Evidence map›Paper›PMID 25979464›Full record

ArticleProtein expression and purification2015

Purification and biochemical characterization of the ATP synthase from Heliobacterium modesticaldum.

Jay-How Yang, Iosifina Sarrou, Jose M Martin-Garcia, Shangji Zhang, Kevin E Redding, Petra Fromme

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein expression and purification, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 2 institutions in 2 countries.

Jay-How YangDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA; Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University, Tempe, AZ 85287-1604, USA.
Iosifina SarrouDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA; Institute of Molecular Biology & Biotechnology, Foundation for Research & Technology-Hellas, Nikolaou Plastira 100, GR-70013 Heraklion, Crete, Greece.
Jose M Martin-GarciaDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA; Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University, Tempe, AZ 85287-1604, USA.
Shangji ZhangSchool of Life Sciences, Arizona State University, Tempe, AZ 85287-1604, USA.
Kevin E ReddingDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA.
Petra FrommeDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA; Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University, Tempe, AZ 85287-1604, USA. Electronic address: pfromme@asu.edu.
Arizona State University · USFoundation for Research and Technology Hellas · GR

Funding

Femtosecond nano-crystallography of membrane proteinsR01GM095583 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2023
$4.3M
Structure and Function of the proton-turbine of the ATP-SynthaseR01GM081490 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2007 to 2010
$1.0M
NIGMS NIH HHS GM081490NIGMS NIH HHS GM095583NIGMS NIH HHS R01 GM081490NIGMS NIH HHS R01 GM095583
6 · The paper itself

Abstract

Heliobacterium modesticaldum is an anaerobic photosynthetic bacterium that grows optimally at pH 6-7 and 52°C and is the only phototrophic member of the Firmicutes phylum family (gram-positive bacteria with low GC content). The ATP synthase of H. modesticaldum was isolated and characterized at the biochemical and biophysical levels. The isolated holoenzyme exhibited the subunit patterns of F-type ATP synthases containing a 5-subunit hydrophilic F1 subcomplex and a 3-subunit hydrophobic F0 subcomplex. ATP hydrolysis by the isolated HF1F0 ATP synthase was successfully detected after pretreatment with different detergents by an in-gel ATPase activity assay, which showed that the highest activity was detected in the presence of mild detergents such as LDAO; moreover, high catalytic activity in the gel was already detected after the initial incubation period of 0.5h. In contrast, HF1F0 showed extremely low ATPase activity in harsher detergents such as TODC. The isolated fully functional enzyme will form the basis for future structural studies.

Indexed as

Adenosine TriphosphateBacterial ProteinsElectrophoresis, Polyacrylamide GelEubacterialesProton-Translocating ATPasesAdenosine TriphosphateBacterial ProteinsProton-Translocating ATPasesATP hydrolysisATP synthaseHeliobacterium modesticaldumIn-gel function assay

Identifiers

PMID25979464
PMCPMC4589444
OpenAlexW242029096

What OpenQuestion holds

Textmetadata
LicenceTDM
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.