Evidence map›Paper›PMID 33773141›Full record

ArticleBiochemical and biophysical research communications2021

Bok binds to a largely disordered loop in the coupling domain of type 1 inositol 1,4,5-trisphosphate receptor.

Laura M Szczesniak, Caden G Bonzerato, Jacqualyn J Schulman, Alaji Bah, Richard J H Wojcikiewicz

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

Article in Biochemical and biophysical research communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Phosphorylation of Bok at Ser-8 blocks its ability to suppress IPCell communication and signaling : CCS · 2025
    Article
  2. Review
  3. Apoptotic mitochondrial poration by a growing list of pore-forming BCL-2 family proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  4. Bok: real killer or bystander with non-apoptotic roles?Frontiers in cell and developmental biology · 2023
    Review
  5. 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

5 authors at 1 institution in 1 country.

Laura M SzczesniakDepartment of Pharmacology, SUNY Upstate Medical University, Syracuse, NY, USA.
Caden G BonzeratoDepartment of Pharmacology, SUNY Upstate Medical University, Syracuse, NY, USA.
Jacqualyn J SchulmanDepartment of Pharmacology, SUNY Upstate Medical University, Syracuse, NY, USA.
Alaji BahDepartment of Biochemistry, Department of Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, USA.
Richard J H WojcikiewiczDepartment of Pharmacology, SUNY Upstate Medical University, Syracuse, NY, USA. Electronic address: wojcikir@upstate.edu.
SUNY Upstate Medical University · 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
Mechanisms by which Bok binds to IP3Rs and regulates mitochondrial dynamicsF30GM134638 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI SZCZESNIAK, LAURA · 2019 to 2021
$152k
NIDDK NIH HHS R01 DK107944NIGMS NIH HHS F30 GM134638NIGMS NIH HHS R01 GM121621
6 · The paper itself

Abstract

Bcl-2-related ovarian killer (Bok) binds tightly to inositol 1,4,5-trisphosphate receptors (IP

Indexed as

Binding SitesHumansInositol 1,4,5-Trisphosphate ReceptorsModels, MolecularMolecular Targeted TherapyProtein BindingProtein DomainsProtein Structure, SecondaryProto-Oncogene Proteins c-bcl-2Sequence DeletionBOK protein, humanInositol 1,4,5-Trisphosphate ReceptorsProto-Oncogene Proteins c-bcl-2Bcl-2 related ovarian killer (Bok)CalciumInositol 1,4,5-trisphosphate receptorIntrinsically disordered regionProtein-protein interactionSecondary structure

Identifiers

PMID33773141
PMCPMC8052301
OpenAlexW3137347477

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.