The metastasis-promoting phosphatase PRL-3 shows activity toward phosphoinositides

Biochemistry

Volumn 50, Issue 35, 2011, Pages 7579-7590

  McParland, Victoria ^a   Varsano, Giulia ^a   Li, Xun ^b   Thornton, Janet ^b   Baby, Jancy ^a   Aravind, Ajay ^a   Meyer, Christoph ^a   Pavic, Karolina ^a   Rios, Pablo ^a   Köhn, Maja ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b WELLCOME TRUST SANGER INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ASSAY; BIOLOGICAL FUNCTIONS; CANCER METASTASIS; CATALYTIC MOTIF; CELL MIGRATION; CELLULAR PHENOTYPES; DEPHOSPHORYLATIONS; HEK293 CELLS; IN-VITRO; INACTIVE MUTANTS; MOLECULAR DETERMINANTS; MOLECULAR DOCKING; NATURAL SUBSTRATES; PHOSPHATASE ACTIVITY; PHOSPHATASE OF REGENERATING LIVERS; PHOSPHATIDYLINOSITOL; PHOSPHOINOSITIDES; PHOSPHOPEPTIDES; PROTEIN SUBSTRATE; STRUCTURAL STABILITIES; SUBSTRATE SPECIFICITY; THERAPEUTIC TARGETS; WILD TYPES;

CELL CULTURE; DISEASES; PATHOLOGY; PHOSPHATASES; PHOSPHOLIPIDS; STABILITY;

SUBSTRATES;

3 METHOXYFLUORESCEIN PHOSPHATE; ALANINE; CYSTEINE; GLUTAMINE; PHOSPHATASE OF REGENERATING LIVER 3; PHOSPHATE; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE PHOSPHODIESTERASE; PHOSPHATIDYLINOSITOL 5 PHOSPHATASE; PHOSPHOPEPTIDE; PHOSPHOPROTEIN PHOSPHATASE; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BIOASSAY; CANCER CELL CULTURE; CATALYSIS; CELL MIGRATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; GENETIC VARIABILITY; HUMAN; HUMAN CELL; IN VITRO STUDY; METASTASIS; MOLECULAR BIOLOGY; MOLECULAR DOCKING; MUTANT; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN MOTIF; PROTEIN STABILITY; WILD TYPE;

AMINO ACID SEQUENCE; CATALYSIS; CELL MOVEMENT; CYSTEINE; ENZYME ACTIVATION; GENETIC VARIATION; HEK293 CELLS; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; NEOPLASM INVASIVENESS; NEOPLASM PROTEINS; PHOSPHATIDYLINOSITOLS; PROTEIN TYROSINE PHOSPHATASES; RECOMBINANT PROTEINS; SERINE; SUBSTRATE SPECIFICITY;

PIPS;

EID: 80052245816     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201095z     Document Type: Article

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