Evidence map›Paper›PMID 30135210›Full record

ArticleThe Journal of biological chemistry2018

The erlin2 T65I mutation inhibits erlin1/2 complex-mediated inositol 1,4,5-trisphosphate receptor ubiquitination and phosphatidylinositol 3-phosphate binding.

Forrest A Wright, Caden G Bonzerato, Danielle A Sliter, Richard J H Wojcikiewicz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Hereditary spastic paraparesis type 18 (SPG18): new ERLIN2 variants in a series of Italian patients, shedding light upon genetic and phenotypic variability.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A rigorousFrontiers in molecular neuroscience · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Dominant mutations in ITPR3 cause Charcot-Marie-Tooth disease.Annals of clinical and translational neurology · 2020
    Article
  17. The emerging link between IPCell calcium · 2020
    Article
  18. Article
  19. Proteomic Changes in Human Sperm During SequentialFrontiers in cell and developmental biology · 2019
    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

4 authors at 2 institutions in 1 country.

Forrest A WrightFrom the Department of Pharmacology, State University of New York (SUNY) Upstate Medical University, Syracuse, New York 13210 and.
Caden G BonzeratoFrom the Department of Pharmacology, State University of New York (SUNY) Upstate Medical University, Syracuse, New York 13210 and.
Danielle A SliterBiochemistry Section, Surgical Neurology Branch, NINDS, National Institutes of Health, Bethesda, Maryland 20892.
Richard J H WojcikiewiczFrom the Department of Pharmacology, State University of New York (SUNY) Upstate Medical University, Syracuse, New York 13210 and wojcikir@upstate.edu.
SUNY Upstate Medical University · USNational Institute of Neurological Disorders and Stroke · US

Funding

Mechanism of IP3 receptor processing by the ERAD pathway and analysis of the IP3 receptor-erlin 1/2 complex-RNF170 axisR01DK107944 · NIDDK · UPSTATE MEDICAL UNIVERSITY · PI WOJCIKIEWICZ, RICHARD J H · 2017 to 2020
$1.6M
Significance of the novel Bok-IP3 receptor interactionR01GM121621 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI WOJCIKIEWICZ, RICHARD J H · 2017 to 2020
$1.2M
NIDDK NIH HHS R01 DK107944NIGMS NIH HHS R01 GM121621
6 · The paper itself

Abstract

The erlin1/2 complex is a ∼2-MDa endoplasmic reticulum membrane-located ensemble of the ∼40-kDa type II membrane proteins erlin1 and erlin2. The best defined function of this complex is to mediate the ubiquitination of activated inositol 1,4,5-trisphosphate receptors (IP

Indexed as

Amino Acid SubstitutionAmino Acid SequenceAnimalsCell Line, TransformedCRISPR-Cas SystemsGene EditingGonadotrophsHumansInositol 1,4,5-Trisphosphate ReceptorsMembrane ProteinsMiceMutationNerve Tissue ProteinsPhosphatidylinositol PhosphatesProtein BindingProteolysisERLIN1 protein, humanerlin-1 protein, mouseerlin-2 protein, mouseInositol 1,4,5-Trisphosphate ReceptorsMembrane ProteinsNerve Tissue Proteinsphosphatidylinositol 3-phosphatePhosphatidylinositol Phosphatesendoplasmic-reticulum-associated protein degradation (ERAD)endoplasmic reticulum (ER)erlin1erlin2inositol trisphosphate receptor (InsP3R)mutationphosphatidylinositol phosphatasephospholipid signalingspastic paraplegiaubiquitylation (ubiquitination)

Identifiers

PMID30135210
PMCPMC6177578
OpenAlexW2888377732

What OpenQuestion holds

Textmetadata
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.