Evidence map›Paper›PMID 35055136›Full record

ArticleInternational journal of molecular sciences2022

Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains.

Rosaria Russo, Margherita Romeo, Tim Schulte, Martina Maritan, Luca Oberti, Maria Monica Barzago, Alberto Barbiroli, Carlo Pappone, Luigi Anastasia, Giovanni Palladini and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 40% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. 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

12 authors at 5 institutions in 1 country.

Rosaria RussoDipartimento di Fisiopatologia Medico-Chirurgica e Dei Trapianti, Università Degli Studi di Milano, 20090 Segrate, Italy.ORCID 0000-0003-0011-5775
Margherita RomeoDipartimento di Biochimica e Farmacologia Molecolare, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, 20156 Milan, Italy.ORCID 0000-0002-3020-8545
Tim SchulteInstitute of Molecular and Translational Cardiology, IRCCS Policlinico San Donato, 20097 Milan, Italy.
Martina MaritanDipartimento di Bioscienze, Università Degli Studi di Milano, 20133 Milano, Italy.
Luca ObertiDipartimento di Bioscienze, Università Degli Studi di Milano, 20133 Milano, Italy.
Maria Monica BarzagoDipartimento di Biochimica e Farmacologia Molecolare, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, 20156 Milan, Italy.
Alberto BarbiroliDipartimento di Scienze per gli Alimenti, La Nutrizione e L'Ambiente, Università Degli Studi di Milano, 20133 Milan, Italy.ORCID 0000-0003-1678-5431
Carlo PapponeInstitute of Molecular and Translational Cardiology, IRCCS Policlinico San Donato, 20097 Milan, Italy.
Luigi AnastasiaInstitute of Molecular and Translational Cardiology, IRCCS Policlinico San Donato, 20097 Milan, Italy.
Giovanni PalladiniAmyloidosis Treatment and Research Center, Fondazione IRCCS Policlinico San Matteo, Università Degli Studi di Pavia, 27100 Pavia, Italy.ORCID 0000-0001-5994-5138
Luisa DiomedeDipartimento di Biochimica e Farmacologia Molecolare, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, 20156 Milan, Italy.ORCID 0000-0002-2258-0531
Stefano RicagnoInstitute of Molecular and Translational Cardiology, IRCCS Policlinico San Donato, 20097 Milan, Italy.ORCID 0000-0001-6678-5873
University of Milan · ITMario Negri Institute for Pharmacological Research · ITVita-Salute San Raffaele University · ITIRCCS Policlinico San Donato · ITIstituti di Ricovero e Cura a Carattere Scientifico · IT

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
Fondazione Cariplo 2016-0489Fondazione Italiana di Ricerca per la Sclerosi Laterale Amiotrofica TDP- 43-STRUCTMinistero della Salute RF-2016-02361756NIH HHS P40 OD010440Telethon Foundation GGP17036
6 · The paper itself

Abstract

Light chain amyloidosis (AL) is caused by the aberrant overproduction of immunoglobulin light chains (LCs). The resulting abnormally high LC concentrations in blood lead to deposit formation in the heart and other target organs. Organ damage is caused not only by the accumulation of bulky amyloid deposits, but extensive clinical data indicate that circulating soluble LCs also exert cardiotoxic effects. The nematode

Indexed as

Amino Acid SubstitutionAnimalsCaenorhabditis elegansCalorimetryCopperDisease Models, AnimalHistidineHumansImmunoglobulin Light-chain AmyloidosisImmunoglobulin Light ChainsModels, MolecularProtein ConformationReactive Oxygen SpeciesCopperHistidineImmunoglobulin Light ChainsReactive Oxygen Speciescopper bindingcopper ionslight chain amyloidosisprotein aggregationsoluble toxicity

Identifiers

PMID35055136
PMCPMC8780072
OpenAlexW4206610511

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.