Evidence map›Paper›PMID 19766589›Full record

ArticleBiochimica et biophysica acta2010

Tuning the insertion properties of pHLIP.

Monika Musial-Siwek, Alexander Karabadzhak, Oleg A Andreev, Yana K Reshetnyak, Donald M Engelman

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

45 citing papers in PubMed, 75 citations in OpenAlex.

  1. Improving the Estimation of pThe journal of physical chemistry. B · 2026
    Article
  2. Article
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  5. Review
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  7. Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.Journal of chemical information and modeling · 2023
    Article
  8. A double-switch pHLIP system enables selective enrichment of circulating tumor microenvironment-derived extracellular vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Increasing the Realism ofJournal of chemical theory and computation · 2022
    Article
  10. CaProtein science : a publication of the Protein Society · 2022
    Article
  11. Article
  12. Pharmacokinetic modeling reveals parameters that govern tumor targeting and delivery by a pH-Low Insertion Peptide (pHLIP).Proceedings of the National Academy of Sciences of the United States of America · 2021
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  16. Review
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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

5 authors at 2 institutions in 1 country.

Monika Musial-SiwekDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
Alexander Karabadzhak
Oleg A Andreev
Yana K Reshetnyak
Donald M Engelman
University of Rhode Island · 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 CA133890NCI NIH HHS R01 CA133890NIGMS NIH HHS GM073857NIGMS NIH HHS R01 GM073857
6 · The paper itself

Abstract

The pH (low) insertion peptide (pHLIP) has exceptional characteristics: at neutral pH it is an unstructured monomer in solution or when bound to lipid bilayer surfaces, and it inserts across a lipid bilayer as a monomeric alpha-helix at acidic pH. The peptide targets acidic tissues in vivo and may be useful in cancer biology for delivery of imaging or therapeutic molecules to acidic tumors. To find ways to vary its useful properties, we have designed and analyzed pHLIP sequence variants. We find that each of the Asp residues in the transmembrane segment is critical for solubility and pH-dependent membrane insertion of the peptide. Changing both of the Asp residues in the transmembrane segment to Glu, inserting an additional Asp into the transmembrane segment, or replacing either of the Asp residues with Ala leads to aggregation and/or loss of pH-dependent membrane insertion of the peptide. However, variants with either of the Asp residues changed to Glu remained soluble in an aqueous environment and inserted into the membrane at acidic pH with a higher pK(app) of membrane insertion.

Indexed as

Drug Delivery SystemsAnimalsCell MembraneHumansHydrogen-Ion ConcentrationMembrane ProteinsNeoplasmsProtein Structure, SecondaryMembrane ProteinspHLIP protein

Identifiers

PMID19766589
PMCPMC2862812
OpenAlexW2108623294

What OpenQuestion holds

Textmetadata
LicenceTDM
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.