Revealing the effects of missense mutations causing snyder-robinson syndrome on the stability and dimerization of spermine synthase

International Journal of Molecular Sciences

Volumn 17, Issue 1, 2016, Pages

  Peng, Yunhui ^a   Norris, Joy ^b   Schwartz, Charles ^b   Alexov, Emil ^a  

^a CLEMSON UNIVERSITY   (United States)

^b GREENWOOD GENETIC CENTER   (United States)

Author keywords

Binding affinity charge; Energy calculations; Missense mutation; Snyder Robinson syndrome; Spermine synthase

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; SPERMINE SYNTHASE;

ALGORITHM; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BLOOD ANALYSIS; CATALYSIS; CELL LYSATE; COMPUTER ANALYSIS; CONTROLLED STUDY; DIMERIZATION; ENZYME STABILITY; GEL ELECTROPHORESIS; GENE MUTATION; GENETIC DISORDER; HUMAN; HUMAN CELL; MISSENSE MUTATION; MULTIPLE SEQUENCE ALIGNMENT ANALYSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN STRUCTURE; PROTEOMICS; SEQUENCE ANALYSIS; SNYDER ROBINSON SYNDROME; WESTERN BLOTTING; AMINO ACID SEQUENCE; CHEMISTRY; COMPUTER SIMULATION; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; MOLECULAR MODEL; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; SEQUENCE ALIGNMENT; X LINKED MENTAL RETARDATION;

AMINO ACID SEQUENCE; COMPUTER SIMULATION; ENZYME STABILITY; HUMANS; MENTAL RETARDATION, X-LINKED; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION, MISSENSE; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; SEQUENCE ALIGNMENT; SPERMINE SYNTHASE;

EID: 84954198602     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms17010077     Document Type: Article

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