Evidence map›Paper›PMID 35889400›Full record

ReviewMolecules (Basel, Switzerland)2022

Speculation on How RIC-3 and Other Chaperones Facilitate α7 Nicotinic Receptor Folding and Assembly.

Ralph H Loring

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. RIC-3 Interacts Directly with the 5-HTbioRxiv : the preprint server for biology · 2026
    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

1 author at 1 institution in 1 country.

Ralph H LoringDepartment Pharmaceutical Sciences, Northeastern University, 360 Huntington Ave., Boston, MA 02115, USA.ORCID 0000-0002-9228-4981
Northeastern University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The process of how multimeric transmembrane proteins fold and assemble in the endoplasmic reticulum is not well understood. The alpha7 nicotinic receptor (α7 nAChR) is a good model for multimeric protein assembly since it has at least two independent and specialized chaperones: Resistance to Inhibitors of Cholinesterase 3 (RIC-3) and Nicotinic Acetylcholine Receptor Regulator (NACHO). Recent cryo-EM and NMR data revealed structural features of α7 nAChRs. A ser-ala-pro (SAP) motif precedes a structurally important but unique "latch" helix in α7 nAChRs. A sampling of α7 sequences suggests the SAP motif is conserved from

Indexed as

Receptors, Nicotinicalpha7 Nicotinic Acetylcholine ReceptorAnimalsArtificial IntelligenceCaenorhabditis elegansCholinesterasesHumansIntracellular Signaling Peptides and ProteinsMolecular Chaperonesalpha7 Nicotinic Acetylcholine ReceptorCholinesterasesIntracellular Signaling Peptides and ProteinsMolecular ChaperonesReceptors, Nicotiniccys-loop receptorsintracellular domainmolecular modelingmultimeric protein assembly

Identifiers

PMID35889400
PMCPMC9318448
OpenAlexW4285733359

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.