Evidence map›Paper›PMID 31780561›Full record

ArticleScience (New York, N.Y.)2019

Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway.

Hyun-Kyu Choi, Duyoung Min, Hyunook Kang, Min Ju Shon, Sang-Hyun Rah, Hak Chan Kim, Hawoong Jeong, Hee-Jung Choi, James U Bowie, Tae-Young Yoon

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 83 citations in OpenAlex.

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  5. Single-molecule dissection of CFTR folding defects and pharmacological rescue.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

10 authors at 3 institutions in 2 countries.

Hyun-Kyu Choi *Department of Physics, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.ORCID 0000-0001-9192-891X
Duyoung Min *Department of Chemistry and Biochemistry, University of California-Los Angeles, Los Angeles, CA 90095, USA.ORCID 0000-0002-2856-8082
Hyunook Kang *School of Biological Sciences, Seoul National University, Seoul 08826, South Korea.ORCID 0000-0002-7017-4597
Min Ju ShonSchool of Biological Sciences, Seoul National University, Seoul 08826, South Korea.ORCID 0000-0002-0333-1150
Sang-Hyun RahDepartment of Physics, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.ORCID 0000-0002-9480-7731
Hak Chan KimSchool of Biological Sciences, Seoul National University, Seoul 08826, South Korea.ORCID 0000-0003-0467-3483
Hawoong JeongDepartment of Physics, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.ORCID 0000-0002-2491-8620
Hee-Jung ChoiSchool of Biological Sciences, Seoul National University, Seoul 08826, South Korea. choihj@snu.ac.kr bowie@mbi.ucla.edu tyyoon@snu.ac.kr.ORCID 0000-0002-1167-1526
James U BowieDepartment of Chemistry and Biochemistry, University of California-Los Angeles, Los Angeles, CA 90095, USA. choihj@snu.ac.kr bowie@mbi.ucla.edu tyyoon@snu.ac.kr.ORCID 0000-0003-2249-5908
Tae-Young YoonSchool of Biological Sciences, Seoul National University, Seoul 08826, South Korea. choihj@snu.ac.kr bowie@mbi.ucla.edu tyyoon@snu.ac.kr.ORCID 0000-0002-5184-7725
Seoul National University · KRUniversity of California, Los Angeles · USKorea Advanced Institute of Science and Technology · KR

Funding

Membrane Protein StabilityR01GM063919 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BOWIE, JAMES U · 2001 to 2021
$5.6M
NIGMS NIH HHS R01 GM063919
6 · The paper itself

Abstract

To understand membrane protein biogenesis, we need to explore folding within a bilayer context. Here, we describe a single-molecule force microscopy technique that monitors the folding of helical membrane proteins in vesicle and bicelle environments. After completely unfolding the protein at high force, we lower the force to initiate folding while transmembrane helices are aligned in a zigzag manner within the bilayer, thereby imposing minimal constraints on folding. We used the approach to characterize the folding pathways of the

Indexed as

Protein FoldingBiological EvolutionDNA-Binding ProteinsEndopeptidasesEscherichia coliEscherichia coli ProteinsHumansMembrane ProteinsModels, MolecularProtein ConformationProtein Modification, TranslationalReceptors, Adrenergic, beta-2Single Molecule ImagingDNA-Binding ProteinsEndopeptidasesEscherichia coli ProteinsGlpG protein, E coliMembrane ProteinsReceptors, Adrenergic, beta-2

Identifiers

PMID31780561
PMCPMC7382370
OpenAlexW2989859371

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.