Evidence map›Paper›PMID 22748693›Full record

ArticleTrends in biochemical sciences2012

Understanding integration of α-helical membrane proteins: the next steps.

Reid Gilmore, Elisabet C Mandon

Open access · greenAbstract read
In one paragraph

Article in Trends in biochemical sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

2 authors at 1 institution in 1 country.

Reid GilmoreDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605-2324, USA. reid.gilmore@umassmed.edu
Elisabet C Mandon
University of Massachusetts Chan Medical School · US

Funding

PROTEIN TRANSLOCATION ACROSS THE ENDOPLASMIC RETICULUMR01GM035687 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GILMORE, JAMES REID · 1985 to 2019
$5.9M
NIGMS NIH HHS GM35687NIGMS NIH HHS R01 GM035687
6 · The paper itself

Abstract

Integration of a protein into the endoplasmic reticulum (ER) membrane occurs through a series of multistep reactions that include targeting of ribosome-nascent polypeptide complexes to the ER, attachment of the ribosome to the protein translocation channel, lateral partitioning of α-helical transmembrane spans into the lipid bilayer, and folding of the lumenal, cytosolic and membrane-embedded domains of the protein. However, the molecular mechanisms and kinetics of these steps are still not entirely clear. To obtain a better understanding of the mechanism of membrane protein integration, we propose that it will be important to utilize in vivo experiments to examine the kinetics of membrane protein integration and in vitro experiments to characterize interactions between nascent membrane proteins, protein translocation factors and molecular chaperones.

Indexed as

Protein Structure, SecondaryCytosolEndoplasmic Reticulum, RoughHydrophobic and Hydrophilic InteractionsMembrane ProteinsMembrane Transport ProteinsProtein BiosynthesisProtein FoldingProtein Structure, TertiaryProtein TransportRibosomesRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsMembrane ProteinsMembrane Transport ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsSEC61 protein, S cerevisiaeSEC Translocation Channels

Identifiers

PMID22748693
PMCPMC3557837
OpenAlexW2004070465

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.