterial proteins chaperone oligomeric protein assembly | journal = Nature | volume = 333 | issue = 6171 | pages = 330–4 | date = May 1988 | pmid = 2897629 | doi = 10.1038/333330a0 | bibcode = 1988Natur.333..330H | s2cid = 4325057 }}</ref> The details of this process were determined in 1989, when the ATP-dependent protein folding was demonstrated ''in vitro''.<ref>{{cite journal | vauthors = Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH | title = Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP | journal = Nature | volume = 342 | issue = 6252 | pages = 884–9 | year = 1989 | pmid = 10532860 | doi = 10.1038/342884a0 | bibcode = 1989Natur.342..884G | s2cid = 4319510 }}</ref>