Evidence map›Paper›PMID 26228793›Full record

ArticleScientific reports2015

Glass is a Viable Substrate for Precision Force Microscopy of Membrane Proteins.

Nagaraju Chada, Krishna P Sigdel, Raghavendar Reddy Sanganna Gari, Tina Rezaie Matin, Linda L Randall, Gavin M King

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 61 citations in OpenAlex.

  1. Artifacts and Practical Issues in Atomic Force Microscopy.Methods in molecular biology (Clifton, N.J.) · 2027
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  17. Protein Translocation Activity in Surface-Supported Lipid Bilayers.Langmuir : the ACS journal of surfaces and colloids · 2019
    Article
  18. Direct visualization of theScience advances · 2019
    Article
  19. Article
  20. 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.

Nagaraju ChadaDepartment of Physics and Astronomy, University of Missouri-Columbia, Columbia, Missouri 65211 USA.
Krishna P SigdelDepartment of Physics and Astronomy, University of Missouri-Columbia, Columbia, Missouri 65211 USA.
Raghavendar Reddy Sanganna GariDepartment of Physics and Astronomy, University of Missouri-Columbia, Columbia, Missouri 65211 USA.
Tina Rezaie MatinDepartment of Physics and Astronomy, University of Missouri-Columbia, Columbia, Missouri 65211 USA.
Linda L RandallDepartment of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211 USA.
Gavin M King1] Department of Physics and Astronomy, University of Missouri-Columbia, Columbia, Missouri 65211 USA [2] Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211 USA.
University of Missouri · US

Funding

The Export of Proteins in Escherichia Coli; Administrative Supplement for EquipmentR01GM029798 · NIGMS · WASHINGTON STATE UNIVERSITY · PI RANDALL, LINDA L. · 1985 to 2019
$7.7M
EXPORT OF PROTEINS IN ESCHERICHIA COLIR37GM029798 · NIGMS · WASHINGTON STATE UNIVERSITY · PI RANDALL, LINDA L. · 1993 to 2002
$1.1M
NIGMS NIH HHS GM29798NIGMS NIH HHS R01 GM029798NIGMS NIH HHS R37 GM029798
6 · The paper itself

Abstract

Though ubiquitous in optical microscopy, glass has long been overlooked as a specimen supporting surface for high resolution atomic force microscopy (AFM) investigations due to its roughness. Using bacteriorhodopsin from Halobacterium salinarum and the translocon SecYEG from Escherichia coli, we demonstrate that faithful images of 2D crystalline and non-crystalline membrane proteins in lipid bilayers can be obtained on microscope cover glass following a straight-forward cleaning procedure. Direct comparison between AFM data obtained on glass and on mica substrates show no major differences in image fidelity. Repeated association of the ATPase SecA with the cytoplasmic protrusion of SecYEG demonstrates that the translocon remains competent for binding after tens of minutes of continuous AFM imaging. This opens the door for precision long-timescale investigations of the active translocase in near-native conditions and, more generally, for integration of high resolution biological AFM with many powerful optical techniques that require non-birefringent substrates.

Indexed as

GlassAdenosine TriphosphatasesAluminum SilicatesBacterial ProteinsBacteriorhodopsinsEscherichia coli ProteinsHalobacterium salinarumImage Processing, Computer-AssistedLipid BilayersMembrane ProteinsMembrane Transport ProteinsMicroscopy, Atomic ForceSecA ProteinsSEC Translocation ChannelsAdenosine TriphosphatasesAluminum SilicatesBacterial ProteinsBacteriorhodopsinsEscherichia coli ProteinsLipid BilayersMembrane ProteinsMembrane Transport ProteinsmicaSecA ProteinsSEC Translocation Channels

Identifiers

PMID26228793
PMCPMC4521160
OpenAlexW1006646293

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.