Evidence map›Paper›PMID 38361954›Full record

ArticleJournal of structural biology: X2024

Grafting the ALFA tag for structural studies of aquaporin Z.

Lauren Stover, Hanieh Bahramimoghaddam, Lie Wang, Samantha Schrecke, Gaya P Yadav, Ming Zhou, Arthur Laganowsky

Open access · goldAbstract read
In one paragraph

Article in Journal of structural biology: X, 2024. 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
1.4field-weighted citation impact, top 20% 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, 6 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Lauren StoverDepartment of Chemistry, Texas A&M University, College Station, TX 77843, United States.
Hanieh BahramimoghaddamDepartment of Chemistry, Texas A&M University, College Station, TX 77843, United States.
Lie WangVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, United States.
Samantha SchreckeDepartment of Chemistry, Texas A&M University, College Station, TX 77843, United States.
Gaya P YadavLaboratory for Biomolecular Structure and Dynamics (LBSD), Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.
Ming ZhouVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, United States.
Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, TX 77843, United States.
Texas A&M University · USBaylor College of Medicine · US

Funding

Understanding the role of lipids in structure and function of membrane proteinsRM1GM145416 · NIGMS · TEXAS A&M UNIVERSITY · PI Erin S Baker, Arthur D Laganowsky · 2022 to 2026
$7.4M
Structure and mechanism of mammalian stearoyl-CoA desaturasesR01DK122784 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI TSAI, AH-LIM, ZHOU, MING · 2019 to 2023
$3.2M
Innovative Native Ion Mobility Approaches for Transformational Measurements in Structural BiologyR01GM138863 · NIGMS · TEXAS A&M UNIVERSITY · PI CLOWERS, BRIAN, LAGANOWSKY, ARTHUR D · 2020 to 2023
$1.2M
Developing new tools to probe membrane protein-lipid interactions for biomedical applicationsR01GM139876 · NIGMS · TEXAS A&M UNIVERSITY · PI LAGANOWSKY, ARTHUR D · 2021 to 2024
$1.2M
NIDDK NIH HHS R01 DK122784NIGMS NIH HHS R01 GM138863NIGMS NIH HHS R01 GM139876NIGMS NIH HHS RM1 GM145416
6 · The paper itself

Abstract

Aquaporin Z (AqpZ), a bacterial water channel, forms a tetrameric complex and, like many other membrane proteins, activity is regulated by lipids. Various methods have been developed to facilitate structure determination of membrane proteins, such as the use of antibodies. Here, we graft onto AqpZ the ALFA tag (AqpZ-ALFA), an alpha helical epitope, to make use of the high-affinity anti-ALFA nanobody (nB). Native mass spectrometry reveals the AqpZ-ALFA fusion forms a stable, 1:1 complex with nB. Single-particle cryogenic electron microscopy studies reveal the octameric (AqpZ-ALFA)

Identifiers

PMID38361954
PMCPMC10867769
OpenAlexW4391487061

What OpenQuestion holds

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LicenceCC BY
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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.