The biology of molecular chaperones - very complex activities for quite simple proteins

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Autor principal: Galigniana, M.D
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Bentham Science Publishers B.V. 2014
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-84904515357 
024 7 |2 cas  |a taipoxin, 52019-39-3; Molecular Chaperones 
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100 1 |a Galigniana, M.D. 
245 1 4 |a The biology of molecular chaperones - very complex activities for quite simple proteins 
260 |b Bentham Science Publishers B.V.  |c 2014 
270 1 0 |m Galigniana, M. D.; Instituto de Biología y Medicina Experimental (IBYME/CONICET), Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires (1428), Argentina; email: mgaligniana@conicet.gov.ar 
506 |2 openaire  |e Política editorial 
504 |a 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 
504 |a 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 
504 |a Ellis, R.J., Minton, A.P., Protein aggregation in crowded environments (2006) Biol. Chem, 387 (5), pp. 485-497 
504 |a Pratt, W.B., Toft, D.O., Steroid receptor interactions with heat shock protein and immunophilin chaperones (1997) Endocr. Rev, 18 (3), pp. 306-360 
504 |a 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 
504 |a Lindquist, S., Protein folding sculpting evolutionary change (2009) Cold Spring Harb. Symp. Quant. Biol, 74, pp. 103-108 
504 |a Ritossa, F., A new puffing pattern induced by temperature shock and DNP in Drosophila (1962) Experientia, 18, pp. 571-573 
504 |a 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 
593 |a Instituto de Biología y Medicina Experimental (IBYME/CONICET), Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires (1428), Argentina 
690 1 0 |a ACTIN 
690 1 0 |a CHAPERONE 
690 1 0 |a CYTOSKELETON PROTEIN 
690 1 0 |a HEAT SHOCK PROTEIN 
690 1 0 |a HEAT SHOCK PROTEIN 90 
690 1 0 |a PROTEOME 
690 1 0 |a TAIPOXIN 
690 1 0 |a TUBULIN 
690 1 0 |a VIMENTIN 
690 1 0 |a CHAPERONE 
690 1 0 |a BIOLOGICAL ACTIVITY 
690 1 0 |a COMPLEX FORMATION 
690 1 0 |a DRUG PROTEIN BINDING 
690 1 0 |a EDITORIAL 
690 1 0 |a HEAT STRESS 
690 1 0 |a NUCLEOSOME 
690 1 0 |a PROTEIN AGGREGATION 
690 1 0 |a PROTEIN ASSEMBLY 
690 1 0 |a PROTEIN DEGRADATION 
690 1 0 |a PROTEIN DENATURATION 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTEIN FOLDING 
690 1 0 |a PROTEIN FUNCTION 
690 1 0 |a PROTEIN HOMEOSTASIS 
690 1 0 |a PROTEIN LOCALIZATION 
690 1 0 |a PROTEIN PROCESSING 
690 1 0 |a PROTEIN STRUCTURE 
690 1 0 |a ANIMAL 
690 1 0 |a CHEMISTRY 
690 1 0 |a HUMAN 
690 1 0 |a METABOLISM 
690 1 0 |a ANIMALS 
690 1 0 |a HUMANS 
690 1 0 |a MOLECULAR CHAPERONES 
773 0 |d Bentham Science Publishers B.V., 2014  |g v. 15  |h pp. 169-170  |k n. 3  |p Curr. Protein Pept. Sci.  |x 13892037  |t Current Protein and Peptide Science 
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856 4 0 |u https://doi.org/10.2174/138920371503140422123952  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_13892037_v15_n3_p169_Galigniana  |y Handle 
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