Evidence map›Paper›PMID 31350338›Full record

ArticleThe Journal of biological chemistry2019

Conserved residue His-257 of

Xuan Fang, Jerzy Osipiuk, Srinivas Chakravarthy, Ming Yuan, William M Menzer, Devin Nissen, Pingdong Liang, Daniel A Raba, Karina Tuz, Andrew J Howard and 3 more

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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025
    Review
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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

13 authors at 3 institutions in 1 country.

Xuan FangDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.
Jerzy OsipiukCenter for Structural Genomics of Infectious Diseases (CSGID), Consortium for Advanced Science and Engineering, University of Chicago, Chicago, Illinois 60637.
Srinivas ChakravarthyDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.
Ming YuanDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.
William M MenzerDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.ORCID 0000-0001-5052-3158
Devin NissenDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.
Pingdong LiangDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.
Daniel A RabaDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.
Karina TuzDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.
Andrew J HowardDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616.
Andrzej JoachimiakCenter for Structural Genomics of Infectious Diseases (CSGID), Consortium for Advanced Science and Engineering, University of Chicago, Chicago, Illinois 60637.
David D L MinhDepartment of Chemistry, Illinois Institute of Technology, Chicago, Illinois 60616.ORCID 0000-0002-4802-2618
Oscar JuarezDepartment of Biological Sciences, Illinois Institute of Technology, Chicago, Illinois 60616 ojuarez@iit.edu.
Illinois Institute of Technology · USArgonne National Laboratory · USIIT Research Institute · US

Funding

Entropy for End-Point and FFT-Based Binding Free Energy CalculationsR01GM127712 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI MINH, DAVID DO LE · 2018 to 2021
$1.3M
NIAID NIH HHS HHSN272201200026CNIAID NIH HHS HHSN272201700060CNIGMS NIH HHS R01 GM127712
6 · The paper itself

Abstract

The flavin transferase ApbE plays essential roles in bacterial physiology, covalently incorporating FMN cofactors into numerous respiratory enzymes that use the integrated cofactors as electron carriers. In this work we performed a detailed kinetic and structural characterization of

Indexed as

Bacterial ProteinsCatalysisCatalytic DomainConserved SequenceFlavin-Adenine DinucleotideFlavin MononucleotideFlavinsHistidineKineticsOxidation-ReductionSubstrate SpecificityTransferasesVibrio choleraeBacterial ProteinsFlavin-Adenine DinucleotideFlavin MononucleotideFlavinsHistidineTransferasesAcid base catalysisApbEelectron transferenzyme catalysisenzyme mechanismflavin adenine dinucleotide (FAD)flavin mononucleotide (FMN)flavin transferaseflavoproteinNQRprotein assemblyVibrio cholerae

Identifiers

PMID31350338
PMCPMC6746461
OpenAlexW2966674042

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.