tallózása szerző szerint "Sorum, Ben"

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Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions

Sorum, Ben; Törőcsik, Beáta; Csanády, László (2017)

CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, is opened by ATP binding to two cytosolic nucleotide binding domains (NBDs), but pore-domain mutations may also impair gating. ATP-bound NBDs dimerize ...
Timing of CFTR Pore Opening and Structure of Its Transition State

Sorum, Ben; Czégé, Dávid; Csanády, László (2015)

In CFTR, the chloride ion channel mutated in cystic fibrosis (CF) patients, pore opening is coupled to ATP-binding-induced dimerization of two cytosolic nucleotide binding domains (NBDs) and closure to dimer disruption ...
Timing of motions in the CFTR channel protein during pore opening

Sorum, Ben (2017)

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