Oncogenic RET kinase domain mutations perturb the autophosphorylation trajectory by enhancing substrate presentation in trans

Molecular Cell

Volumn 53, Issue 5, 2014, Pages 738-751

  Plaza Menacho, Iván ^a   Barnouin, Karin ^a   Goodman, Kerry ^a,c   Martínez Torres, RubénJ ^a   Borg, Annabel ^a   Murray Rust, Judith ^a   Mouilleron, Stephane ^a   Knowles, Phillip ^a   McDonald, NeilQ ^a,b  

^a IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^b UNIVERSITY OF LONDON   (United Kingdom)

^c Columbia University ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTEIN RET;

ACTIVATION LOOP; ALPHA C HELIX; ALPHA HELIX; ARTICLE; AUTOPHOSPHORYLATION; BINDING AFFINITY; CARCINOGENESIS; CONTROLLED STUDY; DNA FLANKING REGION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; GLYCINE RICH LOOP; INSECT CELL; MASS SPECTROMETRY; NONHUMAN; POINT MUTATION; PROTEIN DOMAIN; QUANTITATIVE ANALYSIS; STRUCTURE ANALYSIS; WILD TYPE;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HUMANS; INSECTS; LIGANDS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-RET; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TIME FACTORS; TYROSINE;

EID: 84896714194     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.01.015     Document Type: Article

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