William Taylor Kimberly, Ph.D., M.D.
This page shows the publications co-authored by William Kimberly and Dennis Selkoe.
Physiological regulation of the beta-amyloid precursor protein signaling domain by c-Jun N-terminal kinase JNK3 during neuronal differentiation. J Neurosci. 2005 Jun 08; 25(23):5533-43.
Gamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2. Proc Natl Acad Sci U S A. 2003 May 27; 100(11):6382-7.
Complex N-linked glycosylated nicastrin associates with active gamma-secretase and undergoes tight cellular regulation. J Biol Chem. 2002 Sep 20; 277(38):35113-7.
The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J Biol Chem. 2001 Oct 26; 276(43):40288-92.
The transmembrane aspartates in presenilin 1 and 2 are obligatory for gamma-secretase activity and amyloid beta-protein generation. J Biol Chem. 2000 Feb 04; 275(5):3173-8.
Assembly of the gamma-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin. J Biol Chem. 2003 Sep 26; 278(39):37213-22.
Notch and the amyloid precursor protein are cleaved by similar gamma-secretase(s). Biochemistry. 2003 Jan 14; 42(1):137-44.
Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid beta-protein generation. Proc Natl Acad Sci U S A. 2000 Aug 01; 97(16):9299-304.
Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature. 1999 Apr 08; 398(6727):513-7.
Presenilin 1 regulates the processing of beta-amyloid precursor protein C-terminal fragments and the generation of amyloid beta-protein in endoplasmic reticulum and Golgi. Biochemistry. 1998 Nov 24; 37(47):16465-71.
Activity-dependent isolation of the presenilin- gamma -secretase complex reveals nicastrin and a gamma substrate. Proc Natl Acad Sci U S A. 2002 Mar 05; 99(5):2720-5.
Transition-state analogue inhibitors of gamma-secretase bind directly to presenilin-1. Nat Cell Biol. 2000 Jul; 2(7):428-34.
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