Evidence map›Paper›PMID 7724529›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Phenotypic knockout of the high-affinity human interleukin 2 receptor by intracellular single-chain antibodies against the alpha subunit of the receptor.

J H Richardson, J G Sodroski, T A Waldmann, W A Marasco

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

19 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Applying Antibodies Inside Cells: Principles and Recent Advances in Neurobiology, Virology and Oncology.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's disease.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  11. Article
  12. Generation of recombinant antibodies.Molecular biotechnology · 1999
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. 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

4 authors at 1 institution in 1 country.

J H RichardsonDepartment of Pathology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.
J G Sodroski
T A Waldmann
W A Marasco
Dana-Farber Cancer Institute · US

Funding

VectorP30CA006516 · NCI · DANA-FARBER CANCER INSTITUTE · PI A. Heather Eliassen · 1985 to 2026
$330.6M
DFCI-BIDMC-CH CENTER FOR AIDS RESEARCHP30AI028691 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1989 to 2003
$6.2M
MECHANISM OF ACTION OF THE TAT PRODUCT OF HIV-1R01AI028785 · NIAID · DANA-FARBER CANCER INSTITUTE · PI MARASCO, WAYNE A. · 1989 to 2002
$637k
NCI NIH HHS P30 CA06516NIAID NIH HHS AI28785NIAID NIH HHS P30 AI28691
6 · The paper itself

Abstract

The experimental manipulation of peptide growth hormones and their cellular receptors is central to understanding the pathways governing cellular signaling and growth control. Previous work has shown that intracellular antibodies targeted to the endoplasmic reticulum (ER) can be used to capture specific proteins as they enter the ER, preventing their transport to the cell surface. Here we have used this technology to inhibit the cell surface expression of the alpha subunit of the high-affinity interleukin 2 receptor (IL-2R alpha). A single-chain variable-region fragment of the anti-Tac monoclonal antibody was constructed with a signal peptide and a C-terminal ER retention signal. Intracellular expression of the single-chain antibody was found to completely abrogate cell surface expression of IL-2R alpha in stimulated Jurkat T cells. IL-2R alpha was detectable within the Jurkat cells as an immature 40-kDa form that was sensitive to endoglycosidase H, consistent with its retention in a pre- or early Golgi compartment. A single-chain antibody lacking the ER retention signal was also able to inhibit cell surface expression of IL-2R alpha although the mechanism appeared to involve rapid degradation of the receptor chain within the ER. These intracellular antibodies will provide a valuable tool for examining the role of IL-2R alpha in T-cell activation, IL-2 signal transduction, and the deregulated growth of leukemic cells which overexpress IL-2R alpha.

Indexed as

Amino Acid SequenceAntibodiesBase SequenceCell CompartmentationEndoplasmic ReticulumGenetic TherapyHumansImmunoglobulin FragmentsImmunoglobulin Variable RegionLeukemia, T-CellMolecular Sequence DataPhenotypeReceptors, Interleukin-2Recombinant ProteinsT-LymphocytesAntibodiesImmunoglobulin Fragmentsimmunoglobulin FvImmunoglobulin Variable RegionReceptors, Interleukin-2Recombinant Proteins

Identifiers

PMID7724529
PMCPMC42120
OpenAlexW2080431132

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.