Evidence map›Paper›PMID 25940394›Full record

ArticleScientific reports2015

3D Structural Fluctuation of IgG1 Antibody Revealed by Individual Particle Electron Tomography.

Xing Zhang, Lei Zhang, Huimin Tong, Bo Peng, Matthew J Rames, Shengli Zhang, Gang Ren

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
16.7field-weighted citation impact, top 1% 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

82 citing papers in PubMed, 128 citations in OpenAlex.

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  9. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
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  11. Bispecific antibodies against the hepatitis C virus E1E2 envelope glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2025
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22 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Xing Zhang1] The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA [2] Department of Applied Physics, Xi'an Jiaotong University, Xi'an, Shaanxi 710049, China.
Lei ZhangThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Huimin TongThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Bo PengThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Matthew J RamesThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Shengli ZhangDepartment of Applied Physics, Xi'an Jiaotong University, Xi'an, Shaanxi 710049, China.
Gang RenThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Lawrence Berkeley National Laboratory · USXi'an Jiaotong University · CN

Funding

Structure-Function Relationship Studies of the Plasma Lipid Transfer Proteins CETP and PLTPR01HL115153 · NHLBI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI REN, GANG · 2012 to 2021
$3.9M
Lipoprotein Structure and Function by Individual Particle Electron TomographyR01GM104427 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI REN, GANG · 2013 to 2016
$1.3M
NHLBI NIH HHS R01 HL115153NIGMS NIH HHS R01 GM104427
6 · The paper itself

Abstract

Commonly used methods for determining protein structure, including X-ray crystallography and single-particle reconstruction, often provide a single and unique three-dimensional (3D) structure. However, in these methods, the protein dynamics and flexibility/fluctuation remain mostly unknown. Here, we utilized advances in electron tomography (ET) to study the antibody flexibility and fluctuation through structural determination of individual antibody particles rather than averaging multiple antibody particles together. Through individual-particle electron tomography (IPET) 3D reconstruction from negatively-stained ET images, we obtained 120 ab-initio 3D density maps at an intermediate resolution (~1-3 nm) from 120 individual IgG1 antibody particles. Using these maps as a constraint, we derived 120 conformations of the antibody via structural flexible docking of the crystal structure to these maps by targeted molecular dynamics simulations. Statistical analysis of the various conformations disclosed the antibody 3D conformational flexibility through the distribution of its domain distances and orientations. This blueprint approach, if extended to other flexible proteins, may serve as a useful methodology towards understanding protein dynamics and functions.

Indexed as

CrystallographyElectron Microscope TomographyElectronsHumansImage Interpretation, Computer-AssistedImaging, Three-DimensionalImmunoglobulin GProtein ConformationImmunoglobulin G

Identifiers

PMID25940394
PMCPMC4419541
OpenAlexW2265060724

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.