Evidence map›Paper›PMID 42149505›Full record

ReviewChemical reviews2026

The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.

Edward Lambden, Benjamin Russell Lewis, Zadie L R Baker, Marvin V Dilworth, Erin C Johnston, Juan Palacios-Ortega, Kaylee Patel, Colin P Pilkington, Heather E Findlay, Paula J Booth and 1 more

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Chemical reviews, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Edward LambdenDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.
Benjamin Russell LewisDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.
Zadie L R BakerAston Institute for Membrane Excellence, Aston University, Birmingham, B4 7ET, U.K.
Marvin V DilworthDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.
Erin C JohnstonDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.ORCID 0000-0002-7616-0778
Juan Palacios-OrtegaDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.ORCID 0000-0002-4629-0221
Kaylee PatelDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.
Colin P PilkingtonDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.
Heather E FindlayDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.
Paula J BoothDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London, SE1 1DB, U.K.
Grant A PelloweAston Institute for Membrane Excellence, Aston University, Birmingham, B4 7ET, U.K.ORCID 0000-0003-4314-5261

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding how membrane proteins insert into and fold within cell membranes is critical for explaining the molecular basis of many diseases. It also underpins advances in biotechnology, including the development of therapies for protein misfolding disorders and improved methods for producing membrane proteins at high yield. In cells, nearly all α-helical membrane proteins are synthesized and inserted cotranslationally, folding sequentially as they emerge from the ribosome. This process occurs under spatial constraints imposed by the translational machinery and in membranes with complex physicochemical properties. These processes are vastly different from classical

Indexed as

Membrane ProteinsProtein FoldingRibosomesAnimalsHumansProtein Conformation, alpha-HelicalMembrane Proteins

Identifiers

PMID42149505
PMCPMC13307174

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Registered trials

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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.