Evidence map›Paper›PMID 22547390›Full record

ArticleNucleic acids research2012

KH domains with impaired nucleic acid binding as a tool for functional analysis.

David Hollingworth, Adela M Candel, Giuseppe Nicastro, Stephen R Martin, Paola Briata, Roberto Gherzi, Andres Ramos

Abstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
–field-weighted citation impact
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

85 citing papers in PubMed.

  1. Article
  2. Article
  3. Molecular genetic characterization of bacterial KH-domain proteins.bioRxiv : the preprint server for biology · 2026
    Article
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  5. MEX3A Modulates PPARγ Pathway Activity and Colorectal Cancer Growth.Cellular and molecular gastroenterology and hepatology · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Deletion ofFrontiers in behavioral neuroscience · 2025
    Article
  17. Review
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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

7 authors.

David HollingworthMolecular Structure Division, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.
Adela M Candel
Giuseppe Nicastro
Stephen R Martin
Paola Briata
Roberto Gherzi
Andres Ramos

Funding

Medical Research Council MC_U117533887Medical Research Council MC_U117574558Medical Research Council U117570592Medical Research Council U117574558
6 · The paper itself

Abstract

In eukaryotes, RNA-binding proteins that contain multiple K homology (KH) domains play a key role in coordinating the different steps of RNA synthesis, metabolism and localization. Understanding how the different KH modules participate in the recognition of the RNA targets is necessary to dissect the way these proteins operate. We have designed a KH mutant with impaired RNA-binding capability for general use in exploring the role of individual KH domains in the combinatorial functional recognition of RNA targets. A double mutation in the hallmark GxxG loop (GxxG-to-GDDG) impairs nucleic acid binding without compromising the stability of the domain. We analysed the impact of the GDDG mutations in individual KH domains on the functional properties of KSRP as a prototype of multiple KH domain-containing proteins. We show how the GDDG mutant can be used to directly link biophysical information on the sequence specificity of the different KH domains of KSRP and their role in mRNA recognition and decay. This work defines a general molecular biology tool for the investigation of the function of individual KH domains in nucleic acid binding proteins.

Indexed as

Amino Acid SequenceMolecular Sequence DataMutationProtein Interaction Domains and MotifsRNARNA-Binding ProteinsRNA, MessengerRNA StabilityTrans-ActivatorsKHSRP protein, humanRNARNA-Binding ProteinsRNA, MessengerTrans-Activators

Identifiers

PMID22547390
PMCPMC3413153

What OpenQuestion holds

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Registered trials

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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.