Evidence map›Paper›PMID 41301538›Full record

ArticleBiomolecules2025

Structural and Functional Characterization of LIMCH1 and Its Agmatinase-like Region: A Case of Catalysis in a Highly Disordered Protein.

María-Belén Reyes, Allison Fuentes, Diego Bustamante, Fernando Retamal, Ignacia Lillo, Cristián Villegas, Juan-Pablo Carrasco, Martin Pereira-Silva, Marcell Gatica, Juan Román and 5 more

Abstract read
In one paragraph

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

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

15 authors.

María-Belén ReyesDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.
Allison FuentesDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.
Diego BustamanteDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.
Fernando RetamalDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.
Ignacia LilloDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.ORCID 0009-0008-7793-8992
Cristián VillegasDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.
Juan-Pablo CarrascoDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.
Martin Pereira-SilvaDepartamento de Biología, Facultad de Ciencias, Universidad de Chile, Ñuñoa, Santiago 7800003, Chile.ORCID 0009-0004-2196-6549
Marcell GaticaDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.
Juan RománDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.ORCID 0000-0002-9505-0953
Maximiliano FigueroaDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.ORCID 0000-0002-6563-1984
Yamil NeiraDepartamento de Análisis Instrumental, Facultad de Farmacia, Universidad de Concepción, Concepción 4030000, Chile.
José Martínez-OyanedelDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.ORCID 0000-0001-8616-7474
Víctor Castro-FernándezDepartamento de Biología, Facultad de Ciencias, Universidad de Chile, Ñuñoa, Santiago 7800003, Chile.ORCID 0000-0002-4309-6415
Elena UribeDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070409, Chile.

Funding

Fondo Nacional de Desarrollo Científico y Tecnológico 1230549University of Concepción VRID Nº2022000435-INI
6 · The paper itself

Abstract

Agmatine is a biogenic amine that functions as a neurotransmitter and exhibits anticonvulsant, antineurotoxic, and antidepressant properties. It can be metabolized into putrescine and urea by canonical agmatinases or by the agmatinase-like protein (ALP), which corresponds to the C-terminal region of the LIMCH1 protein. The amino acid sequence of ALP/LIMCH1 diverges significantly from that of canonical agmatinases and lacks the conserved residues typically required for coordination with Mn

Indexed as

Intrinsically Disordered ProteinsUreohydrolasesAmino Acid SequenceAnimalsCatalysisCatalytic DomainManganeseRatsRecombinant ProteinsagmatinaseIntrinsically Disordered ProteinsManganeseRecombinant ProteinsUreohydrolasesagmatinaseagmatinecircular dichroism spectroscopyLIMCH1

Identifiers

PMID41301538
PMCPMC12650571

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.