Article in Proteins, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it
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.
2 · The registry
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.
Liliana GuerreroStructural Biology Initiative, CUNY Advanced Science Research Center, New York, New York, USA.ORCID 0000-0003-1742-577X
Ali EbrahimStructural Biology Initiative, CUNY Advanced Science Research Center, New York, New York, USA.ORCID 0000-0003-2661-381X
Blake T RileyStructural Biology Initiative, CUNY Advanced Science Research Center, New York, New York, USA.ORCID 0000-0003-2176-0503
Sean H KimDepartment of Chemistry, Amherst College, Amherst, Massachusetts, USA.ORCID 0009-0002-7125-1280
Anthony C BishopDepartment of Chemistry, Amherst College, Amherst, Massachusetts, USA.ORCID 0000-0001-8394-280X
Jiaqian WuSanford Burnham Prebys Medical Discovery Institute, NCI-Designated Cancer Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California, USA.ORCID 0009-0004-5987-886X
Ye Na HanSanford Burnham Prebys Medical Discovery Institute, NCI-Designated Cancer Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California, USA.ORCID 0000-0001-6264-9604
Lutz TautzSanford Burnham Prebys Medical Discovery Institute, NCI-Designated Cancer Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California, USA.ORCID 0000-0002-4075-6238
Daniel A KeedyStructural Biology Initiative, CUNY Advanced Science Research Center, New York, New York, USA.ORCID 0000-0002-9184-7586
Funding
Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI ELENA B PASQUALE · 1985 to 2026
$107.2M
Training and OutreachP30GM124166 · NIGMS · CORNELL UNIVERSITY · PI RICHARD A. CERIONE · 2019 to 2026
$28.3M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
G-RISE: Graduate Research Initiative for Student Advancement at The City College of New YorkT32GM136499 · NIGMS · CITY COLLEGE OF NEW YORK · PI RUTH E. STARK · 2020 to 2026
$4.9M
Fragment-Based Discovery of STEP Modulators in Alzheimer's Disease Administrative SupplementRF1AG087011 · NIA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI COSFORD, NICHOLAS DAVID, TAUTZ, LUTZ · 2024 to 2025
$2.9M
Nanuq Cryocooling SystemR35GM133769 · NIGMS · ADVANCED SCIENCE RESEARCH CENTER · PI Daniel A Keedy · 2019 to 2026
$2.9M
Development of STEP Allosteric Inhibitors as Novel Therapeutics for Alzheimer's DiseaseR01AG065387 · NIA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI TAUTZ, LUTZ · 2020 to 2022
$2.7M
Target-specific inhibition and activation of protein tyrosine phosphatasesR15GM071388 · NIGMS · AMHERST COLLEGE · PI BISHOP, ANTHONY C · 2005 to 2021
$1.6M
Development of STEP substrates and probes as novel tools and therapeutics for Alzheimer's diseaseR21AG067155 · NIA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI TAUTZ, LUTZ · 2020 to 2020
Protein tyrosine phosphatases (PTPs) play pivotal roles in myriad cellular processes by counteracting protein tyrosine kinases. Striatal-enriched protein tyrosine phosphatase (STEP, PTPN5) regulates synaptic function and neuronal plasticity in the brain and is a therapeutic target for several neurological disorders. Here, we present three new crystal structures of STEP, each with unexpected features. These include high-resolution conformational heterogeneity at multiple sites, a highly coordinated citrate molecule in the active site, a previously unseen conformational change at an allosteric site, an intramolecular disulfide bond that was characterized biochemically but had never been visualized structurally, and two serendipitous covalent ligand binding events at surface-exposed cysteines that are nearly or entirely unique to STEP among human PTPs. Together, our results offer new views of the conformational landscape of STEP that may inform structure-based design of allosteric small molecules to specifically inhibit this biomedically important enzyme.
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.
Three STEPs Forward: A Trio of Unexpected Structures of PTPN5. · full record | OpenQuestion