Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity.

Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity. Research Abstract Details 

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Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity. Abstract Text:

Brian Jeppesen,Laura Costello,Adam Fung,Erin Stanley,Jessica McDonald,Abbie Lambert,Bennett Johnson,Lisa Gentile,

Since its cloning in 1995, missense point mutations in presenilin I (PS-I) have been shown to be responsible for greater than 70% of the cases of early onset familial Alzheimer's disease (EOFAD), which can affect individuals as early as age 18. PS-I is known to be a component of gamma-secretase, the enzyme responsible for cleavage of the amyloid precursor protein (APP) into 42 amino acid peptides that aggregate to form the plaques surrounding neurons of Alzheimer's patients. It has recently been hypothesized that wild-type (wt) PS-I contains an autoinhibitory module that prevents gamma-secretase cleavage of the APP, while pathogenic PS-I point mutants lack a structure necessary for this inhibition. In this work, spectroscopic data is presented that does not correlate structure or stability of the proposed PS-I autoinhibitory module with pathogenicity.

Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity. Publishing Authors By Initials

B Jeppesen,L Costello,A Fung,E Stanley,J McDonald,A Lambert,B Johnson,L Gentile,

For similar investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research abstracts see: investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research

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Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Biochemical and biophysical research communication

VOLUME: 355

Page Numbers: 820-4

Journal Abbreviation: Biochem. Biophys. Res. Commun.

ISSN: 0006-291X

DAY: 15

MONTH: 02

YEAR: 2007

Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 372516

Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity. Keywords Mesh Terms:

KEYWORDS: Spectrometry, Fluorescence

MESH TERMS: genetics

Chemical & Substance for Abstract: Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity. Information

Substance Name: Presenilin-1

Registry Number: 0

Grant and Affiliation Information for Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity.

AFFILIATION: Department of Chemistry, Western Washington University, Bellingham, WA 98225-9150, USA.

Country: United States

AGENCY: United States NIA

GRANT: R15 AG017032-03

ACRONYM: AG

MEDLINETA: Biochem Biophys Res Commun

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