Multiple folding states and disorder of ribosomal protein SA, a membrane receptor for laminin, anticarcinogens, and pathogens

Biochemistry

Volumn 51, Issue 24, 2012, Pages 4807-4821

  Ould Abeih, Mohamed B ^a,b,c   Petit Topin, Isabelle ^a,b   Zidane, Nora ^a,b   Baron, Bruno ^a,b   Bedouelle, Hugues ^a,b  

^a INSTITUT PASTEUR   (France)

^b CNRS   (France)

^c UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ANTICARCINOGENS; BLOOD-BRAIN BARRIER; BODY TEMPERATURE; C-DOMAIN; C-TERMINAL EXTENSIONS; CELLULAR COMPARTMENTS; CELLULAR LOCALIZATION; CIRCULAR DICHROISM SPECTROMETRIES; DISORDERED STATE; EPIGALLOCATECHIN GALLATE; FLUORESCENT MOLECULES; FUNCTIONAL INTERACTION; GROWTH FACTOR; HIGH PLASTICITY; LAMININ; MEMBRANE RECEPTORS; MONOMERIC INTERMEDIATE; MULTIFUNCTIONAL PROTEIN; N-TERMINAL DOMAINS; PATHOGENIC MICROORGANISMS; RIBOSOMAL PROTEINS; THREE-STATE EQUILIBRIUM;

ESCHERICHIA COLI; RECOMBINANT PROTEINS; UREA; VIRUSES;

FLUORESCENCE;

ANTINEOPLASTIC AGENT; LAMININ RECEPTOR; MEMBRANE RECEPTOR; RECOMBINANT PROTEIN; RIBOSOMAL PROTEIN SA; RIBOSOME PROTEIN; UNCLASSIFIED DRUG; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; BODY TEMPERATURE; CARBOXY TERMINAL SEQUENCE; CELLULAR DISTRIBUTION; CIRCULAR DICHROISM; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE; HEAT; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; QUANTITATIVE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; ANTICARCINOGENIC AGENTS; HUMANS; LAMININ; MICE; MICROBIOLOGY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; RECEPTORS, LAMININ; RIBOSOMAL PROTEINS; SPECTROMETRY, FLUORESCENCE; UREA;

EID: 84862577518     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300335r     Document Type: Article

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