Evidence map›Paper›PMID 32999925›Full record

ReviewACS central science2020

Metal-Organic Frameworks for Enzyme Immobilization: Beyond Host Matrix Materials.

Xiaoliang Wang, Pui Ching Lan, Shengqian Ma

Open access · diamondAbstract readReview
In one paragraph

Review in ACS central science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
15.6field-weighted citation impact, top 1% 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

63 citing papers in PubMed, 370 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. RapidChemical science · 2026
    Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Reticular Chemistry: A Versatile Platform for Engineering Heterogenous Biocatalysts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  14. Enzyme Immobilization in Porous Crystals via Cage Encapsulation.Angewandte Chemie (International ed. in English) · 2025
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review

3 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Xiaoliang WangDepartment of Chemistry, University of South Florida, 4202 East Fowler Avenue, Tampa, Florida 33620, United States.
Pui Ching LanDepartment of Chemistry, University of North Texas, 1508 West Mulberry Street, Denton, Texas 76201, United States.
Shengqian MaDepartment of Chemistry, University of North Texas, 1508 West Mulberry Street, Denton, Texas 76201, United States.
University of North Texas · USUniversity of South Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme immobilization in metal-organic frameworks (MOFs) as a promising strategy is attracting the interest of scientists from different disciplines with the expansion of MOFs' development. Different from other traditional host materials, their unique strengths of high surface areas, large yet adjustable pore sizes, functionalizable pore walls, and diverse architectures make MOFs an ideal platform to investigate hosted enzymes, which is critical to the industrial and commercial process. In addition to the protective function of MOFs, the extensive roles of MOFs in the enzyme immobilization are being well-explored by making full use of their remarkable properties like well-defined structure, high porosity, and tunable functionality. Such development shifts the focus from the exploration of immobilization strategies toward functionalization. Meanwhile, this would undoubtedly contribute to a better understanding of enzymes in regards to the structural transformation after being hosted in a confinement environment, particularly to the orientation and conformation change as well as the interplay between enzyme and matrix MOFs. In this Outlook, we target a comprehensive review of the role diversities of the host matrix MOF based on the current enzyme immobilization research, along with proposing an outlook toward the future development of this field, including the representatives of potential techniques and methodologies being capable of studying the hosted enzymes.

Identifiers

PMID32999925
PMCPMC7517118
OpenAlexW3082203104

What OpenQuestion holds

Textmetadata
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.