Ion-selective conformational stabilization of a disordered repeats-in-toxin protein domain.

Alana P Gudinas, Gatha M Shambharkar, Marina P Chang, Daniel Fernández, Tsutomu Matsui, Danielle J Mai

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Article in Biophysical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

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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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Alana P GudinasDepartment of Physics, Stanford University, Stanford, California.

Gatha M ShambharkarDepartment of Materials Science & Engineering, Stanford University, Stanford, California.

Marina P ChangDepartment of Materials Science & Engineering, Stanford University, Stanford, California.

Daniel FernándezMacromolecular Structure Group, Nucleus at Sarafan ChEM-H, Stanford University, Stanford, California.

Tsutomu MatsuiStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California.

Danielle J MaiDepartment of Materials Science & Engineering, Stanford University, Stanford, California; Department of Chemical Engineering, Stanford University, Stanford, California. Electronic address: djmai@stanford.edu.

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Thomas Michael Weiss · 2020 to 2026

$43.3M

NIGMS NIH HHS P30 GM133894

6 · The paper itself

Abstract

Ion-binding intrinsically disordered proteins (IDPs) recruit and bind to specific metal ions to perform critical biological functions. In proteins where ion binding and structural transitions are coupled, interactions with off-target toxic metals can dramatically disrupt protein structure and function, exemplified by lead and mercury poisoning. Understanding the complex mechanisms underlying how IDPs exclude or allow binding to different ionic species is crucial for addressing the origins of metal toxicity in biological systems. Here, we elucidate mechanisms of ion selectivity in an IDP that adopts a structure upon Ca

Indexed as

Intrinsically Disordered ProteinsCalciumMagnesiumModels, MolecularProtein DomainsProtein StabilityScattering, Small AngleCalciumIntrinsically Disordered ProteinsMagnesium

Identifiers

PMID41088755

DOI10.1016/j.bpj.2025.10.014

PMCPMC12821022

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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.