Evidence map›Paper›PMID 27778400›Full record

ReviewChemistry (Weinheim an der Bergstrasse, Germany)2016

Site-Selective Disulfide Modification of Proteins: Expanding Diversity beyond the Proteome.

Seah Ling Kuan, Tao Wang, Tanja Weil

Open access · hybridAbstract readReview
In one paragraph

Review in Chemistry (Weinheim an der Bergstrasse, Germany), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Multicyclic D-Stereospecific Hydrolase Dimer With High Sustained Activity.Angewandte Chemie (International ed. in English) · 2026
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  12. Not So Bioorthogonal Chemistry.Journal of the American Chemical Society · 2025
    Review
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  16. Article
  17. Review
  18. Review
  19. A phosphine-based redox method for direct conjugation of disulfides.Chemical communications (Cambridge, England) · 2022
    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

3 authors at 1 institution in 2 countries.

Seah Ling KuanInstitute of Organic Chemistry III, Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Tao WangInstitute of Organic Chemistry III, Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Tanja WeilInstitute of Organic Chemistry III, Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Universität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synthetic transformation of polypeptides with molecular accuracy holds great promise for providing functional and structural diversity beyond the proteome. Consequently, the last decade has seen an exponential growth of site-directed chemistry to install additional features into peptides and proteins even inside living cells. The disulfide rebridging strategy has emerged as a powerful tool for site-selective modifications since most proteins contain disulfide bonds. In this Review, we present the chemical design, advantages and limitations of the disulfide rebridging reagents, while summarizing their relevance for synthetic customization of functional protein bioconjugates, as well as the resultant impact and advancement for biomedical applications.

Indexed as

DisulfidesHumansPeptidesProteinsProteomeDisulfidesPeptidesProteinsProteomebioactive hybridsdisulfide rebridgingdrug deliverymultimodal proteinssite-selective protein modifications

Identifiers

PMID27778400
PMCPMC5600100
OpenAlexW2537629632

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.