Evidence map›Paper›PMID 25937845›Full record

ArticleChemCatChem2014

Self-Assembly of Amyloid Fibrils That Display Active Enzymes.

Xiao-Ming Zhou, Aiman Entwistle, Hong Zhang, Antony P Jackson, Thomas O Mason, Ulyana Shimanovich, Tuomas P J Knowles, Andrew T Smith, Elizabeth B Sawyer, Sarah Perrett

Open access · bronzeAbstract read
In one paragraph

Article in ChemCatChem, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 43 citations in OpenAlex.

  1. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
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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

10 authors at 3 institutions in 3 countries.

Xiao-Ming ZhouNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences 15 Datun Road, Chaoyang District, Beijing 100101 (China) ; Department of Chemistry, University of Cambridge Lensfield Road, Cambridge CB2 1EW (UK) ; University of the Chinese Academy of Sciences 19 A Yuquanlu, Shijingshan District, Beijing 100049 (China).
Aiman EntwistleNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences 15 Datun Road, Chaoyang District, Beijing 100101 (China).
Hong ZhangNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences 15 Datun Road, Chaoyang District, Beijing 100101 (China).
Antony P JacksonNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences 15 Datun Road, Chaoyang District, Beijing 100101 (China) ; Department of Biochemistry, University of Cambridge Tennis Court Road, Cambridge CB2 1QW (UK).
Thomas O MasonDepartment of Chemistry, University of Cambridge Lensfield Road, Cambridge CB2 1EW (UK).
Ulyana ShimanovichDepartment of Chemistry, University of Cambridge Lensfield Road, Cambridge CB2 1EW (UK).
Tuomas P J KnowlesDepartment of Chemistry, University of Cambridge Lensfield Road, Cambridge CB2 1EW (UK).
Andrew T SmithSchool of Applied Sciences, RMIT University La Trobe Street, Melbourne, Victoria 3000 (Australia).
Elizabeth B SawyerNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences 15 Datun Road, Chaoyang District, Beijing 100101 (China).
Sarah PerrettNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences 15 Datun Road, Chaoyang District, Beijing 100101 (China) ; Department of Chemistry, University of Cambridge Lensfield Road, Cambridge CB2 1EW (UK).
Chinese Academy of Sciences · CNUniversity of Cambridge · GBLa Trobe University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme immobilization is an important strategy to enhance the stability and recoverability of enzymes and to facilitate the separation of enzymes from reaction products. However, enzyme purification followed by separate chemical steps to allow immobilization on a solid support reduces the efficiency and yield of the active enzyme. Here we describe polypeptide constructs that self-assemble spontaneously into nanofibrils with fused active enzyme subunits displayed on the amyloid fibril surface. We measured the steady-state kinetic parameters for the appended enzymes in situ within fibrils and compare these with the identical protein constructs in solution. Finally, we demonstrated that the fibrils can be recycled and reused in functional assays both in conventional batch processes and in a continuous-flow microreactor.

Indexed as

enzyme catalysisimmobilizationkineticsmicroreactorsnanostructures

Identifiers

PMID25937845
PMCPMC4413355
OpenAlexW2111174903

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.