ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1996
STEP61: a member of a family of brain-enriched PTPs is localized to the endoplasmic reticulum.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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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
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Who cites it
41 citing papers in PubMed, 79 citations in OpenAlex.
- Impairment of neuronal tyrosine phosphatase STEP worsens post-ischemic inflammation and brain injury under hypertensive condition.Journal of neuroinflammation · 2024Article
- Uncovering the Significance of STEP61 in Alzheimer's Disease: Structure, Substrates, and Interactome.Cellular and molecular neurobiology · 2023Review
- The Implication of STEP in Synaptic Plasticity and Cognitive Impairments in Alzheimer's Disease and Other Neurological Disorders.Frontiers in cell and developmental biology · 2021Review
- Insight into the Role of the STriatal-Enriched Protein Tyrosine Phosphatase (STEP) in AFrontiers in pharmacology · 2021Article
- Regulation of glutamate receptors by striatal-enriched tyrosine phosphatase 61 (STEPThe Journal of physiology · 2021Review
- The STEPProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Altered Intracellular Calcium Homeostasis Underlying Enhanced Glutamatergic Transmission in Striatal-Enriched Tyrosine Phosphatase (STEP) Knockout Mice.Molecular neurobiology · 2018Article
- Inhibition of STEPMolecular psychiatry · 2018Article
- Use of Peptides for the Management of Alzheimer's Disease: Diagnosis and Inhibition.Frontiers in aging neuroscience · 2018Review
- PSD-95 stabilizes NMDA receptors by inducing the degradation of STEP61.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Aging is associated with dimerization and inactivation of the brain-enriched tyrosine phosphatase STEP.Neurobiology of aging · 2016Article
- Inhibition of the tyrosine phosphatase STEP61 restores BDNF expression and reverses motor and cognitive deficits in phencyclidine-treated mice.Cellular and molecular life sciences : CMLS · 2016Article
- Down-regulation of BDNF in cell and animal models increases striatal-enriched protein tyrosine phosphatase 61 (STEP61 ) levels.Journal of neurochemistry · 2016Article
- Molecular underpinnings of neurodegenerative disorders: striatal-enriched protein tyrosine phosphatase signaling and synaptic plasticity.F1000Research · 2016Review
- Role of Striatal-Enriched Tyrosine Phosphatase in Neuronal Function.Neural plasticity · 2016Review
- Striatal-enriched protein tyrosine phosphatase regulates the PTPα/Fyn signaling pathway.Journal of neurochemistry · 2015Article
- Disruption of striatal-enriched protein tyrosine phosphatase (STEP) function in neuropsychiatric disorders.Neuroscience research · 2014Review
- Rapid regulation of endoplasmic reticulum dynamics in dendritic spines by NMDA receptor activation.Molecular brain · 2014Article
- Inhibitor of the tyrosine phosphatase STEP reverses cognitive deficits in a mouse model of Alzheimer's disease.PLoS biology · 2014Article
- Neuroprotective role of a brain-enriched tyrosine phosphatase, STEP, in focal cerebral ischemia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The STEP family of protein tyrosine phosphatases is highly enriched within the CNS. Members of this family are alternatively spliced to produce both transmembrane and cytosolic variants. This manuscript describes the distinctive intracellular distribution and enzymatic activity of the membrane-associated isoform STEP61. Transfection experiments in fibroblasts, as well as subcellular fractionations, sucrose density gradients, immunocytochemical labeling, and electron microscopy in brain tissue, show that STEP61 is an intrinsic membrane protein of striatal neurons and is associated with the endoplasmic reticulum. In addition, structural analysis of the novel N-terminal region of STEP61 reveals several motifs not present in the cytosolic variant STEP46. These include two putative transmembrane domains, two sequences rich in Pro, Glu, Asp, Ser, and Thr (PEST sequences), and two polyproline-rich domains. Like STEP46, STEP61 is enriched in the brain, but the recombinant protein has less enzymatic activity than STEP46. Because STEP46 is contained in its entirety within STEP61 and differs only in the extended N terminus of STEP61, this amino acid sequence is responsible for the association of STEP61 with membrane compartments and may also regulate its enzymatic activity.
Indexed as
Identifiers
8987810PMC6579237W2149875160What 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.