Evidence map›Paper›PMID 40557600›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025

Amyloid Forming Human Lysozyme Intermediates are Stabilized by Non-Native Amide-π Interactions.

Minkoo Ahn, Julian O Streit, Christopher A Waudby, Tomasz Włodarski, Angelo Miguel Figueiredo, John Christodoulou, Janet R Kumita

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. 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
–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

2 citing papers in PubMed.

  1. Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026
    Article
  2. Article
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

7 authors.

Minkoo AhnSchool of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.ORCID https://orcid.org/0000-0001-9131-7334
Julian O StreitResearch Department of Structural and Molecular Biology, Biosciences, University College London, Gower Street, London, WC1E 6BT, UK.ORCID https://orcid.org/0000-0001-6114-3636
Christopher A WaudbyResearch Department of Structural and Molecular Biology, Biosciences, University College London, Gower Street, London, WC1E 6BT, UK.ORCID https://orcid.org/0000-0001-7810-3753
Tomasz WłodarskiResearch Department of Structural and Molecular Biology, Biosciences, University College London, Gower Street, London, WC1E 6BT, UK.ORCID https://orcid.org/0000-0001-6498-334X
Angelo Miguel FigueiredoResearch Department of Structural and Molecular Biology, Biosciences, University College London, Gower Street, London, WC1E 6BT, UK.ORCID https://orcid.org/0000-0001-7039-5341
John ChristodoulouResearch Department of Structural and Molecular Biology, Biosciences, University College London, Gower Street, London, WC1E 6BT, UK.ORCID https://orcid.org/0000-0002-6710-3843
Janet R KumitaCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID https://orcid.org/0000-0002-3887-4964

Funding

Fundação para a Ciência e a Tecnologia (FCT) 2024.07359.IACDCFundação para a Ciência e a Tecnologia (FCT) UIDP/00313/2020Medical Research Council MR/W01632X/1Wellcome Trust 094425/Z/10/ZWellcome Trust 097806/Z/11/ZWellcome Trust 206409/Z/17/ZWellcome Trust FC001029
6 · The paper itself

Abstract

Mutational variants of human lysozyme cause a rare but fatal hereditary systemic amyloidosis by populating an intermediate state that self-assembles into amyloid fibrils. However, this intermediate state is recalcitrant to detailed structural investigation, as it is only transiently and sparsely populated. Here, this work investigates the intermediate state of an amyloid-forming human lysozyme variant (I59T) using CEST and CPMG RD NMR at low pH.

Indexed as

AmidesAmyloidMuramidaseHumansMolecular Dynamics SimulationProtein FoldingThermodynamicsAmidesAmyloidMuramidaseamide‐π interactionsamyloidCEST NMRhuman lysozymeMD simulationsprotein intermediate

Identifiers

PMID40557600
PMCPMC12442690

What OpenQuestion holds

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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.