Mutational studies of conserved residues in the dimer interface of nerve growth factor

Protein Science

Volumn 5, Issue 3, 1996, Pages 447-455

  Guo, Meihua ^a,c   Meyer, Sheryl L ^b   Kaur, Hardeep ^b   Gao, Jing Jin ^a,d   Neet, Kenneth E ^a  

^a The Chicago Medical College   (United States)

^b CEPHALON INC   (United States)

^c NORTHWESTERN MEMORIAL HOSPITAL   (United States)

^d UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

dimer; hydrophobic interaction; mutant, nerve growth factor; receptor binding; recombinant; structure; subunit contacts

Indexed keywords

NERVE GROWTH FACTOR; RECEPTOR SUBUNIT;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CELL SURVIVAL; CHOLINERGIC NERVE CELL; COMPUTER INTERFACE; DIMERIZATION; GENE MUTATION; GENETIC CONSERVATION; HUMAN; HUMAN CELL; HYDROPHOBICITY; MUTATION RATE; PRIORITY JOURNAL; RECEPTOR BINDING; RESIDUE ANALYSIS;

EID: 0029937850     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050306     Document Type: Article

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