Evidence map›Paper›PMID 26733158›Full record

ReviewBiological chemistry2016

Functional organization of human SAMHD1 and mechanisms of HIV-1 restriction.

Jinwoo Ahn

Open access · greenAbstract readReview
In one paragraph

Review in Biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. SAMHD1 in cancer: curse or cure?Journal of molecular medicine (Berlin, Germany) · 2022
    Review
  5. Aicardi-Goutières Syndrome due to aMolecular syndromology · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Mechanisms of HIV-1 Control.Current HIV/AIDS reports · 2017
    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

1 author at 1 institution in 1 country.

Jinwoo Ahn
University of Pittsburgh · US

Funding

Structure and function relationships regulating SAMHD1's dual enzymatic activitiesR01GM116642 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI AHN, JINWOO · 2015 to 2018
$1.4M
NIGMS NIH HHS GM116642NIGMS NIH HHS R01 GM116642
6 · The paper itself

Abstract

Sterile alpha motif and histidine-aspartate domain containing protein 1 (SAMHD1) is a triphosphohydrolase that catalyzes the conversion of deoxyribonucleoside triphosphate to deoxyribonucleoside and triphosphate. SAMHD1 has been a recent focus of study since it was identified as a potent human immunodeficiency virus-1 (HIV-1) restriction factor in the intrinsic antiviral immune system. Recent biochemical and biological studies have suggested that SAMHD1 restricts HIV-1 infection in non-cycling cells by limiting the pool of deoxyribonucleoside triphosphates, thereby interfering with HIV-1 reverse transcription. SAMHD1 also possesses single-stranded DNA and RNA binding activity, with reported nuclease activity, conferring additional HIV-1 restriction function. This review summarizes current knowledge regarding the structure of SAMHD1 and the regulation of its function in HIV-1 restriction.

Indexed as

HIV-1HIV InfectionsHumansMonomeric GTP-Binding ProteinsSAM Domain and HD Domain-Containing Protein 1Monomeric GTP-Binding ProteinsSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, human

Identifiers

PMID26733158
PMCPMC4939630
OpenAlexW2413421775

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.