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Documento: Artículo
Título:The biology of molecular chaperones - very complex activities for quite simple proteins
Autor:Galigniana, M.D.
Filiación:Instituto de Biología y Medicina Experimental (IBYME/CONICET), Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires (1428), Argentina
Palabras clave:actin; chaperone; cytoskeleton protein; heat shock protein; heat shock protein 90; proteome; taipoxin; tubulin; vimentin; chaperone; biological activity; complex formation; drug protein binding; editorial; heat stress; nucleosome; protein aggregation; protein assembly; protein degradation; protein denaturation; protein expression; protein folding; protein function; protein homeostasis; protein localization; protein processing; protein structure; animal; chemistry; human; metabolism; Animals; Humans; Molecular Chaperones
Año:2014
Volumen:15
Número:3
Página de inicio:169
Página de fin:170
DOI: http://dx.doi.org/10.2174/138920371503140422123952
Título revista:Current Protein and Peptide Science
Título revista abreviado:Curr. Protein Pept. Sci.
ISSN:13892037
CODEN:CPPSC
CAS:taipoxin, 52019-39-3; Molecular Chaperones
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13892037_v15_n3_p169_Galigniana

Referencias:

  • Fohlman, J., Eaker, D., Karlsoon, E., Thesleff, S., Taipoxin, an extremely potent presynaptic neurotoxin from the venom of the australian snake taipan (Oxyuranus s. scutellatus). Isolation, characterization, quaternary structure and pharmacological properties (1976) Eur. J. Biochem, 68 (2), pp. 457-469
  • Laskey, R.A., Honda, B.M., Mills, A.D., Finch, J.T., Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA (1978) Nature, 275 (5679), pp. 416-420
  • Ellis, R.J., Minton, A.P., Protein aggregation in crowded environments (2006) Biol. Chem, 387 (5), pp. 485-497
  • Pratt, W.B., Toft, D.O., Steroid receptor interactions with heat shock protein and immunophilin chaperones (1997) Endocr. Rev, 18 (3), pp. 306-360
  • Galigniana, M.D., Echeverria, P.C., Erlejman, A.G., Piwien-Pilipuk, G., Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore (2010) Nucleus, 1 (4), pp. 299-308
  • Lindquist, S., Protein folding sculpting evolutionary change (2009) Cold Spring Harb. Symp. Quant. Biol, 74, pp. 103-108
  • Ritossa, F., A new puffing pattern induced by temperature shock and DNP in Drosophila (1962) Experientia, 18, pp. 571-573
  • Quinta, H.R., Galigniana, N.M., Erlejman, A.G., Lagadari, M., Piwien-Pilipuk, G., Galigniana, M.D., Management of cytoskeleton architecture by molecular chaperones and immunophilins (2011) Cell Signal, 23 (12), pp. 1907-1920

Citas:

---------- APA ----------
(2014) . The biology of molecular chaperones - very complex activities for quite simple proteins. Current Protein and Peptide Science, 15(3), 169-170.
http://dx.doi.org/10.2174/138920371503140422123952
---------- CHICAGO ----------
Galigniana, M.D. "The biology of molecular chaperones - very complex activities for quite simple proteins" . Current Protein and Peptide Science 15, no. 3 (2014) : 169-170.
http://dx.doi.org/10.2174/138920371503140422123952
---------- MLA ----------
Galigniana, M.D. "The biology of molecular chaperones - very complex activities for quite simple proteins" . Current Protein and Peptide Science, vol. 15, no. 3, 2014, pp. 169-170.
http://dx.doi.org/10.2174/138920371503140422123952
---------- VANCOUVER ----------
Galigniana, M.D. The biology of molecular chaperones - very complex activities for quite simple proteins. Curr. Protein Pept. Sci. 2014;15(3):169-170.
http://dx.doi.org/10.2174/138920371503140422123952