Exploring the molecular function of PIN1 by nuclear magnetic resonance

Current Protein and Peptide Science

Volumn 7, Issue 3, 2006, Pages 179-194

  Landrieu, Isabelle ^a   Smet, C ^a   Wieruszeski, J M ^a   Sambo, A V ^b   Wintjens, R ^a   Buee L ^b   Lippens, Guy ^a  

^a UNIVERSITÉ DES SCIENCES ET TECHNOLOGIES DE LILLE   (France)

^b INSERM   (France)

Author keywords

Catalytic Domain; Cis trans conformation; Disordered Proteins; Multiphosphorylated tau; PIN1 substrates; WW domain

Indexed keywords

EPITOPE; ISOMERASE; PEPTIDYLPROLYL ISOMERASE PIN1; PROLINE; PROLINE DERIVATIVE; REGULATOR PROTEIN; SERINE; TAU PROTEIN; THREONINE; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARABIDOPSIS; CARBOXY TERMINAL SEQUENCE; HUMAN; ISOMERIZATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DEPHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATALYTIC DOMAIN; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDYLPROLYL ISOMERASE; PHOSPHORYLATION; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

ARABIDOPSIS THALIANA;

EID: 33745112909     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920306777452303     Document Type: Review

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