Evidence map›Paper›PMID 25223459›Full record

ArticleScientific reports2014

Real time ligand-induced motion mappings of AChBP and nAChR using X-ray single molecule tracking.

Hiroshi Sekiguchi, Yasuhito Suzuki, Yuri Nishino, Suzuko Kobayashi, Yoshiko Shimoyama, Weiyan Cai, Kenji Nagata, Masato Okada, Kouhei Ichiyanagi, Noboru Ohta and 4 more

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

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

19 citing papers in PubMed, 40 citations in OpenAlex.

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  10. Visualizing Intramolecular Dynamics of Membrane Proteins.International journal of molecular sciences · 2022
    Review
  11. Dynamic motions of ice-binding proteins in livingBiochemistry and biophysics reports · 2022
    Article
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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

14 authors at 6 institutions in 1 country.

Hiroshi Sekiguchi1] CREST Sasaki Team, Japan Science and Technology Agency, The University of Tokyo, #609 Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan [2] Research &Utilization Division, Japan Synchrotron Radiation Research Institute, SPring-8 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Yasuhito Suzuki1] CREST Sasaki Team, Japan Science and Technology Agency, The University of Tokyo, #609 Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan [2] Graduate School of Frontier Sciences, The University of Tokyo, Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan.
Yuri Nishino1] Graduate School of Life Sciences, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo, 679-1297, Japan [2] RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5148, Japan.
Suzuko KobayashiBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.
Yoshiko ShimoyamaBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.
Weiyan CaiBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.
Kenji NagataGraduate School of Frontier Sciences, The University of Tokyo, Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan.
Masato OkadaGraduate School of Frontier Sciences, The University of Tokyo, Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan.
Kouhei Ichiyanagi1] CREST Sasaki Team, Japan Science and Technology Agency, The University of Tokyo, #609 Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan [2] Graduate School of Frontier Sciences, The University of Tokyo, Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan.
Noboru OhtaResearch &Utilization Division, Japan Synchrotron Radiation Research Institute, SPring-8 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Naoto Yagi1] CREST Sasaki Team, Japan Science and Technology Agency, The University of Tokyo, #609 Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan [2] Research &Utilization Division, Japan Synchrotron Radiation Research Institute, SPring-8 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Atsuo Miyazawa1] Graduate School of Life Sciences, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo, 679-1297, Japan [2] RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5148, Japan.
Tai Kubo1] CREST Sasaki Team, Japan Science and Technology Agency, The University of Tokyo, #609 Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan [2] Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan [3] Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), 2-4-7 Aomi, Koto-ku, Tokyo 135-0064, Japan.
Yuji C Sasaki1] CREST Sasaki Team, Japan Science and Technology Agency, The University of Tokyo, #609 Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan [2] Research &Utilization Division, Japan Synchrotron Radiation Research Institute, SPring-8 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan [3] Graduate School of Frontier Sciences, The University of Tokyo, Kiban Bldg., 5-1-5 Kashiwanoha, Kashiwa City, Chiba, 277-8561, Japan.
The University of Tokyo · JPNational Institute of Advanced Industrial Science and Technology · JPUniversity of Hyogo · JPJapan Science and Technology Agency · JPJapan Synchrotron Radiation Research Institute · JPSPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We observed the dynamic three-dimensional (3D) single molecule behaviour of acetylcholine-binding protein (AChBP) and nicotinic acetylcholine receptor (nAChR) using a single molecule tracking technique, diffracted X-ray tracking (DXT) with atomic scale and 100 μs time resolution. We found that the combined tilting and twisting motions of the proteins were enhanced upon acetylcholine (ACh) binding. We present the internal motion maps of AChBP and nAChR in the presence of either ACh or α-bungarotoxin (αBtx), with views from two rotational axes. Our findings indicate that specific motion patterns represented as biaxial angular motion maps are associated with channel function in real time and on an atomic scale.

Indexed as

AcetylcholineAnimalsAplysiaBinding SitesBungarotoxinsCarrier ProteinsCrystallography, X-RayModels, MolecularProtein ConformationReceptors, NicotinicTorpedoAcetylcholineBungarotoxinsCarrier ProteinsReceptors, Nicotinic

Identifiers

PMID25223459
PMCPMC4165275
OpenAlexW1973138984

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.