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Titolo:
Macromolecular dynamics in living cell nuclei revealed by fluorescence redistribution after photobleaching
Autore:
Houtsmuller, AB; Vermeulen, W;
Indirizzi:
Erasmus Univ, Dept Pathol, Josephine Nefkens Inst, NL-3000 DR Rotterdam, Netherlands Erasmus Univ Rotterdam Netherlands NL-3000 DR DR Rotterdam, Netherlands Erasmus Univ, Dept Cell Biol & Genet, Ctr Biol & Genet, NL-3000 DR Rotterdam, Netherlands Erasmus Univ Rotterdam Netherlands NL-3000 DR DR Rotterdam, Netherlands
Titolo Testata:
HISTOCHEMISTRY AND CELL BIOLOGY
fascicolo: 1, volume: 115, anno: 2001,
pagine: 13 - 21
SICI:
0948-6143(200101)115:1<13:MDILCN>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
METAPHASE CHROMOSOME STRUCTURE; INTERPHASE CHROMOSOMES; TOPOISOMERASE-II; TERRITORIES; ORGANIZATION; COMPARTMENTALIZATION; TRANSCRIPTION; DIFFUSION; PROTEINS; DOMAINS;
Keywords:
nuclear protein dynamics; GFP; FRAP; FLIP;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Houtsmuller, AB Erasmus Univ, Dept Pathol, Josephine Nefkens Inst, POB 1738, NL-3000 DR Rotterdam, Netherlands Erasmus Univ POB 1738 Rotterdam Netherlands NL-3000 DR ds
Citazione:
A.B. Houtsmuller e W. Vermeulen, "Macromolecular dynamics in living cell nuclei revealed by fluorescence redistribution after photobleaching", HISTOCHEM C, 115(1), 2001, pp. 13-21

Abstract

Regulation and structural requirements of vital nuclear processes such as DNA replication, transcription, RNA processing and DNA repair inside the eukaryote nucleus are as yet poorly understood. Although a wealth of evidenceexists pointing to a considerable degree of spatial organisation of chromatin and nuclear processes, there are still questions concerning the dynamics and interaction of nuclear proteins that remain unanswered. The cloning of the gene encoding the green fluorescent protein (GFP) has revolutionised the study of proteins in living cells. The expression of recombinant cDNA fusion plasmids of GFP and proteins of interest currently enables the investigation of those proteins in living cells. Time-lapse confocal microscopy as well as quantitative fluorescence methods such as fluorescence redistribution after photobleaching (FRAP) and fluorescence resonance energy transferare widely applied to living cells expressing GFP fusion proteins. This review gives an overview of the current state of knowledge of nuclear structure and function. In particular, the different applications of FRAP technology to study the dynamics of GFP-tagged nuclear proteins will be summarised.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 23:02:37