Evidence map›Paper›PMID 40364740›Full record

ReviewChemical communications (Cambridge, England)2025

Protein and peptide confinement within metal-organic materials.

Jack D Wright, Tongtong Zhang, Xiangyu Wang, Imogen A Riddell

Abstract readReview
In one paragraph

Review in Chemical communications (Cambridge, England), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–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

2 citing papers in PubMed.

  1. Review
  2. 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.

Jack D WrightDepartment of Chemistry, The University of Manchester, Oxford Road, Manchester M13 9PL, UK. imogen.riddell@manchester.ac.uk.
Tongtong ZhangDepartment of Chemistry, The University of Manchester, Oxford Road, Manchester M13 9PL, UK. imogen.riddell@manchester.ac.uk.
Xiangyu WangDepartment of Chemistry, The University of Manchester, Oxford Road, Manchester M13 9PL, UK. imogen.riddell@manchester.ac.uk.
Imogen A RiddellDepartment of Chemistry, The University of Manchester, Oxford Road, Manchester M13 9PL, UK. imogen.riddell@manchester.ac.uk.ORCID http://orcid.org/0000-0002-6801-0198

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metal-organic materials (MOMs), including both discrete metal-organic cages (MOCs) and metal-organic frameworks (MOFs), are emerging as promising materials for peptide and protein immobilisation. In particular, the ease of synthesis of MOMs alongside their well-defined and modular internal void spaces makes them appealing when considering routes to immobilise and stabilise peptides and proteins outside of biological environments whilst retaining their native activity. Here we review recent advances made in understanding the conformation of peptidic materials confined within MOMs and the enzymes@MOF constructs which show the best enzymatic performance. We highlight opportunities for further advancement in each of these areas and proposed that complementary approaches taken by the MOC and MOF communities might be fruitfully combined to advance our understanding and the development of peptide/protein@MOM applications.

Indexed as

Metal-Organic FrameworksPeptidesProteinsMetal-Organic FrameworksPeptidesProteins

Identifiers

PMID40364740
PMCPMC12076117

What OpenQuestion holds

Textmetadata
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.