Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE (2006)
- Authors:
- USP affiliated authors: WARD, RICHARD JOHN - FFCLRP ; CIANCAGLINI, PIETRO - FFCLRP
- Unidade: FFCLRP
- Assunto: ENZIMAS
- Language: Inglês
- Imprenta:
- Source:
- Título: Cell Biochemistry and Biophysics
- ISSN: 1085-9195
- Volume/Número/Paginação/Ano: v. 44, n. 3, p. 438-445, 2006
-
ABNT
RIGOS, Carolina Fortes et al. Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE. Cell Biochemistry and Biophysics, v. 44, n. 3, p. 438-445, 2006Tradução . . Acesso em: 09 nov. 2024. -
APA
Rigos, C. F., Santos, H. de L., Ward, R. J., & Ciancaglini, P. (2006). Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE. Cell Biochemistry and Biophysics, 44( 3), 438-445. -
NLM
Rigos CF, Santos H de L, Ward RJ, Ciancaglini P. Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE. Cell Biochemistry and Biophysics. 2006 ; 44( 3): 438-445.[citado 2024 nov. 09 ] -
Vancouver
Rigos CF, Santos H de L, Ward RJ, Ciancaglini P. Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE. Cell Biochemistry and Biophysics. 2006 ; 44( 3): 438-445.[citado 2024 nov. 09 ] - Thermal denaturation of the Na,K-ATPase solubilized and incorporated in DPPC:DPPE-liposomes
- Stability of '('alfa''beta') IND. 2' form of Na, K-ATPase: conformational states in the presence of chemical agents and thermal denaturation
- Influence of enzyme conformational changes on catalytic activity of solubilized Na,K-ATPase investigated by circular dichroism spectroscopy
- pH effects in Na, K-ATPase: catalytic activity, fluorescence and circular dichroism analysis
- Estabilidade térmica da Na, K-ATPase solubilizada e incorporada em lipossomos de DPPC:DPPE
- Influence of enzyme conformational changes catalytic activity investigated by circular dichroism spectroscopy
- The study of the association of the ('alfa''beta) protomer of Na, K-ATPase solubilized with 'C IND.12''E IND. 8'
- The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity
- Circular dichroism associated with surface tension and dilatational elasticity to study the association of NA,K-ATPase subunits
- Crystal structure of mitoxin II, a manomeric Lys49-Phospholipase 'A IND. 2' homologue isolated from the venom of Cerrophidion (Bothrops) godmani
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