Evidence map›Paper›PMID 29379009›Full record

ArticleNature communications2018

The SAM domain of mouse SAMHD1 is critical for its activation and regulation.

Olga Buzovetsky, Chenxiang Tang, Kirsten M Knecht, Jenna M Antonucci, Li Wu, Xiaoyun Ji, Yong Xiong

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 16 citations in OpenAlex.

  1. Transition State Analysis of SAMHD1 from PrimaryJournal of the American Chemical Society · 2025
    Article
  2. Article
  3. Review
  4. Sticky, Adaptable, and Many-sided: SAM protein versatility in normal and pathological hematopoietic states.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
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

7 authors at 2 institutions in 1 country.

Olga BuzovetskyDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Chenxiang TangDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Kirsten M KnechtDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Jenna M AntonucciCenter of Retrovirus Research, Department of Veterinary Biosciences, The Ohio State University, Columbus, OH, 43210, USA.
Li WuCenter of Retrovirus Research, Department of Veterinary Biosciences, The Ohio State University, Columbus, OH, 43210, USA.ORCID http://orcid.org/0000-0002-5468-2487
Xiaoyun JiThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, Jiangsu, 210023, China. xiaoyun.ji@nju.edu.cn.
Yong XiongDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA. yong.xiong@yale.edu.
Yale University · USThe Ohio State University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
Viral Hijacking of Host Membrane Trafficking PathwaysR01AI102778 · NIAID · YALE UNIVERSITY · PI GUATELLI, JOHN C., XIONG, YONG · 2013 to 2017
$3.0M
Mechanisms of SAMHD1-mediated HIV-1 restriction in dendritic cellsR01AI104483 · NIAID · OHIO STATE UNIVERSITY · PI WU, LI · 2013 to 2016
$1.5M
Molecular basis of HIV restriction by SAMHD1K99AI120845 · NIAID · YALE UNIVERSITY · PI JI, XIAOYUN · 2015 to 2016
$209k
NIAID NIH HHS K99 AI120845NIAID NIH HHS R01 AI102778NIAID NIH HHS R01 AI104483NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32 GM008283
6 · The paper itself

Abstract

Human SAMHD1 (hSAMHD1) is a retroviral restriction factor that blocks HIV-1 infection by depleting the cellular nucleotides required for viral reverse transcription. SAMHD1 is allosterically activated by nucleotides that induce assembly of the active tetramer. Although the catalytic core of hSAMHD1 has been studied extensively, previous structures have not captured the regulatory SAM domain. Here we report the crystal structure of full-length SAMHD1 by capturing mouse SAMHD1 (mSAMHD1) structures in three different nucleotide bound states. Although mSAMHD1 and hSAMHD1 are highly similar in sequence and function, we find that mSAMHD1 possesses a more complex nucleotide-induced activation process, highlighting the regulatory role of the SAM domain. Our results provide insights into the regulation of SAMHD1 activity, thereby facilitating the improvement of HIV mouse models and the development of new therapies for certain cancers and autoimmune diseases.

Indexed as

Allosteric SiteAnimalsCrystallography, X-RayHydrolysisMiceModels, MolecularProtein DomainsProtein MultimerizationSAM Domain and HD Domain-Containing Protein 1SAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, humanSamhd1 protein, mouse

Identifiers

PMID29379009
PMCPMC5788916
OpenAlexW2767041233

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.