Evidence map›Paper›PMID 9465118›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Identification and characterization of a cell membrane nucleic acid channel.

B Hanss, E Leal-Pinto, L A Bruggeman, T D Copeland, P E Klotman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

29 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Protein Kinase C-α is a Critical Protein for Antisense Oligonucleotide-mediated Silencing in Mammalian Cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2016
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. DING proteins: numerous functions, elusive genes, a potential for health.Cellular and molecular life sciences : CMLS · 2013
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
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  20. Review
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 1 institution in 1 country.

B HanssDivision of Nephrology, Box 1243, Mt. Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029, USA. b_hanss@smtplink.mssm.edu
E Leal-Pinto
L A Bruggeman
T D Copeland
P E Klotman
BioScience Laboratories (United States) · US

Funding

MOLECULAR THERAPY FOR RENAL DISEASEP01DK050795 · NIDDK · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KLOTMAN, PAUL EVAN · 1996 to 2001
$1.3M
NIDDK NIH HHS 1PO1DK50795-02NIDDK NIH HHS P01 DK050795
6 · The paper itself

Abstract

We have identified a 45-kDa protein purified from rat renal brush border membrane that binds short single-stranded nucleic acid sequences. This activity was purified, reconstituted in proteoliposomes, and then fused with model planar lipid bilayers. In voltage-clamp experiments, the reconstituted 45-kDa protein functioned as a gated channel that allows the passage of nucleic acids. Channel activity was observed immediately after addition of oligonucleotide. Channel activity was not observed in the absence of purified protein or of oligonucleotide or when protein was heat-inactivated prior to forming proteoliposomes. In the presence of symmetrical buffered solution and oligonucleotide, current passed linearly over the range of holding potentials tested. Conductance was 10.4 +/- 0.4 picosiemens (pS) and reversal potential was 0.2 +/- 1.7 mV. There was no difference in channel conductance or reversal potential between phosphodiester and phosphorothioate oligonucleotides. Ion-substitution experiments documented a shift in reversal potential only when a concentration gradient for oligonucleotide was established, indicating that movement of oligonucleotide alone was responsible for current. Movement of oligonucleotide across the bilayer was confirmed by using 32P-labeled oligonucleotides. Channel open probability decreased significantly in the presence of heparan sulfate. These studies provide evidence for a cell surface channel that conducts nucleic acids.

Indexed as

AnimalsBiological TransportDNA-Binding ProteinsIon ChannelsKidneyLipid BilayersMaleMembrane ProteinsMicrovilliOligonucleotidesRatsRats, Sprague-DawleyDNA-Binding ProteinsIon ChannelsLipid BilayersMembrane ProteinsOligonucleotides

Identifiers

PMID9465118
PMCPMC19214
OpenAlexW2067049923

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.