Evidence map›Paper›PMID 38038947›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Engineering New Protease Inhibitors Using α

Seandean Lykke Harwood, Jan J Enghild

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. 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
4.3field-weighted citation impact, top 5% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Human α2-Macroglobulin: Architecture, Mechanisms, and Functional Implications.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  2. Review
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

2 authors at 1 institution in 1 country.

Seandean Lykke HarwoodDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Jan J EnghildDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark. jje@mbg.au.dk.
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protease inhibitors of the alpha-macroglobulin family (αM) have a unique mechanism that allows them to trap proteases that is dependent not on the protease's class, but rather on its cleavage specificity. Proteases trigger a conformational change in the αM protein by cleaving within a "bait region," resulting in the sequestering of the protease inside the αM molecule. This nonspecific inhibitory mechanism appears to have arisen early in the αM family, and the broad protease-trapping capacity that it allows may play a role in pathogen defense.Human α

Indexed as

Pregnancy-Associated alpha 2-Macroglobulinsalpha-MacroglobulinsEndopeptidasesEnzyme InhibitorsFemaleHumansMacroglobulinsPeptide HydrolasesPregnancyProtease Inhibitorsalpha-MacroglobulinsEndopeptidasesEnzyme InhibitorsMacroglobulinsPeptide HydrolasesPregnancy-Associated alpha 2-MacroglobulinsProtease InhibitorsBait regionMutagenesis in vitroProteaseProtease inhibitionProtein engineeringProteolysisα2-Macroglobulin

Identifiers

PMID38038947
OpenAlexW4389224812

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.