Evidence map›Paper›PMID 31755215›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Photobodies: Light-Activatable Single-Domain Antibody Fragments.

Benedikt Jedlitzke, Zahide Yilmaz, Wolfgang Dörner, Henning D Mootz

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

25 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Photoactivatable Nanobody Conjugate Dimerizer Temporally Resolves Tiam1-Rac1 Signaling Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Engineering Homogeneous Photoactive Antibody Fragments.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  12. Article
  13. A Light-Activatable Photocaged Variant of the Ultra-High Affinity ALFA-Tag Nanobody.Chembiochem : a European journal of chemical biology · 2022
    Article
  14. Efficient Amber SuppressionACS synthetic biology · 2022
    Article
  15. Article
  16. Writing and erasing O-GlcNAc from target proteins in cells.Biochemical Society transactions · 2021
    Article
  17. Structure-based design of a photoswitchable affibody scaffold.Protein science : a publication of the Protein Society · 2021
    Article
  18. Article
  19. Review
  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

4 authors.

Benedikt JedlitzkeInstitute of Biochemistry, Department of Chemistry and Pharmacy, University of Muenster, Wilhelm-Klemm-Str. 2, 48149, Münster, Germany.ORCID 0000-0001-7300-4131
Zahide YilmazInstitute of Biochemistry, Department of Chemistry and Pharmacy, University of Muenster, Wilhelm-Klemm-Str. 2, 48149, Münster, Germany.
Wolfgang DörnerInstitute of Biochemistry, Department of Chemistry and Pharmacy, University of Muenster, Wilhelm-Klemm-Str. 2, 48149, Münster, Germany.
Henning D MootzInstitute of Biochemistry, Department of Chemistry and Pharmacy, University of Muenster, Wilhelm-Klemm-Str. 2, 48149, Münster, Germany.ORCID 0000-0002-3385-0234

Funding

Deutsche Forschungsgemeinschaft MO1073/7-1
6 · The paper itself

Abstract

Photocaged antibody fragments, termed photobodies, have been developed that are impaired in their antigen-binding capacity and can be activated by irradiation with UV light (365 nm). This rational design concept builds on the selective photocaging of a single tyrosine in a nanobody (a single-domain antibody fragment). Tyrosine is a frequently occurring residue in central positions of the paratope region. o-Nitrobenzyl-protected tyrosine variants were incorporated into four nanobodies, including examples directed against EGFR and HER2, and photodeprotection restores the native sequence. An anti-GFP photobody exhibited an at least 10 000-fold impaired binding affinity before photodeprotection compared with the parent nanobody. A bispecific nanobody-photobody fusion protein was generated to trigger protein heterodimerization by light. Photoactivatable antibodies are expected to become versatile protein reagents and to enable novel approaches in diagnostic and therapeutic applications.

Indexed as

AntibodiesSingle-Domain AntibodiesAntibodiesSingle-Domain Antibodiesantibodiesnanobodiesphotochemistryprotein-protein interactionsunnatural amino acids

Identifiers

PMID31755215
PMCPMC7004160

What OpenQuestion holds

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LicenceCC BY
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.