Evidence map›Paper›PMID 22328160›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Design of a binding scaffold based on variable lymphocyte receptors of jawless vertebrates by module engineering.

Sang-Chul Lee, Keunwan Park, Jieun Han, Joong-jae Lee, Hyun Jung Kim, Seungpyo Hong, Woosung Heu, Yu Jung Kim, Jae-Seok Ha, Seung-Goo Lee and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
9.5field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 143 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Benchmarking AlphaFold for protein complex modeling reveals accuracy determinants.Protein science : a publication of the Protein Society · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Designed leucine-rich repeat proteins bind two muramyl dipeptide ligands.Protein science : a publication of the Protein Society · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

14 authors at 4 institutions in 1 country.

Sang-Chul LeeDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Korea.
Keunwan Park
Jieun Han
Joong-jae Lee
Hyun Jung Kim
Seungpyo Hong
Woosung Heu
Yu Jung Kim
Jae-Seok Ha
Seung-Goo Lee
Hae-Kap Cheong
Young Ho Jeon
Dongsup Kim
Hak-Sung Kim
Korea Advanced Institute of Science and Technology · KRKorea Basic Science Institute · KRKorea Research Institute of Bioscience and Biotechnology · KRChungbuk National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Repeat proteins have recently been of great interest as potential alternatives to immunoglobulin antibodies due to their unique structural and biophysical features. We here present the development of a binding scaffold based on variable lymphocyte receptors, which are nonimmunoglobulin antibodies composed of Leucine-rich repeat modules in jawless vertebrates, by module engineering. A template scaffold was first constructed by joining consensus repeat modules between the N- and C-capping motifs of variable lymphocyte receptors. The N-terminal domain of the template scaffold was redesigned based on the internalin-B cap by analyzing the modular similarity between the respective repeat units using a computational approach. The newly designed scaffold, termed "Repebody," showed a high level of soluble expression in bacteria, displaying high thermodynamic and pH stabilities. Ease of molecular engineering was shown by designing repebodies specific for myeloid differentiation protein-2 and hen egg lysozyme, respectively, by a rational approach. The crystal structures of designed repebodies were determined to elucidate the structural features and interaction interfaces. We demonstrate general applicability of the scaffold by selecting repebodies with different binding affinities for interleukin-6 using phage display.

Indexed as

Protein EngineeringAmino Acid SequenceAnimalsCircular DichroismConsensus SequenceCrystallography, X-RayHagfishesHydrogen-Ion ConcentrationLampreysModels, MolecularMolecular Sequence DataPeptide FragmentsPeptide LibraryProtein BindingProtein ConformationProtein StabilityPeptide FragmentsPeptide LibraryReceptors, ImmunologicRecombinant Fusion Proteins

Identifiers

PMID22328160
PMCPMC3295290
OpenAlexW2099641930

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.