Evidence map›Paper›PMID 22447980›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2012

Molecular mechanisms in the dramatic enhancement of HIV-1 Tat transduction by cationic liposomes.

Guan-Han Li, Wenxue Li, Russell J Mumper, Avindra Nath

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Observational
  3. Article
  4. Two-pore channels regulate Tat endolysosome escape and Tat-mediated HIV-1 LTR transactivation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Proteins reprogramming: present and future.TheScientificWorldJournal · 2012
    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 3 institutions in 1 country.

Guan-Han LiDepartment of Neurology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Wenxue Li
Russell J Mumper
Avindra Nath
Johns Hopkins University · USNational Institute of Neurological Disorders and Stroke · USUniversity of North Carolina at Chapel Hill · US

Funding

Neuropathogenesis of Retroviral InfectionsZIANS003130 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI NATH, AVINDRA · 2011 to 2025
$73.7M
Role of HIV Tat protein in pathogenesis of HIV dementiaR01NS039253 · NINDS · UNIVERSITY OF KENTUCKY · PI SCHNAAR, RONALD L · 1999 to 2014
$4.5M
Nanoparticle HIV Protein Vaccines for Cellular ResponsesR01AI058842 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MUMPER, RUSSELL J · 2005 to 2009
$1.5M
NIAID NIH HHS R01 AI058842NIAID NIH HHS R01AI058842NINDS NIH HHS R01 NS039253NINDS NIH HHS R01NS039253
6 · The paper itself

Abstract

Human immunodeficiency virus type 1 (HIV-1) transactivator of transcription (Tat) protein possesses a unique membrane-transduction property. Interestingly, Tat transduction could be dramatically increased 1000-fold based on LTR-transactivation assay when complexed with cationic liposomes (lipo-Tat), compared with Tat alone. Therefore, underlining mechanisms were explored further. Microscopy and flow cytometry showed that this effect was associated with enhanced membrane binding, large particle formation (1-2 μm) and increased intracellular uptake of Tat fluorescent proteins. Using pharmacological assays and immune colocalizations, it was found that lipid raft-dependent endocytosis and macropinocytosis were major pathways involved in lipo-Tat uptake, and actin-filaments played a major role in intracellular trafficking of lipo-Tat to the nucleus. Furthermore, we found that the Tat hydrophobic domain (aa 36-47) mediated formation of two positively charged molecules into lipo-Tat complexes via hydrophobic bonds, based on LTR-transactivation inhibition assay. Thus, the hydrophobic domain may play an important role in Tat protein uptake and be useful for intracellular delivery of biomacromolecules if coupled together with Tat basic peptide, a cell-penetrating peptide.

Indexed as

Actin CytoskeletonAmino Acid MotifsAmino Acid SequenceCationsCell LineEndocytosisHIV-1HIV Long Terminal RepeatHumansHydrophobic and Hydrophilic InteractionsLiposomesMembrane MicrodomainsPinocytosisProtein Transporttat Gene Products, Human Immunodeficiency VirusTranscriptional ActivationCationsLiposomestat Gene Products, Human Immunodeficiency Virus

Identifiers

PMID22447980
PMCPMC3382090
OpenAlexW2153194849

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.