Evidence map›Paper›PMID 31193333›Full record

ArticleAlzheimer's & dementia (New York, N. Y.)2019

In vitro degradation of β-amyloid fibrils by microbial keratinase.

Debananda S Ningthoujam, Saikat Mukherjee, Laishram Jaya Devi, Elangbam Shanta Singh, Keising Tamreihao, Rakhi Khunjamayum, Sumita Banerjee, Debashis Mukhopadhyay

Open access · goldAbstract read
In one paragraph

Article in Alzheimer's & dementia (New York, N. Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 23 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Debananda S NingthoujamDepartment of Biochemistry, Advanced Level State Biotech Hub, Microbial Biotechnology Research Laboratory, Manipur University, Imphal, Manipur, India.
Saikat MukherjeeDepartment of Biochemistry, Advanced Level State Biotech Hub, Microbial Biotechnology Research Laboratory, Manipur University, Imphal, Manipur, India.
Laishram Jaya DeviDepartment of Biochemistry, Advanced Level State Biotech Hub, Microbial Biotechnology Research Laboratory, Manipur University, Imphal, Manipur, India.
Elangbam Shanta SinghDepartment of Biochemistry, Advanced Level State Biotech Hub, Microbial Biotechnology Research Laboratory, Manipur University, Imphal, Manipur, India.
Keising TamreihaoDepartment of Biochemistry, Advanced Level State Biotech Hub, Microbial Biotechnology Research Laboratory, Manipur University, Imphal, Manipur, India.
Rakhi KhunjamayumDepartment of Biochemistry, Advanced Level State Biotech Hub, Microbial Biotechnology Research Laboratory, Manipur University, Imphal, Manipur, India.
Sumita BanerjeeDepartment of Oral Pathology, Dental College, Regional Institute of Medical Sciences, Imphal, Manipur, India.
Debashis MukhopadhyayBiophysics and Structural Genomics Division, Saha Institute of Nuclear Physics, Kolkata, West Bengal, India.
Manipur University · INRegional Institute of Medical Sciences · INSaha Institute of Nuclear Physics · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionAmyloid fibrils are misfolded, protease-resistant forms of normal proteins. They are infectious such as prions or noninfectious such as β-amyloid (Aβ) fibrils causing Alzheimer's disease (AD). Prions and amyloids are structurally similar, possessing cross β-pleated sheet-like structures. As microbial keratinase could degrade prions, we tested keratinase activity on Aβ fibrils.

methodsLysozyme treated with urea generates Aβ fibrils demonstrated by immunoblotting with anti-Aβ antibody, high-performance liquid chromatography, and Congo red absorption spectroscopy. Two keratinases, Ker1 and Ker2, were purified from an actinomycete Amycolatopsis sp. MBRL 40 and incubated with Aβ fibrils.

resultsSoluble Ker1 and Ker1 reconstituted on neutral/cationic liposomes degraded Aβ fibrils efficiently. Ker 2 was less potent. DISCUSSION: Drugs that target AD inhibit acetylcholinesterase or formation of Aβ fibrils and downstream effects. These drugs have side effects and do not benefit globally in cognition. Keratinases are novel molecules for drug development against AD.

Indexed as

ActinomyceteIn vitro degradationKer 1Keratinaseβ-amyloid fibrils

Identifiers

PMID31193333
PMCPMC6527806
OpenAlexW2946701470

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.