Evidence map›Paper›PMID 37645886›Full record

ArticlebioRxiv : the preprint server for biology2023

Effects of phosphorylation on Drp1 activation by its receptors, actin, and cardiolipin.

Ao Liu, Anna L Hatch, Henry N Higgs

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

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ao LiuDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover NH 03755.
Anna L HatchDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover NH 03755.
Henry N HiggsDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover NH 03755.
Dartmouth College · US

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
Comparative molecular physiology of mammalian forminsR01GM069818 · NIGMS · DARTMOUTH COLLEGE · PI HIGGS, HENRY N · 2004 to 2017
$4.3M
NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R01 GM069818
6 · The paper itself

Abstract

Drp1 is a dynamin family GTPase that is required for mitochondrial and peroxisomal division, in which it oligomerizes into a ring and constricts the underlying membrane in a GTP hydrolysis-dependent manner. Oligomerization increases Drp1 GTPase activity through interactions between neighboring GTPase domains. In cells, Drp1 is regulated by several factors including Drp1 receptors, actin filaments, cardiolipin, and phosphorylation at two sites: S579 and S600. Phosphorylation of S579 is widely regarded as activating, while S600 phosphorylation is commonly considered inhibiting. However, the direct effects of phosphorylation on Drp1 GTPase activity have not been investigated in detail. In this study, we compare the effects of S579 and S600 phosphorylation on purified Drp1, using phospho-mimetic mutants and

Indexed as

CDKK38APKAS616S637

Identifiers

PMID37645886
PMCPMC10462108
OpenAlexW4386029413

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.