Cited by 26Lipid Membrane Structure and BehaviorCellular transport and secretionCaveolin-1 and cellular processes

Initiation and Dynamics of Hemifusion in Lipid Bilayers

Open access
Hed, Guy, Safran, S.A.·2003·Biophysical Journal

Abstract

One approach to the understanding of fusion in cells and model membranes involves stalk formation and expansion of the hemifusion diaphragm. We predict theoretically the initiation of hemifusion by stalk expansion and the dynamics of mesoscopic hemifusion diaphragm expansion in the light of recent experiments and theory that suggested that hemifusion is driven by intramembrane tension far from the fusion zone. Our predictions include a square-root scaling of the hemifusion zone size on time as well as an estimate of the minimal tension for initiation of hemifusion. Whereas a minimal amount of pressure is evidently needed for stalk formation, it is not necessarily required for stalk expansion. The energy required for tension-induced fusion is much smaller than that required for pressure-driven fusion.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/s0006-3495(03)74482-8

Cites

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Fusogenic proteins mediate membrane fusion by pulling the membranes into contact to overcome the high energy barrier imposed by hydration repulsion.

    “It is often considered in the presence of fusogenic proteins, which mediate the fusion by pulling the membranes into contact to overcome the high energy barrier imposed by hydration repulsion [4][5][6][7] .”

    From Fusion of lipid membranes: an alternative pathway (2026) · cites this paper as [6]

    Section IV (Boundary Conditions and Global Dynamics; page unavailable) says fusion proteins promote stalk formation and expansion, and describes SNARE proteins as pulling on a stalk to widen it—not pulling two membranes into contact. Section VI (The Role of Pressure; page unavailable) explains that hydration forces maintain a water layer between bilayers, but does not say proteins overcome that barrier by drawing the membranes together. (LLM, conf=0.86)

    Experimental — accuracy not yet measured
  • Lipid headgroups forming membrane surfaces are highly hydrophilic and hydrated, imposing a high energy barrier for two membranes to fuse due to hydration repulsion.

    “The lipidic headgroups forming the membranes' surface are highly hydrophilic and hydrated, imposing a high energy barrier for two membranes to fuse due to hydration repulsion [4][5][6][7] .”

    From Fusion of lipid membranes: an alternative pathway (2026) · cites this paper as [6]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

No references could be resolved yet.

Research works printed but not linked: 3

  1. Arnold, K. 1995. Cation induced vesicle fusion modulated by polymers and proteins. In Handbook of Biological Physics, Vol. 1B. R. Lipowsky, and E. Sackman, editors. Elsevier, Amsterdam.
  2. Ben-Shaul, A. 1995. Molecular theory of chain packing, elas- ticity and lipid-protein interaction in lipid bilayers. In Handbook of Biological Physics, Vol. 1B. R. Lipowsky, and E. Sackman, editors. Elsevier, Amsterdam.
  3. Israelachvili, J. 1991. Intermolecular & surface forces, Chap- ter 17. Academic Press, London, 2nd edition.

Cited by

Sorted by citations

Authors
Hed, G., & Safran, S. A.
Affiliations
Weizmann Institute of Science (IL)
Corresponding author
Hed, Guy
Venue
Biophysical Journal
Publisher
Elsevier BV
Published
2003-07
Volume
85
Issue
1
Pages
381-389
ISSN
0006-3495 (ISSN-L)
OpenAlex
W2055865545
Cited by
26
References
0
Citations by year
2026: 3 · 2021: 1 · 2019: 1 · 2018: 2 · 2017: 1 · 2015: 1 · 2014: 2 · 2012: 3
FWCI
0.43
Type
journal article
Language
en
Open access
Locations
  • Biophysical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • arXiv (Cornell University) (submittedVersion)
  • arXiv (Cornell University)
  • APS March Meeting Abstracts
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Keywords
hemifusion, lipid bilayers, stalk formation, membrane fusion, membrane mechanics
MeSH terms
Computer Simulation, Lipid Bilayers, Membrane Fluidity, Membrane Fusion, Membranes, Artificial, Models, Chemical, Models, Molecular, Molecular Conformation, Surface Tension, Viscosity, Water, Friction, Macromolecular Substances

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review