ReviewJournal of molecular neuroscience : MN2001
gamma-Secretase inhibitors as molecular probes of presenilin function.
Review in Journal of molecular neuroscience : MN, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 39 citations in OpenAlex.
- A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli.Scientific reports · 2019Article
- Differential spatial expression of peripheral olfactory neuron-derived BACE1 induces olfactory impairment by region-specific accumulation of β-amyloid oligomer.Cell death & disease · 2017Article
- CSF Presenilin-1 complexes are increased in Alzheimer's disease.Acta neuropathologica communications · 2013Article
- Regulation of innate and adaptive immunity by Notch.Nature reviews. Immunology · 2013Review
- Presenilin-dependent gamma-secretase-mediated control of p53-associated cell death in Alzheimer's disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Growth suppression of pre-T acute lymphoblastic leukemia cells by inhibition of notch signaling.Molecular and cellular biology · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Mutations in the presenilins cause Alzheimer's disease (AD) and alter gamma-secretase activity to increase the production of the 42-residue amyloid-beta peptide (Abeta) found disproportionally in the cerebral plaques that characterize the disease. The serpentine presenilins are required for transmembrane cleavage of both the amyloid-beta precursor protein (APP) and the Notch receptor by y-secretase, and presenilins are biochemically associated with the protease. Inhibitors of gamma-secretase have provided critical clues to the function of presenilins. Pharmacological profiling suggested that gamma-secretase is an aspartyl protease, leading to the identification of two conserved aspartates important to presenilin's role in proteolysis. Conversion of transition-state analogue inhibitors of gamma-secretase to affinity reagents resulted in specific tagging of the heterodimeric form of presenilins, strongly suggesting that the active site of gamma-secretase lies at the interface of the presenilin heterodimer. Heterodimeric presenilin appears to be the catalytic portion of a multi-protein gamma-secretase complex.
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.