Evidence map›Paper›PMID 24442234›Full record

ArticleRNA biology2014

Single-molecule FRET supports the two-state model of Argonaute action.

Adrian Zander, Phil Holzmeister, Daniel Klose, Philip Tinnefeld, Dina Grohmann

Open access · hybridAbstract read
In one paragraph

Article in RNA biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

45 citing papers in PubMed, 88 citations in OpenAlex.

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  14. Molecular and Spectroscopic Characterization of Green and Red Cyanine Fluorophores from the Alexa Fluor and AF Series*.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
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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

5 authors at 2 institutions in 1 country.

Adrian ZanderPhysikalische und Theoretische Chemie - NanoBioSciences; Technische Universität Braunschweig; Hans-Sommer-Strasse 10; Braunschweig, Germany.
Phil HolzmeisterPhysikalische und Theoretische Chemie - NanoBioSciences; Technische Universität Braunschweig; Hans-Sommer-Strasse 10; Braunschweig, Germany.
Daniel KloseDepartment of Physics; University of Osnabrück; Barbarastrasse 7; Osnabrück, Germany.
Philip TinnefeldPhysikalische und Theoretische Chemie - NanoBioSciences; Technische Universität Braunschweig; Hans-Sommer-Strasse 10; Braunschweig, Germany.
Dina GrohmannPhysikalische und Theoretische Chemie - NanoBioSciences; Technische Universität Braunschweig; Hans-Sommer-Strasse 10; Braunschweig, Germany.
Technische Universität Braunschweig · DEOsnabrück University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Argonaute can be found in all three domains of life and is the functional core of the eukaryotic RNA-silencing machinery. In order to shed light on the conformational changes that drive Argonaute action, we performed single-molecule FRET measurements employing a so far uncharacterized member of the Argonaute family, namely Argonaute from the archaeal organism Methanocaldococcus jannaschii (MjAgo). We show that MjAgo is a catalytically active Argonaute variant hydrolyzing exclusively DNA target strands out of a DNA/DNA hybrid. We studied the interplay between Argonaute and nucleic acids using fluorescent dyes covalently attached at different positions of the DNA guide as steric reporters. This allowed us to determine structurally confined parts of the protein scaffold and flexible regions of the DNA guide. Single-molecule FRET measurements demonstrate that the 3'end of the DNA guide is released from the PAZ domain upon target strand loading. This conformational change does not necessitate target strand cleavage but a fully complementary target strand. Thus, our data support the two state model for Argonaute action.

Indexed as

Argonaute ProteinsCloning, MolecularDNAFluorescence Resonance Energy TransferMethanocaldococcusModels, MolecularProtein BindingProtein ConformationProtein Structure, TertiarySequence Homology, Amino AcidArgonaute ProteinsDNAamber suppressor strategyArchaeaArgonautebiophysicsdynamicsfluorescenceFRETsingle-molecule fluorescence spectroscopy

Identifiers

PMID24442234
PMCPMC3929424
OpenAlexW2001738471

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.