Evidence map›Paper›PMID 31527086›Full record

ArticleThe Journal of biological chemistry2019

PCu

Oriana S Fisher, Madison R Sendzik, Matthew O Ross, Thomas J Lawton, Brian M Hoffman, Amy C Rosenzweig

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

8 citing papers in PubMed, 18 citations in OpenAlex.

  1. AccA fromChemical science · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Orchestrating copper binding: structure and variations on the cupredoxin fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  8. 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 1 institution in 1 country.

Oriana S FisherDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208.ORCID 0000-0003-3215-0831
Madison R SendzikDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208.ORCID 0000-0003-1363-6297
Matthew O RossDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208.ORCID 0000-0003-2115-9806
Thomas J LawtonDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208.
Brian M HoffmanDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208.
Amy C RosenzweigDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208 amyr@northwestern.edu.ORCID 0000-0001-8472-4134
Northwestern University · US

Funding

Metalloenzymes and metal homeostasisR35GM118035 · NIGMS · NORTHWESTERN UNIVERSITY · PI AMY C. ROSENZWEIG · 2016 to 2026
$7.1M
Coboglobins-Cobalt-Substituted Hemoglobins and MyoglobinR01GM111097 · NIGMS · NORTHWESTERN UNIVERSITY · PI HOFFMAN, BRIAN M · 2014 to 2025
$6.7M
Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
Characterization of pmoDF32GM119191 · NIGMS · NORTHWESTERN UNIVERSITY · PI FISHER, ORIANA S · 2016 to 2018
$174k
NIGMS NIH HHS F32 GM119191NIGMS NIH HHS R01 GM111097NIGMS NIH HHS R35 GM118035NIGMS NIH HHS T32 GM008382
6 · The paper itself

Abstract

Copper is critically important for methanotrophic bacteria because their primary metabolic enzyme, particulate methane monooxygenase (pMMO), is copper-dependent. In addition to pMMO, many other copper proteins are encoded in the genomes of methanotrophs, including proteins that contain

Indexed as

Binding SitesCopperCrystallography, X-RayElectron Spin Resonance SpectroscopyHistidineLigandsMethylococcaceaeMethylocystaceaeMixed Function OxygenasesModels, MolecularOrganometallic CompoundsOxygenasesPeriplasmic Binding ProteinsProtein DomainsCoppercopper histidineHistidineLigandsmethane monooxygenaseMixed Function OxygenasesOrganometallic CompoundsOxygenasesPeriplasmic Binding Proteinsbioinformaticscopper chaperonecopper transportcrystal structurehistidine bracemetal homeostasismetalloproteinmethanotroph

Identifiers

PMID31527086
PMCPMC6827282
OpenAlexW2974656599

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.