Evidence map›Paper›PMID 35974043›Full record

ArticleCommunications biology2022

Structural features of Dnase1L3 responsible for serum antigen clearance.

Jon J McCord, Minal Engavale, Elahe Masoumzadeh, Johanna Villarreal, Britney Mapp, Michael P Latham, Peter A Keyel, R Bryan Sutton

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Nanomaterials-Based Immunotherapy for Atherosclerosis.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Review
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  13. A novel DNase assay reveals low DNase activity in severe asthma.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
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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

8 authors at 1 institution in 1 country.

Jon J McCordTexas Tech University Health Sciences Center, Dept of Cell Physiology and Molecular Biophysics, Lubbock, TX, USA.ORCID 0000-0002-8816-1022
Minal EngavaleTexas Tech University, Dept. of Biological Sciences, Lubbock, TX, USA.
Elahe MasoumzadehTexas Tech University, Dept. of Chemistry & Biochemistry, Lubbock, TX, USA.
Johanna VillarrealTexas Tech University Health Sciences Center, Dept of Cell Physiology and Molecular Biophysics, Lubbock, TX, USA.
Britney MappTexas Tech University, Dept. of Biological Sciences, Lubbock, TX, USA.
Michael P LathamTexas Tech University, Dept. of Chemistry & Biochemistry, Lubbock, TX, USA.ORCID 0000-0002-2209-5798
Peter A KeyelTexas Tech University, Dept. of Biological Sciences, Lubbock, TX, USA.ORCID 0000-0001-8637-8538
R Bryan SuttonTexas Tech University Health Sciences Center, Dept of Cell Physiology and Molecular Biophysics, Lubbock, TX, USA. roger.b.sutton@ttuhsc.edu.ORCID 0000-0001-8393-5239
Texas Tech University · US

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
Structural Biology Studies of a Large DNA Repair ComplexR35GM128906 · NIGMS · UNIVERSITY OF MINNESOTA · PI Michael Parker Latham · 2018 to 2026
$3.1M
NIGMS NIH HHS P30 GM133894NIGMS NIH HHS R35 GM128906
6 · The paper itself

Abstract

Autoimmunity develops when extracellular DNA released from dying cells is not cleared from serum. While serum DNA is primarily digested by Dnase1 and Dnase1L3, Dnase1 cannot rescue autoimmunity arising from Dnase1L3 deficiencies. Dnase1L3 uniquely degrades antigenic forms of cell-free DNA, including DNA complexed with lipids and proteins. The distinct activity of Dnase1L3 relies on its unique C-terminal Domain (CTD), but the mechanism is unknown. We used multiple biophysical techniques and functional assays to study the interplay between the core catalytic domain and the CTD. While the core domain resembles Dnase1, there are key structural differences between the two enzymes. First, Dnase1L3 is not inhibited by actin due to multiple differences in the actin recognition site. Second, the CTD augments the ability of the core to bind DNA, thereby facilitating the degradation of complexed DNA. Together, these structural insights will inform the development of Dnase1L3-based therapies for autoimmunity.

Indexed as

ActinsEndodeoxyribonucleasesDNAActinsDNAEndodeoxyribonucleases

Identifiers

PMID35974043
PMCPMC9381713
OpenAlexW4292004599

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.