Evidence map›Paper›PMID 14988507›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Microscopic observations reveal that fusogenic peptides induce liposome shrinkage prior to membrane fusion.

Fumimasa Nomura, Takehiko Inaba, Satoshi Ishikawa, Miki Nagata, Sho Takahashi, Hirokazu Hotani, Kingo Takiguchi

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

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  19. SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes.Proceedings of the National Academy of Sciences of the United States of America · 2008
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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

7 authors.

Fumimasa NomuraDepartment of Molecular Biology, School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.
Takehiko Inaba
Satoshi Ishikawa
Miki Nagata
Sho Takahashi
Hirokazu Hotani
Kingo Takiguchi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To study the mechanisms involved in membrane fusion, we visualized the fusion process of giant liposomes in real time by optical dark-field microscopy. To induce membrane fusion, we used (i) influenza hemagglutinin peptide (HA), a 20-aa peptide derived from the N-terminal fusion peptide region of the HA2 subunit, and (ii) two synthetic analogue peptides of HA, a negatively (E5) and positively (K5) charged analogue. We were able to visualize membrane fusion caused by E5 or by K5 alone, as well as by the mixture of these two peptides. The HA peptide however, did not induce membrane fusion, even at an acidic pH, which has been described as the optimal condition for the fusion of large unilamellar vesicles. Surprisingly, before membrane fusion, the shrinkage of liposomes was always observed. Our results suggest that a perturbation of lipid bilayers, which probably resulted from alterations in the bending folds of membranes, is a critical factor in fusion efficiency.

Indexed as

Amino Acid SequenceBiophysical PhenomenaBiophysicsHemagglutinin Glycoproteins, Influenza VirusIn Vitro TechniquesLiposomesMembrane FusionMicroscopy, VideoMolecular Sequence DataPhosphatidylcholinesProtein Structure, SecondarySequence Homology, Amino AcidViral Fusion ProteinsHemagglutinin Glycoproteins, Influenza VirusLiposomesPhosphatidylcholinesViral Fusion Proteins

Identifiers

PMID14988507
PMCPMC373477

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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.