Evidence map›Paper›PMID 34884581›Full record

ReviewInternational journal of molecular sciences2021

Folding and Insertion of Transmembrane Helices at the ER.

Paul Whitley, Brayan Grau, James C Gumbart, Luis Martínez-Gil, Ismael Mingarro

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Structural insights into SARS-CoV-2 nonstructural protein 4 (nsp4) biogenesis.Protein science : a publication of the Protein Society · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mechanisms of ER Protein Import.International journal of molecular sciences · 2022
    Article
  13. Review
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 3 institutions in 3 countries.

Paul WhitleyDepartment of Biology and Biochemistry, Centre for Regenerative Medicine, University of Bath, Bath BA2 7AY, UK.
Brayan GrauDepartment of Biochemistry and Molecular Biology, Institute of Biotechnology and Biomedicine (BIOTECMED), Universitat de València, E-46100 Burjassot, Spain.ORCID 0000-0002-8582-023X
James C GumbartSchool of Physics, School of Chemistry and Biochemistry, Parker H. Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332, USA.ORCID 0000-0002-1510-7842
Luis Martínez-GilDepartment of Biochemistry and Molecular Biology, Institute of Biotechnology and Biomedicine (BIOTECMED), Universitat de València, E-46100 Burjassot, Spain.
Ismael MingarroDepartment of Biochemistry and Molecular Biology, Institute of Biotechnology and Biomedicine (BIOTECMED), Universitat de València, E-46100 Burjassot, Spain.ORCID 0000-0002-1910-1229
Universitat de València · ESGeorgia Institute of Technology · USUniversity of Bath · GB

Funding

Dynamic characterization of outer-membrane-protein biogenesis by the BAM and TAM complexesR01GM123169 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI GUMBART, JAMES C. · 2017 to 2021
$1.4M
NIGMS NIH HHS R01 GM123169NIH HHS R01-GM123169
6 · The paper itself

Abstract

In eukaryotic cells, the endoplasmic reticulum (ER) is the entry point for newly synthesized proteins that are subsequently distributed to organelles of the endomembrane system. Some of these proteins are completely translocated into the lumen of the ER while others integrate stretches of amino acids into the greasy 30 Å wide interior of the ER membrane bilayer. It is generally accepted that to exist in this non-aqueous environment the majority of membrane integrated amino acids are primarily non-polar/hydrophobic and adopt an α-helical conformation. These stretches are typically around 20 amino acids long and are known as transmembrane (TM) helices. In this review, we will consider how transmembrane helices achieve membrane integration. We will address questions such as: Where do the stretches of amino acids fold into a helical conformation? What is/are the route/routes that these stretches take from synthesis at the ribosome to integration through the ER translocon? How do these stretches 'know' to integrate and in which orientation? How do marginally hydrophobic stretches of amino acids integrate and survive as transmembrane helices?

Indexed as

Protein FoldingAnimalsEndoplasmic ReticulumHumansHydrophobic and Hydrophilic InteractionsMembrane ProteinsProtein Conformation, alpha-HelicalMembrane Proteinsfoldinginsertionmembrane proteinribosometranslocontransmembrane segment

Identifiers

PMID34884581
PMCPMC8657811
OpenAlexW3214855804

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.