Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor?-Reference-Cited by-同舟云学术

Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor?

Published:2008-08-15 Issue:36 Volume:47 Page:9428-9446
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Beel Andrew J.¹,Mobley Charles K.¹,Kim Hak Jun¹,Tian Fang¹,Hadziselimovic Arina¹,Jap Bing¹,Prestegard James H.¹,Sanders Charles R.¹

Affiliation:

1. Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232-8725, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, and Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800993c

Reference99 articles.

1. A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60

2. Irvine, G. B., El-Agnaf, O. M., Shankar, G. M., and Walsh, D. M. (2008) Protein aggregation in the brain—the molecular basis for Alzheimer’s and Parkinson’s Diseases.Mol. Med.14, 451−464.

3. Protein Denaturation and Aggregation: Cellular Responses to Denatured and Aggregated Proteins

4. The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics

5. The Non-Amyloidogenic Pathway: Structure and Function of α-Secretases

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