Complete thermodynamic and kinetic characterization of the isomer-specific interaction between Pin1-WW domain and the amyloid precursor protein cytoplasmic tail phosphorylated at Thr668

Biochemistry

Volumn 51, Issue 43, 2012, Pages 8583-8596

  De, Soumya ^a,d   Greenwood, Alexander I ^a   Rogals, Monique J ^a   Kovrigin, Evgenii L ^b   Lu, Kun Ping ^c   Nicholson, Linda K ^a  

^a Department of Obstetrics Gynecology   (United States)

^b Marquette University   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

^d UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEINS; BINDING DOMAIN; BINDING EQUILIBRIA; BINDING EVENTS; BINDING KINETICS; BIOLOGICAL PROCESS; CELLULAR SIGNALING; CIS-TRANS; CIS-TRANS ISOMERIZATION; CYTOPLASMIC TAIL; DEPHOSPHORYLATIONS; DIFFUSION LIMITS; DISSOCIATION RATES; DYNAMIC EVENTS; EXPERIMENTAL METHODS; ISOTHERMAL TITRATION CALORIMETRY; KINETIC AND THERMODYNAMIC PARAMETERS; KINETIC CHARACTERIZATION; MOLECULAR SWITCHES; NMR LINE SHAPE ANALYSIS; PATHOLOGICAL PROCESS; RAPID RESPONSE; THREE-STATE MODELS; TIME-SCALES; TRANS ISOMERS; WW DOMAIN;

AMINO ACIDS; DISSOCIATION; FLUORESCENCE SPECTROSCOPY; GLYCOPROTEINS; ISOMERS; PHOSPHORYLATION; THERMODYNAMICS;

KINETICS;

AMYLOID PRECURSOR PROTEIN; PEPTIDYLPROLYL ISOMERASE PIN1; PROLINE; SERINE; THREONINE;

ARTICLE; BINDING KINETICS; CIS TRANS ISOMERISM; CONTROLLED STUDY; CYTOPLASM; DIFFUSION; DISSOCIATION; ENZYME SUBSTRATE; FLUORESCENCE SPECTROSCOPY; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PHOSPHORYLATION AND DEPHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; THERMODYNAMICS;

AMYLOID BETA-PROTEIN PRECURSOR; BINDING SITES; HUMANS; ISOMERISM; KINETICS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDYLPROLYL ISOMERASE; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS; TRYPTOPHAN;

EID: 84868148442     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3008214     Document Type: Article

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