Evidence map›Paper›PMID 17360423›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

RNA aptamers directed to discrete functional sites on a single protein structural domain.

Hua Shi, Xiaochun Fan, Aarti Sevilimedu, John T Lis

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Methods for Improving Aptamer Binding Affinity.Molecules (Basel, Switzerland) · 2016
    Review
  3. Review
  4. Article
  5. Array-based discovery of aptamer pairs.Analytical chemistry · 2015
    Article
  6. Article
  7. Peptide aptamers: development and applications.Current topics in medicinal chemistry · 2015
    Review
  8. Article
  9. Review
  10. Article
  11. Dynamic evolution and immunoreactivity of aptamers binding to polyclonal antibodies against MPT64 antigen of Mycobacterium tuberculosis.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2014
    Article
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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

4 authors at 2 institutions in 1 country.

Hua ShiDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA. hshi@albany.edu
Xiaochun Fan
Aarti Sevilimedu
John T Lis
Cornell University · USUniversity at Albany, State University of New York · US

Funding

NIGMS NIH HHS GM 40918
6 · The paper itself

Abstract

Cellular regulatory networks are organized such that many proteins have few interactions, whereas a few proteins have many. These densely connected protein "hubs" are critical for the system-wide behavior of cells, and the capability of selectively perturbing a subset of interactions at these hubs is invaluable in deciphering and manipulating regulatory mechanisms. SELEX-generated RNA aptamers are proving to be highly effective reagents for inhibiting targeted proteins, but conventional methods generate one or several aptamer clones that usually bind to a single target site most preferred by a nucleic acid ligand. We advance a generalized scheme for isolating aptamers to multiple sites on a target molecule by reducing the ability of the preferred site to select its cognate aptamer. We demonstrate the use of this scheme by generating aptamers directed to discrete functional surfaces of the yeast TATA-binding protein (TBP). Previously we selected "class 1" RNA aptamers that interfere with the TBP's binding to TATA-DNA. By masking TBP with TATA-DNA or an unamplifiable class 1 aptamer, we isolated a new aptamer class, "class 2," that can bind a TBP.DNA complex and is in competition with binding another general transcription factor, TFIIA. Moreover, we show that both of these aptamers inhibit RNA polymerase II-dependent transcription, but analysis of template-bound factors shows they do so in mechanistically distinct and unexpected ways that can be attributed to binding either the DNA or TFIIA recognition sites. These results should spur innovative approaches to modulating other highly connected regulatory proteins.

Indexed as

Aptamers, NucleotideBase SequenceBinding SitesEvolution, MolecularFungal ProteinsModels, MolecularMolecular ConformationMolecular Sequence DataNucleic AcidsPolymersProtein ConformationProtein Structure, TertiaryRNATATA-Box Binding ProteinTranscription Factor TFIIAAptamers, NucleotideFungal ProteinsNucleic AcidsPolymersRNATATA-Box Binding ProteinTranscription Factor TFIIA

Identifiers

PMID17360423
PMCPMC1820654
OpenAlexW1984213085

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.