Evidence map›Paper›PMID 40203538›Full record

ReviewCurrent opinion in structural biology2025

Nanodiscs remain indispensable for Cryo-EM studies of membrane proteins.

Giorgos Hiotis, Ryan Q Notti, Huan Bao, Thomas Walz

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Design of Fluorescent Membrane Scaffold Proteins for Nanodiscs.bioRxiv : the preprint server for biology · 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

4 authors.

Giorgos HiotisLaboratory of Molecular Electron Microscopy, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA; Tri-Institutional PhD Program in Chemical Biology, The Rockefeller University, 1300 York Avenue, New York, NY, USA.
Ryan Q NottiLaboratory of Molecular Electron Microscopy, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA; Department of Medicine, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA.
Huan BaoDepartment of Molecular Physiology and Biological Physics, University of Virginia, 480 Ray C. Hunt Drive, Charlottesville, VA 22903, USA.
Thomas WalzLaboratory of Molecular Electron Microscopy, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA. Electronic address: twalz@rockefeller.edu.

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SELWYN M VICKERS · 1985 to 2026
$347.4M
Platelet Integrin AlphaIIbBeta3 Structure, Activation, and Ligand Binding: Fibrinogen, Fibrin, D-dimer, and von Willebrand FactorR01HL019278 · NHLBI · STATE UNIVERSITY NEW YORK STONY BROOK · PI Claudia Lorena Buitrago, Barry Coller · 1985 to 2026
$17.6M
Structural characterization of MPER-TM immunogensP01AI181597 · NIAID · DANA-FARBER CANCER INST · PI ELLIS L REINHERZ · 2024 to 2026
$9.1M
Institutional Career Development CoreKL2TR001865 · NCATS · ROCKEFELLER UNIVERSITY · PI SCHLESINGER, SARAH JANE · 2016 to 2025
$8.7M
Developing next-generation nanodiscs for the study and modulation of membrane proteinsDP2GM140920 · NIGMS · UNIVERSITY OF VIRGINIA · PI BAO, HUAN · 2020 to 2020
$2.7M
Elucidating the gating mechanisms of bacterial mechanosensitive channelsR01GM144581 · NIGMS · ROCKEFELLER UNIVERSITY · PI THOMAS WALZ · 2023 to 2026
$2.0M
A cost-effective, high-throughput screening platform for modulator discovery of a-synuclein membrane interactions involved in neurodegenerative diseasesR21AG078699 · NIA · UNIVERSITY OF VIRGINIA · PI BAO, HUAN · 2023 to 2024
$492k
NCATS NIH HHS KL2 TR001865NCI NIH HHS P30 CA008748NHLBI NIH HHS R01 HL019278NIAID NIH HHS P01 AI181597NIA NIH HHS R21 AG078699NIGMS NIH HHS DP2 GM140920NIGMS NIH HHS R01 GM144581
6 · The paper itself

Abstract

Nanodiscs, small discoidal membrane patches stabilized by membrane-scaffold proteins (MSPs), are popular tools to stabilize integral membrane proteins (IMPs) for structural studies by cryogenic electron microscopy (cryo-EM). While nanodiscs provide a near-native membrane environment for the incorporated IMPs, they do not reproduce all characteristics of a native membrane. Also, IMPs must first be purified in detergent before they can be reconstituted into MSP-based nanodiscs, a problem that has been overcome by newer approaches, such as copolymer-based native nanodiscs and cell-derived vesicles. In this review, we argue that despite these advances, MSP-based nanodiscs remain a unique tool for the structural interrogation of IMPs.

Indexed as

Cryoelectron MicroscopyMembrane ProteinsNanostructuresHumansMembrane Proteins

Identifiers

PMID40203538
PMCPMC12146086

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.