Evidence map›Paper›PMID 20160113›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

pH (low) insertion peptide (pHLIP) inserts across a lipid bilayer as a helix and exits by a different path.

Oleg A Andreev, Alexander G Karabadzhak, Dhammika Weerakkody, Gregory O Andreev, Donald M Engelman, Yana K Reshetnyak

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

90 citing papers in PubMed, 166 citations in OpenAlex.

  1. Review
  2. Self-Assembling Short Peptide Carriers for Gene Delivery.International journal of molecular sciences · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.Journal of chemical information and modeling · 2023
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. pHLIP Peptides Target Acidity in Activated Macrophages.Molecular imaging and biology · 2022
    Article
  20. Review

30 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 1 country.

Oleg A AndreevPhysics Department, University of Rhode Island, 2 Lippitt Road, Kingston, RI 02881, USA. andreev@mail.uri.edu
Alexander G Karabadzhak
Dhammika Weerakkody
Gregory O Andreev
Donald M Engelman
Yana K Reshetnyak
University of Rhode Island · USUniversity of California, San Diego · USYale University · US

Funding

TM INTERACTIONS IN MEMBRANE PROTEIN FOLDING AND FUNCTIONR01GM073857 · NIGMS · YALE UNIVERSITY · PI ANDREEV, OLEG A, ENGELMAN, DONALD M. · 2006 to 2023
$8.4M
pHLIP Nanotechnology Platform for Cancer Imaging and TherapyR01CA133890 · NCI · UNIVERSITY OF RHODE ISLAND · PI ANDREEV, OLEG A, ENGELMAN, DONALD M. · 2008 to 2012
$3.8M
NCI NIH HHS R01 CA133890NIGMS NIH HHS R01 GM073857PHS HHS R01 133890
6 · The paper itself

Abstract

What are the molecular events that occur when a peptide inserts across a membrane or exits from it? Using the pH-triggered insertion of the pH low insertion peptide to enable kinetic analysis, we show that insertion occurs in several steps, with rapid (0.1 sec) interfacial helix formation, followed by a much slower (100 sec) insertion pathway to give a transmembrane helix. The reverse process of unfolding and peptide exit from the bilayer core, which can be induced by a rapid rise of the pH from acidic to basic, proceeds approximately 400 times faster than folding/insertion and through different intermediate states. In the exit pathway, the helix-coil transition is initiated while the polypeptide is still inside the membrane. The peptide starts to exit when about 30% of the helix is unfolded, and continues a rapid exit as it unfolds inside the membrane. These insights may guide understanding of membrane protein folding/unfolding and the design of medically useful peptides for imaging and drug delivery.

Indexed as

Lipid BilayersCircular DichroismHydrogen-Ion ConcentrationMembrane ProteinsProtein ConformationProtein FoldingSpectrometry, FluorescenceThermodynamicsLipid BilayersMembrane ProteinspHLIP protein

Identifiers

PMID20160113
PMCPMC2840156
OpenAlexW2169059963

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.