ArticleProceedings of the National Academy of Sciences of the United States of America1998
Additional evidence for an eight-transmembrane-domain topology for Caenorhabditis elegans and human presenilins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 157 citations in OpenAlex.
- Article
- Non-Catalytic Roles of Presenilin Throughout Evolution.Journal of Alzheimer's disease : JAD · 2016Review
- 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
- Pharmacotherapeutic targets in Alzheimer's disease.Journal of cellular and molecular medicine · 2009Review
- Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Current Alzheimer research · 2008Review
- Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Current genomics · 2007Article
- Structural principles of intramembrane proteases.Current opinion in structural biology · 2007Review
- Alterations in presenilin 1 processing by amyloid-beta peptide in the rat retina.Experimental brain research · 2007Article
- Structure nor stability of the transmembrane spanning 6/7 domain of presenilin I correlates with pathogenicity.Biochemical and biophysical research communications · 2007Article
- 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
- Structure of the catalytic pore of gamma-secretase probed by the accessibility of substituted cysteines.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Electron microscopic structure of purified, active gamma-secretase reveals an aqueous intramembrane chamber and two pores.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Inhibition of gamma-secretase as a therapeutic intervention for Alzheimer's disease: prospects, limitations and strategies.CNS drugs · 2006Review
- 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
- Familial Alzheimer's disease presenilin 1 mutations cause alterations in the conformation of presenilin and interactions with amyloid precursor protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
- The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity.The EMBO journal · 2004Article
- The ins and outs of presenilin 1 membrane topology.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The presenilins turned inside out: implications for their structures and functions.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Presenilins have been implicated in the genesis of Alzheimer's disease and in facilitating LIN-12/Notch activity during development. All presenilins have multiple hydrophobic regions that could theoretically span a membrane, and a description of the membrane topology is a crucial step toward deducing the mechanism of presenilin function. Previously, we proposed an eight-transmembrane-domain model for presenilin, based on studies of the Caenorhabditis elegans SEL-12 presenilin. Here, we describe experiments that support the view that two of the hydrophobic regions of SEL-12 function as the seventh and eighth transmembrane domains. Furthermore, we have shown that human presenilin 1 behaves like SEL-12 presenilin when analyzed by our methods. Our results provide additional experimental support for the eight-transmembrane-domain model of presenilin topology.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.