dc.contributor.author | Goldberg, Michel E. | - |
dc.date.accessioned | 2014-07-03T06:47:04Z | |
dc.date.available | 2014-07-03T06:47:04Z | |
dc.date.issued | 2005 | fr_FR |
dc.identifier.citation | Goldberg, Michel E. ; Le repliement des protéines : seconde traduction du message génétique, Med Sci (Paris), 2005, Vol. 21, N° 6-7; p. 563-568 ; DOI : 10.1051/medsci/2005216-7563 | fr_FR |
dc.identifier.issn | 1958-5381 | fr_FR |
dc.identifier.uri | http://hdl.handle.net/10608/5533 | |
dc.description.abstract | Translation of the message encoded in a gene proceeds in two steps: one translates the gene’s base sequence into the protein’s aminoacid sequence; the second translates the latter into a complex, very precisely defined folded structure, the single one endowed with the specific biological properties. The second step, named « protein folding », is currently a central issue in biological research. The present editorial introduces a series of articles dedicated to this problem. It gives a brief historical overview of how our understanding of the folding mechanisms has evolved, which will be described in more details by J. Yon-Kahn. It also places the problem of protein folding in the context of basic research and its applications in several domains: (1) medicine, where folding diseases (reviewed by G. Grateau) and in particular neurodegenerative diseases caused by prions (see article by R. Melki), are more and more recognized as a public health issue ; (2) biotechnology, where the production of recombinant proteins for research, diagnostic or therapy purposes is often hampered by misfolding when a protein is expressed at high concentration in a foreign host (modern approaches to overcome this difficulty will be discussed by J.M. Betton and A. Chaffotte, and the way in which « chaperones » prevent misfolding in the cell under natural conditions will be described by A.P. Arrigo) ; (3) postgenomics, where the interpretation of the immense amount of base-sequence information collected through genome sequencing needs to be translated as rapidly as possible into structural and functional information (the computer approaches used to predict the 3D structure of a protein from its aminoacid sequence will be outlined by T. Simonson). This series comes timely, at a moment when the efforts of experimentalists, theoriticians, and « users » of protein folding start converging, and boost the power of molecular biology. | en |
dc.language.iso | fr | fr_FR |
dc.publisher | EDK | fr_FR |
dc.relation.ispartof | Éditorial | fr_FR |
dc.rights | Article en libre accès | fr |
dc.rights | Médecine/Sciences - Inserm - SRMS | fr |
dc.source | M/S. Médecine sciences [ISSN papier : 0767-0974 ; ISSN numérique : 1958-5381], 2005, Vol. 21, N° 6-7; p. 563-568 | fr_FR |
dc.subject.mesh | Pliage des protéines | fr |
dc.subject.mesh | Protéines | fr |
dc.title | Le repliement des protéines : seconde traduction du message génétique | fr |
dc.type | Article | fr_FR |
dc.contributor.affiliation | Unité de repliement et modélisation des protéines, Institut Pasteur, 28, rue du Docteur Roux, 75724 Paris Cedex 15, France | fr_FR |
dc.identifier.doi | 10.1051/medsci/2005216-7563 | fr_FR |
dc.identifier.pmid | 15985190 | fr_FR |