Evidence map›Paper›PMID 26835447›Full record

ReviewFrontiers in bioengineering and biotechnology2015

Synthetic Peptides as Protein Mimics.

Andrea Groß, Chie Hashimoto, Heinrich Sticht, Jutta Eichler

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in bioengineering and biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
8.2field-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

51 citing papers in PubMed, 153 citations in OpenAlex.

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  6. Design of a Multi-Epitope Vaccine Based onInternational journal of molecular sciences · 2025
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  19. Studying Peptide-Metal Ion Complex Structures by Solution-State NMR.International journal of molecular sciences · 2022
    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 at 1 institution in 1 country.

Andrea GroßDepartment of Chemistry and Pharmacy, University of Erlangen-Nuremberg , Erlangen , Germany.
Chie HashimotoDepartment of Chemistry and Pharmacy, University of Erlangen-Nuremberg , Erlangen , Germany.
Heinrich StichtInstitute of Biochemistry, University of Erlangen-Nuremberg , Erlangen , Germany.
Jutta EichlerDepartment of Chemistry and Pharmacy, University of Erlangen-Nuremberg , Erlangen , Germany.
Friedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The design and generation of molecules capable of mimicking the binding and/or functional sites of proteins represents a promising strategy for the exploration and modulation of protein function through controlled interference with the underlying molecular interactions. Synthetic peptides have proven an excellent type of molecule for the mimicry of protein sites because such peptides can be generated as exact copies of protein fragments, as well as in diverse chemical modifications, which includes the incorporation of a large range of non-proteinogenic amino acids as well as the modification of the peptide backbone. Apart from extending the chemical and structural diversity presented by peptides, such modifications also increase the proteolytic stability of the molecules, enhancing their utility for biological applications. This article reviews recent advances by this and other laboratories in the use of synthetic protein mimics to modulate protein function, as well as to provide building blocks for synthetic biology.

Indexed as

biomaterialspeptidesprotein mimicsprotein–protein interactionsstructure-based design

Identifiers

PMID26835447
PMCPMC4717299
OpenAlexW2293277814

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.