Article in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
0numbers the graph read from it
0cells of the map it votes in
3citing 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.
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what money
Authors and funding
9 authors.
Matthew EglestonDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, United States.ORCID 0000-0002-6601-7425
Shridhar BhatDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, United States.
A Hasan HowladerDepartment of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218, United States.
Mario A BianchetDepartment of Biophysics & Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, United States.
Yi LiuDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, United States.
Laura Maria Lopez RoviraDepartment of Biophysics & Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, United States.
Brandon SmithDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, United States.
Marc M GreenbergDepartment of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218, United States.ORCID 0000-0002-5786-6118
James T StiversDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, United States.ORCID 0000-0003-2572-7807
Funding
X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Vivian Stojanoff · 2019 to 2026
$38.6M
PHARMACOLOGY TRAINING GRANTT32GM008763 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FREEL MEYERS, CAREN L. · 2000 to 2019
$6.1M
How Damaged DNA Forms, and its Subsequent Chemistry: Fundamental Studies and ApplicationsR35GM131736 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MARC M GREENBERG · 2019 to 2026
$4.3M
Pharmacology and Molecular Sciences Training Program: Enhancing Inclusivity Through Universal Design for Learning in Graduate CoursesT32GM135083 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Caren L. Freel Meyers · 2020 to 2026
$3.3M
Discovery of Chemical Probes of SAMHD1 for Modulation of Cancer Therapy and the Immune SystemR01CA233567 · NCI · JOHNS HOPKINS UNIVERSITY · PI STIVERS, JAMES T. · 2020 to 2023
$1.5M
Acquisition of a 500 MHz NMR Spectrometer to Support Small-Molecule Chemistry at Johns Hopkins Medical SchoolS10OD034217 · OD · JOHNS HOPKINS UNIVERSITY · PI BHAT, SHRIDHAR · 2024 to 2024
Sterile alpha motif histidine-aspartate domain protein 1 (SAMHD1) is an enzyme with diverse activities. Its dNTPase activity degrades all canonical dNTPs and many anticancer nucleoside drugs, while its single-stranded nucleic acid binding activity promotes DNA repair and RNA homeostasis in cells. These functions require guanine nucleotide binding to a specific allosteric site (A1) on the enzyme. We previously described how the activities of SAMHD1 could be inhibited in vitro with fragment-based inhibitor design, using dGMP as a targeting fragment for the A1 site. However, these dGMP-tethered inhibitors had poor cell permeability due to the charged guanine monophosphate group. Here, we describe a new approach where the amino form of the guanine acyclic nucleoside acyclovir (NH
Indexed as
AcyclovirAntiviral AgentsEnzyme InhibitorsSAM Domain and HD Domain-Containing Protein 1Allosteric SiteGuanineHumansAcyclovirAntiviral AgentsEnzyme InhibitorsGuanineSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, human
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.
Inhibitors of SAMHD1 Obtained from Chemical Tethering to the Guanine Antiviral Acyclovir. · full record | OpenQuestion