Evidence map›Paper›PMID 21073201›Full record

ArticleBiochemistry2010

Dynamic origins of differential RNA binding function in two dsRBDs from the miRNA "microprocessor" complex.

Christopher Wostenberg, Kaycee A Quarles, Scott A Showalter

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Regulation of the microprocessor by post-translational modifications.Frontiers in cell and developmental biology · 2025
    Review
  2. The Functional Mechanism of MicroRNA in Oral Lichen Planus.Journal of inflammation research · 2022
    Review
  3. Article
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  7. Noncoding RNA as regulators of cardiac fibrosis: current insight and the road ahead.Pflugers Archiv : European journal of physiology · 2016
    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

3 authors at 1 institution in 1 country.

Christopher WostenbergDepartment of Chemistry, The Pennsylvania State University, 104 Chemistry Building, University Park, Pennsylvania 16802, United States.
Kaycee A Quarles
Scott A Showalter
Pennsylvania State University · US

Funding

Specificity of miRNA Processing Provided by Double-Stranded RNA Binding DomainsR01GM098451 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI SHOWALTER, SCOTT A · 2011 to 2015
$1.5M
NIGMS NIH HHS R01 GM098451
6 · The paper itself

Abstract

MicroRNAs (miRNAs) affect gene regulation by base pairing with mRNA and contribute to the control of cellular homeostasis. The first step in miRNA maturation is conducted in the nucleus by the "microprocessor" complex made up of an RNase III enzyme, Drosha, that contains one dsRNA binding domain (dsRBD), and DGCR8, that contains two dsRBDs in tandem. The crystal structure of DGCR8-Core (493-720), containing both dsRBDs, and the NMR solution structure of Drosha-dsRBD (1259-1337) have been reported, but the solution dynamics have not been explored for any of these dsRBDs. To better define the mechanism of dsRNA binding and thus the nuclear maturation step of miRNA processing, we report NMR spin relaxation and MD simulations of Drosha-dsRBD (1259-1337) and DGCR8-dsRBD1 (505-583). The study was motivated by electrophoretic mobility shift assays (EMSAs) of the two dsRBDs, which showed that Drosha-dsRBD does not bind a representative miRNA but isolated DGCR8-dsRBD1 does (K(d) = 9.4 ± 0.4 μM). Our results show that loop 2 in both dsRBDs is highly dynamic but the pattern of the correlations observed in MD is different for the two proteins. Additionally, the extended loop 1 of Drosha-dsRBD is more flexible than the corresponding loop in DGCR8-dsRBD1 but shows no correlation with loop 2, which potentially explains the lack of dsRNA binding by Drosha-dsRBD in the absence of the RNase III domains. The results presented in this study provide key structural and dynamic features of dsRBDs that contribute to the binding mechanism of these domains to dsRNA.

Indexed as

Amino Acid SequenceElectrophoretic Mobility Shift AssayHumansMagnetic Resonance SpectroscopyMicroRNAsMolecular Dynamics SimulationMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryRibonuclease IIISequence Homology, Amino AcidDROSHA protein, humanMicroRNAsRibonuclease III

Identifiers

PMID21073201
PMCPMC3565223
OpenAlexW2075467235

What OpenQuestion holds

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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.