Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation

We have studied the biochemical features, the conformational preferences in solution, and the DNA binding properties of human p8 (hp8), a nucleoprotein whose expression is affected during acute pancreatitis. Biochemical studies show that hp8 has properties of the high mobility group proteins, HMG-I/...

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Detalles Bibliográficos
Autores principales: Mallo, Gustavo V., Mizyrycki, Cynthia L., Giono, Luciana Eugenia, Cánepa, Eduardo Tomás, Moreno de Colonna, Silvia
Publicado: 2001
Materias:
Biochemistry
DNA
Electrophoresis
Fourier transform infrared spectroscopy
Nuclear magnetic resonance spectroscopy
Gel shift analysis
Proteins
cyclic AMP dependent protein kinase
high mobility group B1 protein
monomer
nucleoprotein
protein hp8
unclassified drug
basic helix loop helix transcription factor
DNA binding protein
growth promotor
high mobility group A1a protein
high mobility group protein
P8 protein, human
transcription factor
tumor protein
acute pancreatitis
article
binding affinity
biophysics
circular dichroism
gel mobility shift assay
human
infrared spectroscopy
nuclear magnetic resonance spectroscopy
priority journal
protein conformation
protein DNA binding
protein folding
protein phosphorylation
protein secondary structure
sequence analysis
sequence homology
structure analysis
amino acid sequence
comparative study
genetics
metabolism
molecular genetics
nuclear magnetic resonance
nucleotide sequence
phosphorylation
protein binding
protein tertiary structure
Amino Acid Sequence
Basic Helix-Loop-Helix Transcription Factors
Circular Dichroism
Conserved Sequence
Cyclic AMP-Dependent Protein Kinases
DNA-Binding Proteins
Growth Substances
High Mobility Group Proteins
HMGA1a Protein
Humans
Molecular Sequence Data
Neoplasm Proteins
Nuclear Magnetic Resonance, Biomolecular
Phosphorylation
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Spectroscopy, Fourier Transform Infrared
Transcription Factors
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v276_n4_p2742_Encinar
http://hdl.handle.net/20.500.12110/paper_00219258_v276_n4_p2742_Encinar
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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