Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins

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Research done in the last years strongly support the hypothesis that PIP aquaporin can form heterooligomeric assemblies, specially combining PIP2 monomers with PIP1 monomers. Nevertheless, the structural elements involved in the ruling of homo versus heterooligomeric organization are not completely...

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Detalles Bibliográficos
Autores principales: Jozefkowicz, C., Rosi, P., Sigaut, L., Soto, G., Pietrasanta, L.I., Amodeo, G., Alleva, K.
Formato: Artículo publishedVersion
Publicado: 2013
Materias:
aquaporin
complementary RNA
article
beet
cell membrane
confocal microscopy
controlled study
dose response
molecular dynamics
mutagenesis
nonhuman
nucleotide sequence
oocyte
pH
phylogeny
protein content
protein expression
protein function
protein localization
protein protein interaction
RNA synthesis
sequence analysis
water permeability
water transport
Amino Acid Sequence
Animals
Aquaporins
Beta vulgaris
Cell Membrane Permeability
Conserved Sequence
Hydrogen-Ion Concentration
Molecular Dynamics Simulation
Molecular Sequence Data
Mutant Proteins
Osmosis
Plant Proteins
Protein Binding
Protein Structure, Secondary
Recombinant Proteins
Structure-Activity Relationship
Xenopus laevis
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_19326203_v8_n3_p_Jozefkowicz
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_19326203_v8_n3_p_Jozefkowicz_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

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