Evidence map›Paper›PMID 36398895›Full record

ArticleBiochemistry2022

Dynamic Long-Range Interactions Influence Substrate Binding and Catalysis by Human Histidine Triad Nucleotide-Binding Proteins (HINTs), Key Regulators of Multiple Cellular Processes and Activators of Antiviral ProTides.

Alexander Strom, Rachit Shah, Rafal Dolot, Melanie S Rogers, Cher-Ling Tong, David Wang, Youlin Xia, John D Lipscomb, Carston R Wagner

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2022. 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
0.1field-weighted citation impact, top 56% of its field
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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. The Many Faces of Histidine Triad Nucleotide Binding Protein 1 (HINT1).ACS pharmacology & translational science · 2023
    Review
4 · The record

Corrections and comments

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 at 3 institutions in 2 countries.

Alexander StromDepartment of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota55455, United States.
Rachit ShahDepartment of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota55455, United States.
Rafal DolotCentre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Sienkiewicza 112, 90-363Lodz, Poland.
Melanie S RogersDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota55455, United States.ORCID 0000-0002-2657-7065
Cher-Ling TongDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota55455, United States.
David WangDepartment of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota55455, United States.
Youlin XiaDepartment of Structural Biology, St. Jude's Research Hospital, Memphis, Tennessee38105, United States.
John D LipscombDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota55455, United States.ORCID 0000-0002-8158-5594
Carston R WagnerDepartment of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota55455, United States.ORCID 0000-0001-7927-719X
University of Minnesota · USCentrum Badań Molekularnych i Makromolekularnych Polskiej Akademii Nauk · PLSt. Jude Children's Research Hospital · US

Funding

Anchimerically Activatable Anti-Zika/Dengue ProTidesR01AI146049 · NIAID · UNIVERSITY OF MINNESOTA · PI WAGNER, CARSTON R. · 2021 to 2025
$2.9M
Intermediates in O2 Activation by Oxygenases at Non-heme Iron CentersR35GM118030 · NIGMS · UNIVERSITY OF MINNESOTA · PI LIPSCOMB, JOHN D · 2016 to 2020
$2.7M
NIAID NIH HHS R01 AI146049NIGMS NIH HHS R35 GM118030
6 · The paper itself

Abstract

Human histidine triad nucleotide-binding (hHINT) proteins catalyze nucleotide phosphoramidase and acyl-phosphatase reactions that are essential for the activation of antiviral proTides, such as Sofosbuvir and Remdesivir. hHINT1 and hHINT2 are highly homologous but exhibit disparate roles as regulators of opioid tolerance (hHINT1) and mitochondrial activity (hHINT2). NMR studies of hHINT1 reveal a pair of dynamic surface residues (Q62, E100), which gate a conserved water channel leading to the active site 13 Å away. hHINT2 crystal structures identify analogous residues (R99, D137) and water channel. hHINT1 Q62 variants significantly alter the steady-state

Indexed as

Antiviral AgentsHistidineAnalgesics, OpioidCatalysisDrug ToleranceHumansKineticsNucleotidesAnalgesics, OpioidAntiviral AgentsHistidineNucleotides

Identifiers

PMID36398895
PMCPMC9854251
OpenAlexW4309288356

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.