Evidence map›Paper›PMID 28434103›Full record

ArticleJournal of biomolecular NMR2017

Structure restraints from heteronuclear pseudocontact shifts generated by lanthanide tags at two different sites.

Benjamin J G Pearce, Shereen Jabar, Choy-Theng Loh, Monika Szabo, Bim Graham, Gottfried Otting

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2017. 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. Localising individual atoms of tryptophan side chains in the metallo-Magnetic resonance (Gottingen, Germany) · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. 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

6 authors.

Benjamin J G PearceResearch School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia.
Shereen JabarResearch School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia.
Choy-Theng LohResearch School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia.
Monika SzaboMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, 3052, Australia.
Bim GrahamMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, 3052, Australia.
Gottfried OttingResearch School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia. gottfried.otting@anu.edu.au.ORCID http://orcid.org/0000-0002-0563-0146

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pseudocontact shifts (PCS) encode long-range information on 3D structures of protein backbones and side-chains. The level of structural detail that can be obtained increases with the number of different sites tagged with a paramagnetic metal ion to generate PCSs. Here we show that PCSs from two different sites can suffice to determine the structure of polypeptide chains and their location and orientation relative to the magnetic susceptibility tensor χ, provided that PCSs are available for

Indexed as

Amino Acids, Branched-ChainLanthanoid Series ElementsNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsUbiquitinAmino Acids, Branched-ChainLanthanoid Series ElementsProteinsUbiquitinHuman ubiquitinLanthanide tagPseudocontact shiftResidual anisotropic chemical shiftsStructure determination

Identifiers

PMID28434103

What OpenQuestion holds

Textmetadata
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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.