BONE MORPHOGENETIC PROTEIN;
BONE MORPHOGENETIC PROTEIN INHIBITOR;
CHORDIN;
IMMUNOGLOBULIN;
PROTEIN INHIBITOR;
SUPEROXIDE DISMUTASE;
UNCLASSIFIED DRUG;
BACTERIAL PROTEIN;
GLYCOPROTEIN;
SIGNAL PEPTIDE;
AMINO ACID SEQUENCE;
DATA BASE;
HUMAN;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN STRUCTURE;
REVIEW;
SEQUENCE HOMOLOGY;
STRUCTURE ANALYSIS;
TANDEM REPEAT;
CHEMISTRY;
DRUG ANTAGONISM;
GENETICS;
MOLECULAR GENETICS;
PROTEIN TERTIARY STRUCTURE;
SEQUENCE ALIGNMENT;
AMINO ACID SEQUENCE;
BACTERIAL PROTEINS;
BONE MORPHOGENETIC PROTEINS;
GLYCOPROTEINS;
INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS;
MOLECULAR SEQUENCE DATA;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
Genomic organisation of the human chordin gene and mutation screening of candidate Cornelia de Lange syndrome genes
Smith M., et al. Genomic organisation of the human chordin gene and mutation screening of candidate Cornelia de Lange syndrome genes. Hum. Genet. 205:1999;104-111.
Cleavage of chordin by Xolloid metalloprotease suggests a role for proteolytic processing in the regulation of Spemann organizer activity
Piccolo S., et al. Cleavage of chordin by Xolloid metalloprotease suggests a role for proteolytic processing in the regulation of Spemann organizer activity. Cell. 91:1997;407-416.
FUGUE: Sequence-structure homology recognition using environment- specific substitution tables and structure-dependent gap penalties
Shi J., et al. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310:2001;243-257.
The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
Thompson J.D., et al. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24:1997;4876-4882.