ArticleProceedings of the National Academy of Sciences of the United States of America2004
The presenilins turned inside out: implications for their structures and functions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- Intraperitoneal injection of JNK-specific inhibitor SP600125 inhibits the expression of presenilin-1 and Notch signaling in mouse brain without induction of apoptosis.Brain research · 2012Article
- Structural investigation of the C-terminal catalytic fragment of presenilin 1.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- BACE and gamma-secretase characterization and their sorting as therapeutic targets to reduce amyloidogenesis.Neurochemical research · 2010Review
- Antibody library-based tumor endothelial cells surface proteomic functional screen reveals migration-stimulating factor as an anti-angiogenic target.Molecular & cellular proteomics : MCP · 2009Article
- Analysis of transcriptional modulation of the presenilin 1 gene promoter by ZNF237, a candidate binding partner of the Ets transcription factor ERM.Brain research · 2007Article
- An early specific cell-cell interaction occurs in the production of beta-amyloid in cell cultures.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Evidence that the COOH terminus of human presenilin 1 is located in extracytoplasmic space.American journal of physiology. Cell physiology · 2005Article
- CD147 is a regulatory subunit of the gamma-secretase complex in Alzheimer's disease amyloid beta-peptide production.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Processing of Notch and amyloid precursor protein by gamma-secretase is spatially distinct.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The ins and outs of presenilin 1 membrane topology.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The presenilin (PS) proteins are polytopic integral membrane proteins that are critically involved in the development of Alzheimer's disease. The topography of the PS molecule in the endoplasmic reticulum membrane is widely accepted as exhibiting eight-hydrophobic-transmembrane (8-TM) helices. We have previously provided evidence, however, that the intact PS molecule is also present in the cell surface where it exhibits exclusively a 7-TM topography, which differs in significant structural features from the 8-TM model. This evidence, however, has been disparaged and generally rejected by researchers in Alzheimer's disease. The 7-TM model is definitively demonstrated in the present study for PS-1 at the surfaces of PS-1-transfected cells and for endogenous PS-1 at the surfaces of untransfected cells, by immunofluorescence studies using mAbs. These studies force substantial revision of current views of the structural and functional properties of the PS proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.