Evidence map›Paper›PMID 32224302›Full record

ArticleBiophysical journal2020

Atomic Force Microscopy Visualizes Mobility of Photosynthetic Proteins in Grana Thylakoid Membranes.

Bibiana Onoa, Shingo Fukuda, Masakazu Iwai, Carlos Bustamante, Krishna K Niyogi

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
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

5 authors at 2 institutions in 1 country.

Bibiana OnoaHoward Hughes Medical Institute, University of California, Berkeley, California. Electronic address: bibianaonoa@berkeley.edu.
Shingo FukudaHoward Hughes Medical Institute, University of California, Berkeley, California.
Masakazu IwaiMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California; Department of Plant and Microbial Biology, University of California, Berkeley, California.
Carlos BustamanteHoward Hughes Medical Institute, University of California, Berkeley, California; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California; Jason L. Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, California; Department of Molecular and Cell Biology, University of California, Berkeley, California; Department of Physics, University of California, Berkeley, California; Kavli Energy NanoScience Institute, Lawrence Berkeley National Laboratory, University of California, Berkeley, California.
Krishna K NiyogiHoward Hughes Medical Institute, University of California, Berkeley, California; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California; Department of Plant and Microbial Biology, University of California, Berkeley, California. Electronic address: niyogi@berkeley.edu.
Howard Hughes Medical Institute · USLawrence Berkeley National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thylakoid membranes in chloroplasts contain photosynthetic protein complexes that convert light energy into chemical energy. Photosynthetic protein complexes are considered to undergo structural reorganization to maintain the efficiency of photochemical reactions. A detailed description of the mobility of photosynthetic complexes in real time is necessary to understand how macromolecular organization of the membrane is altered by environmental fluctuations. Here, we used high-speed atomic force microscopy to visualize and characterize the in situ mobility of individual protein complexes in grana thylakoid membranes isolated from Spinacia oleracea. Our observations reveal that these membranes can harbor complexes with at least two distinctive classes of mobility. A large fraction of grana membranes contained proteins with quasistatic mobility exhibiting molecular displacements smaller than 10 nm

Indexed as

Photosystem II Protein ComplexThylakoidsMicroscopy, Atomic ForcePhotosynthesisSpinacia oleraceaPhotosystem II Protein Complex

Identifiers

PMID32224302
PMCPMC7175462
OpenAlexW3011078298

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.