Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis

Proteins: Structure, Function and Genetics

Volumn 59, Issue 2, 2005, Pages 347-355

  Le Maire, Albane ^a,e   Weber, Thomas ^b,f   Saunier, Sophie ^b   Broutin, Isabelle ^a   Antignac, Corinne ^b,c   Ducruix, Arnaud ^a   Dardel, Frédéric ^a,d  

^a UNIVERSITÉ PARIS DESCARTES   (France)

^b INSERM   (France)

^c HÔPITAL NECKER ENFANTS MALADES   (France)

^d UNIVERSITÉ PARIS DESCARTES   (France)

^e DIF   (France)

^f HENKEL KGAA   (Germany)

Author keywords

Cell adhesion; Cytoskeleton; Kidney disease; NMR; Protein folding

Indexed keywords

ASPARAGINE; ASPARTIC ACID; GENE PRODUCT; GLUTAMIC ACID; NEPHROCYSTIN; PROLINE; SOLVENT; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; AUTOSOMAL RECESSIVE DISORDER; BINDING SITE; CELL ADHESION; CELL MOTILITY; CHRONIC KIDNEY FAILURE; CYTOSKELETON; GENE MUTATION; LIGAND BINDING; NEPHRONOPHTHISIS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN VARIANT; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAIN;

GENE EXPRESSION REGULATION; HUMANS; KIDNEY DISEASES, CYSTIC; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEINS; SRC HOMOLOGY DOMAINS;

EID: 16344363784     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20344     Document Type: Article

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