The HPV16 E7 Viral Oncoprotein Self-Assembles into Defined Spherical Oligomers

Despite the fact that E7 is a major transforming oncoprotein in papillomavirus, its structure and precise molecular mechanism of action remain puzzling to date. E7 proteins share sequence homology and proteasome targeting properties of tumor suppressors with adenovirus E1A and SV40 T antigen, two ot...

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Detalles Bibliográficos
Autores principales: Alonso, L.G., García-Alai, M.M., Smal, C., Centeno, J.M., Iacono, R., Castaño, E., Gualfetti, P., De Prat-Gay, G.
Formato: JOUR
Materias:
Chelation
DNA
Hydrophobicity
Oligomers
pH
Proteins
Self assembly
Tumors
Viruses
Oncoproteins
Spherical materials
Biochemistry
congo red
oligomer
oncoprotein
protein E7
thioflavine
virus protein
virus T antigen
article
beta sheet
cancer inhibition
circular dichroism
conformational transition
DNA tumor virus
electron microscopy
fluorescence
hydrophobicity
light scattering
molecular mechanics
molecular weight
nonhuman
pH measurement
priority journal
protein assembly
protein binding
protein conformation
protein folding
protein stability
protein structure
protein tertiary structure
sequence homology
Simian virus 40
Wart virus
Casein Kinase II
Circular Dichroism
Congo Red
Dimerization
Fluorescent Dyes
Humans
Molecular Weight
Oncogene Proteins, Viral
Papillomaviridae
Phosphorylation
Protein Binding
Protein Structure, Secondary
Protein-Serine-Threonine Kinases
Solubility
Thiazoles
Virus Assembly
Zinc
Adenoviridae
DNA viruses
Human papillomavirus types
Papillomavirus
Simiae
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00062960_v43_n12_p3310_Alonso
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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