Evidence map›Paper›PMID 35742891›Full record

ArticleInternational journal of molecular sciences2022

New Insights into the Determinants of Specificity in Human Type I Arginase: Generation of a Mutant That Is Only Active with Agmatine as Substrate.

María-Soledad Orellana, Gonzalo A Jaña, Maximiliano Figueroa, José Martínez-Oyanedel, Fabiola E Medina, Estefanía Tarifeño-Saldivia, Marcell Gatica, María Ángeles García-Robles, Nelson Carvajal, Elena Uribe

Open access · goldAbstract read
PubMed Full text at PMC Publisher
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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 43% 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. 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

10 authors at 3 institutions in 1 country.

María-Soledad OrellanaDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción 4070386, Chile.
Gonzalo A JañaDepartamento de Ciencias Químicas, Facultad Ciencias Exactas, Universidad Andres Bello, Autopista Concepción-Talcahuano 7100, Concepción 4070386, Chile.ORCID 0000-0001-7337-2946
Maximiliano FigueroaDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción 4070386, Chile.ORCID 0000-0002-6563-1984
José Martínez-OyanedelDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción 4070386, Chile.ORCID 0000-0001-8616-7474
Fabiola E MedinaDepartamento de Química, Facultad de Ciencias, Universidad del Bio-Bio, Concepción 4051381, Chile.ORCID 0000-0002-0230-8717
Estefanía Tarifeño-SaldiviaDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción 4070386, Chile.
Marcell GaticaDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción 4070386, Chile.
María Ángeles García-RoblesDepartamento de Biología Celular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4070386, Chile.
Nelson CarvajalDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción 4070386, Chile.
Elena UribeDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción 4070386, Chile.
University of Concepción · CLUniversidad Andrés Bello · CLUniversity of Bío-Bío · CL

Funding

University of Concepción VRID-Enlace 217.037.022-1
6 · The paper itself

Abstract

Arginase catalyzes the hydrolysis of L-arginine into L-ornithine and urea. This enzyme has several analogies with agmatinase, which catalyzes the hydrolysis of agmatine into putrescine and urea. However, this contrasts with the highlighted specificity that each one presents for their respective substrate. A comparison of available crystal structures for arginases reveals an important difference in the extension of two loops located in the entrance of the active site. The first, denominated

Indexed as

AgmatineArginaseArginineEscherichia coliHumansOrnithineSubstrate SpecificityUreaAgmatineArginaseArginineOrnithineUreaagmatinearginaseargininedeterminants of specificity

Identifiers

PMID35742891
PMCPMC9224512
OpenAlexW4281770203

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.