Evidence map›Paper›PMID 11014593›Full record

ArticleJournal of biomolecular NMR2000

The auto-orientation in high magnetic fields of oxidized cytochrome b562 as source of constraints for solution structure determination.

F Arnesano, L Banci, I Bertini, K Van Der Wetering, M Czisch, R Kaptein

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2000. 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
2.8field-weighted citation impact, top 10% 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

6 citing papers in PubMed, 25 citations in OpenAlex.

  1. NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c(556).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2004
    Article
  2. 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 at 3 institutions in 2 countries.

F ArnesanoMagnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy.
L Banci
I Bertini
K Van Der Wetering
M Czisch
R Kaptein
Interuniversity Consortium for Magnetic Resonance · ITUtrecht University · NLUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

15N-1H 1J couplings were measured at 500 MHz and 800 MHz for 15N enriched oxidized cytochrome b562 from E. coli. The magnetic field dependence of 70 1J values, which could be measured without signal overlap, shows that there is a molecular magnetic anisotropy which provides partial molecular orientation in the magnetic field and, consequently, residual dipolar couplings (rdc). The rdc were used as further constraints to improve the existing structure [Arnesano et al. (1999) Biochemistry, 38, 8657-8670] with a protocol which uses the rhombic anisotropy [Banci et al. (1998) J. Am. Ctherz. Soc., 120, 12903-12909]. The overall large molecular magnetic anisotropy has been found to be determined by both the low spin iron (III) and the four helix bundle structure magnetic susceptibility anisotropy contributions.

Indexed as

Escherichia coli ProteinsAnisotropyBacterial ProteinsCytochrome b GroupEscherichia coliMagneticsNuclear Magnetic Resonance, BiomolecularOxidation-ReductionProtein ConformationProtein Structure, SecondarySolutionsBacterial Proteinscytochrome b562, E coliCytochrome b GroupEscherichia coli ProteinsSolutions

Identifiers

PMID11014593
OpenAlexW54541393

What OpenQuestion holds

Textmetadata
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.