Evidence map›Paper›PMID 35216461›Full record

ReviewInternational journal of molecular sciences2022

Diffracted X-ray Tracking Method for Measuring Intramolecular Dynamics of Membrane Proteins.

Shoko Fujimura, Kazuhiro Mio, Tatsunari Ohkubo, Tatsuya Arai, Masahiro Kuramochi, Hiroshi Sekiguchi, Yuji C Sasaki

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Special Issue: Structure, Function and Evolution of Protein Domains.International journal of molecular sciences · 2022
    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

7 authors.

Shoko FujimuraAIST-UTokyo Advanced Operando-Measurement Technology Open Innovation Laboratory (OPERANDO-OIL), National Institute of Advanced Industrial Science and Technology (AIST), 6-2-3 Kashiwanoha, Kashiwa 277-0882, Japan.
Kazuhiro MioAIST-UTokyo Advanced Operando-Measurement Technology Open Innovation Laboratory (OPERANDO-OIL), National Institute of Advanced Industrial Science and Technology (AIST), 6-2-3 Kashiwanoha, Kashiwa 277-0882, Japan.ORCID 0000-0002-1655-8231
Tatsunari OhkuboAIST-UTokyo Advanced Operando-Measurement Technology Open Innovation Laboratory (OPERANDO-OIL), National Institute of Advanced Industrial Science and Technology (AIST), 6-2-3 Kashiwanoha, Kashiwa 277-0882, Japan.
Tatsuya AraiGraduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan.
Masahiro KuramochiGraduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan.ORCID 0000-0003-1643-3997
Hiroshi SekiguchiCenter for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo 679-5198, Japan.ORCID 0000-0001-7590-3624
Yuji C SasakiAIST-UTokyo Advanced Operando-Measurement Technology Open Innovation Laboratory (OPERANDO-OIL), National Institute of Advanced Industrial Science and Technology (AIST), 6-2-3 Kashiwanoha, Kashiwa 277-0882, Japan.ORCID 0000-0003-3403-237X

Funding

Japan Science and Technology Agency JP18071859Japan Society for the Promotion of Science JP17H05539Japan Society for the Promotion of Science JP18K06601Japan Society for the Promotion of Science JP26102748Japan Synchrotron Radiation Research Institute 2017A1140Japan Synchrotron Radiation Research Institute 2018A1417Japan Synchrotron Radiation Research Institute 2019A1498Photon Factory Program Advisory Committee 2017G556
6 · The paper itself

Abstract

Membrane proteins change their conformations in response to chemical and physical stimuli and transmit extracellular signals inside cells. Several approaches have been developed for solving the structures of proteins. However, few techniques can monitor real-time protein dynamics. The diffracted X-ray tracking method (DXT) is an X-ray-based single-molecule technique that monitors the internal motion of biomolecules in an aqueous solution. DXT analyzes trajectories of Laue spots generated from the attached gold nanocrystals with a two-dimensional axis by tilting (

Indexed as

GoldMembrane ProteinsMotionNanotechnologyX-Ray DiffractionX-RaysGoldMembrane Proteinsconformation dynamicsdiffracted X-ray tracking techniquemembrane proteinssingle molecule analysis

Identifiers

PMID35216461
PMCPMC8880040

What OpenQuestion holds

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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.