Evidence map›Paper›PMID 21755948›Full record

ArticleJournal of medicinal chemistry2011

Conformationally constrained peptides from CD2 to modulate protein-protein interactions between CD2 and CD58.

Ameya Gokhale, Thomas K Weldeghiorghis, Veena Taneja, Seetharama D Satyanarayanajois

Open access · greenAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Design of aptamer peptides for immunomodulation.Journal of enzyme inhibition and medicinal chemistry · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. CD58 Immunobiology at a Glance.Frontiers in immunology · 2021
    Review
  8. Article
  9. Article
  10. Homo- and Heterodimerization of Proteins in Cell Signaling: Inhibition and Drug Design.Advances in protein chemistry and structural biology · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Medicinal chemistry for 2020.Future medicinal chemistry · 2011
    Article
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.

Ameya GokhaleDepartment of Basic Pharmaceutical Sciences, College of Pharmacy, University of Louisiana at Monroe, Monroe, Louisiana 71201, United States.
Thomas K Weldeghiorghis
Veena Taneja
Seetharama D Satyanarayanajois
University of Louisiana at Monroe · USLouisiana State University · USMayo Clinic · US

Funding

Role of B cells in pathogenesis of Collagen-induced Arthritis in Humanized MiceR01AI075262 · NIAID · MAYO CLINIC ROCHESTER · PI TANEJA, VEENA · 2009 to 2012
$1.2M
Impact of smoking on immune response and arthritis in humanized miceR21AR060077 · NIAMS · MAYO CLINIC ROCHESTER · PI TANEJA, VEENA · 2010 to 2011
$379k
IasB is Essential for Surface Motility in P. aeruginosaR15AI060752 · NIAID · UNIVERSITY OF DAYTON · PI ROBINSON, JAYNE B · 2004 to 2004
$221k
NIAID NIH HHS AI60752NIAID NIH HHS R01 AI075262NIAID NIH HHS R15 AI060752NIAMS NIH HHS AR60077NIAMS NIH HHS R21 AR060077
6 · The paper itself

Abstract

Cell adhesion molecule CD2 and its ligand CD58 provide good examples of protein-protein interactions in cells that participate in the immune response. To modulate the cell adhesion interaction, peptides were designed from the discontinuous epitopes of the β-strand region of CD2 protein. The two strands were linked by a peptide bond. β-Strands in the peptides were nucleated by inserting a β-sheet-inducing (D)-Pro-Pro sequence or a dibenzofuran (DBF) turn mimetic with key amino acid sequences from CD2 protein that binds to CD58. The solution structures of the peptides (5-10) were studied by NMR and molecular dynamics simulations. The ability of these peptides to inhibit cell adhesion interaction was studied by E-rosetting and lymphocyte epithelial assays. Peptides 6 and 7 inhibit the cell adhesion activity with an IC(50) of 7 and 11 nM, respectively, in lymphocyte epithelial adhesion assay. NMR and molecular modeling results indicated that peptides 6 and 7 exhibited β-hairpin structure in solution.

Indexed as

Amino Acid SequenceAnimalsCaco-2 CellsCD2 AntigensCD58 AntigensCell AdhesionCell SurvivalHumansJurkat CellsMiceMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularPeptidesProtein ConformationProtein Interaction MappingRosette FormationCD2 AntigensCD58 AntigensPeptides

Identifiers

PMID21755948
PMCPMC3171192
OpenAlexW2027493019

What OpenQuestion holds

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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.