Associated Papers
Specific Mutations in Aph1 Cause γ-Secretase Activation.
Watanabe H et al.
International Journal of Molecular Sciences, 2022
Contribution of the Presenilins in the cell biology, structure and function of γ-secretase.
Escamilla-Ayala A et al.
Seminars in Cell & Developmental Biology, 2020
Specific mutations in presenilin 1 cause conformational changes in γ-secretase to modulate amyloid β trimming.
Imai S et al.
Journal of Biochemistry, 2019
Suppressor Mutations for Presenilin 1 Familial Alzheimer Disease Mutants Modulate γ-Secretase Activities.
Futai E et al.
The Journal of Biological Chemistry, 2016
Mutations in nicastrin protein differentially affect amyloid beta-peptide production and Notch protein processing.
Pamrén A et al.
The Journal of Biological Chemistry, 2011
Gamma-secretase composed of PS1/Pen2/Aph1a can cleave notch and amyloid precursor protein in the absence of nicastrin.
Zhao G et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2010
Nicastrin is dispensable for gamma-secretase protease activity in the presence of specific presenilin mutations.
Futai E et al.
The Journal of Biological Chemistry, 2009
Hydrophilic loop 1 of Presenilin-1 and the APP GxxxG transmembrane motif regulate γ-secretase function in generating Alzheimer-causing Aβ peptides.
Liu L et al.
The Journal of Biological Chemistry, 0
Select a paper to view details