Evidence map›Paper›PMID 42046369›Full record

ArticleAdvanced materials (Deerfield Beach, Fla.)2026

Hierarchically Engineered Multi-Enzyme Nanoreactors for in vitro Drug Biosynthesis and Pathway Transplantation Into Cells.

Ainur Sharip, Somayah S Qutub, Manar M Farooqui, Walaa Baslyman, Nida Khalfay, Lukman O Alimi, Patricia Lopez Sanchez, Lingyun Zhao, Milena Chernyshevskaia, Giovanni Colombo and 3 more

Abstract read
In one paragraph

Article in Advanced materials (Deerfield Beach, Fla.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Ainur SharipBiomedical Sciences Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0000-0001-5307-4829
Somayah S QutubBiomedical Sciences Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0000-0001-6578-6006
Manar M FarooquiBiomedical Sciences Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0009-0007-5391-6732
Walaa BaslymanPhysical Science and Engineering Division (PSE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0000-0003-3548-022X
Nida KhalfayBiomedical Sciences Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0009-0000-0793-1199
Lukman O AlimiPhysical Science and Engineering Division (PSE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0000-0003-2626-6328
Patricia Lopez SanchezAnalytical Chemistry Core Laboratory, KAUST, Thuwal, Saudi Arabia.
Lingyun ZhaoImaging and Characterization Core Laboratory, KAUST, Thuwal, Saudi Arabia.
Milena ChernyshevskaiaBiomedical Sciences Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.
Giovanni ColomboBiomedical Sciences Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.
Niveen M KhashabPhysical Science and Engineering Division (PSE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0000-0003-2728-0666
Stefan T AroldBiomedical Sciences Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0000-0001-5278-0668
Raik GrünbergBiomedical Sciences Division, King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID https://orcid.org/0000-0001-9532-6043

Funding

King Abdullah University of Science and Technology BAS/1/1056-01-01King Abdullah University of Science and Technology BAS/1/1343-01-01King Abdullah University of Science and Technology URF/1/1976-36
6 · The paper itself

Abstract

Even though most proteins evolved to function within multi-protein systems such as metabolic networks or signaling pathways, most technical protein applications are based on isolated proteins, for example therapeutic antibodies or industrial enzymes. Reliable methods for the stabilization, in vitro operation and intracellular delivery of multi-protein systems could unlock new applications in green biotechnology, diagnostics, and medical therapy. We demonstrate that the entire violacein biosynthesis pathway, consisting of up to six separately purified enzymes, can be infiltrated into a hierarchically etched MIL-101(Fe) (eMIL) metal organic framework. eMIL nanoreactors reshaped pathway dynamics and reaction flows, multiplied violacein yield in vitro and enabled pathway reuse, lyophilization and storage. Moreover, eMIL nanoreactors delivered the six-protein system into mammalian cells, where it produced violacein from cell-provided substrates and cofactors. These findings pave the way for the design of "smart" stimuli-responsive multi-enzyme nanoreactors for biotechnological and medical applications.

Indexed as

EnzymesNanostructuresNanotechnologyProtein EngineeringHumansIndolesEnzymesIndolesviolaceinbiosynthesis pathwaysenzymesmetal‐organic frameworksmulti‐protein systemsnatural productsprotein deliveryprotein therapeutics

Identifiers

PMID42046369
PMCPMC13274686

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.