The infective polymerization of conformationally unstable antithrombin mutants may play a role in the clinical severity of antithrombin deficiency.

Molecular medicine (Cambridge, Mass.)

Volumn 18, Issue , 2012, Pages 762-770

  Martínez Martínez, Irene ^a   Navarro Fernández, José ^b   Aguila, Sonia ^b   Miñano, Antonia ^b   Bohdan, Nataliya ^b   De La Morena Barrio, María Eugenia ^b   Ordóñez, Adriana ^b   Martínez, Constantino ^b   Vicente, Vicente ^b   Corral, Javier ^b  

^a UNIVERSITY OF MURCIA   (Spain)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBIN; ANTITHROMBIN LONDON; MUTANT PROTEIN;

ANTITHROMBIN III DEFICIENCY; ARTICLE; CELL LINE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PHYSIOLOGICAL STRESS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STABILITY;

ANTITHROMBIN III DEFICIENCY; ANTITHROMBIN PROTEINS; CELL LINE; HUMANS; MUTANT PROTEINS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; STRESS, PHYSIOLOGICAL;

EID: 84874764654     PISSN: None     EISSN: 15283658     Source Type: Journal    
DOI: 10.2119/molmed.2012.00017     Document Type: Article

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