Evidence map›Paper›PMID 31108891›Full record

ReviewInternational journal of molecular sciences2019

Protein Structure Determination in Living Cells.

Teppei Ikeya, Peter Güntert, Yutaka Ito

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Review
  2. Computational and Experimental Approaches and Applications of Biological NMR.Advances in experimental medicine and biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Toll-like Receptor 3 in the Hybrid Yellow Catfish (Animals : an open access journal from MDPI · 2023
    Article
  8. Characterization ofFrontiers in immunology · 2023
    Article
  9. Article
  10. Article
  11. Protein assembly and crowding simulations.Current opinion in structural biology · 2022
    Review
  12. Article
  13. Review
  14. 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

3 authors.

Teppei IkeyaDepartment of Chemistry, Graduate School of Science, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, Tokyo 192-0397, Japan. tikeya@tmu.ac.jp.ORCID 0000-0002-6721-3727
Peter GüntertDepartment of Chemistry, Graduate School of Science, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, Tokyo 192-0397, Japan. guentert@em.uni-frankfurt.de.ORCID 0000-0002-2911-7574
Yutaka ItoDepartment of Chemistry, Graduate School of Science, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, Tokyo 192-0397, Japan. ito-yutaka@tmu.ac.jp.ORCID 0000-0002-1030-4660

Funding

Japan Science and Technology Agency CREST JPMJCR13M3Japan Society for the Promotion of Science JP26102538, JP25120003, JP16H00779, JP15H01645, JP16H00847, JP15K06979, JP17K07312
6 · The paper itself

Abstract

To date, in-cell NMR has elucidated various aspects of protein behaviour by associating structures in physiological conditions. Meanwhile, current studies of this method mostly have deduced protein states in cells exclusively based on 'indirect' structural information from peak patterns and chemical shift changes but not 'direct' data explicitly including interatomic distances and angles. To fully understand the functions and physical properties of proteins inside cells, it is indispensable to obtain explicit structural data or determine three-dimensional (3D) structures of proteins in cells. Whilst the short lifetime of cells in a sample tube, low sample concentrations, and massive background signals make it difficult to observe NMR signals from proteins inside cells, several methodological advances help to overcome the problems. Paramagnetic effects have an outstanding potential for in-cell structural analysis. The combination of a limited amount of experimental in-cell data with software for

Indexed as

AlgorithmsModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsSoftwareProteinsnon-uniform sampling 2paramagnetic effectsprotein structure determination 1spectrum reconstruction 3structural calculation 4

Identifiers

PMID31108891
PMCPMC6567067

What OpenQuestion holds

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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.