Evidence map›Paper›PMID 41141816›Full record

ArticleACS omega2025

Structural Characterization of Lytic Transglycosylase SltB2 of

Vega Miguel-Ruano, María T Batuecas, Elena Lastochkin, Teresa Domínguez-Gil, Rafael Molina, Shahriar Mobashery, Juan A Hermoso

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Article in ACS omega, 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

7 authors.

Vega Miguel-RuanoDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", Spanish National Research Council (CSIC), Serrano 119, Madrid 28006, Spain.ORCID https://orcid.org/0000-0002-2492-7164
María T BatuecasDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", Spanish National Research Council (CSIC), Serrano 119, Madrid 28006, Spain.
Elena LastochkinDepartment of Chemistry and Biochemistry, University of Notre Dame, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Teresa Domínguez-GilDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", Spanish National Research Council (CSIC), Serrano 119, Madrid 28006, Spain.
Rafael MolinaDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", Spanish National Research Council (CSIC), Serrano 119, Madrid 28006, Spain.ORCID https://orcid.org/0000-0002-6443-4989
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.ORCID https://orcid.org/0000-0002-7695-7883
Juan A HermosoDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry "Blas Cabrera", Spanish National Research Council (CSIC), Serrano 119, Madrid 28006, Spain.ORCID https://orcid.org/0000-0002-1862-8950

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lytic transglycosylases (LTs) belong to a family of enzymes that turnover the bacterial cell-wall peptidoglycan through a nonhydrolytic cleavage of the β(1-4) glycosidic bond, generating a hallmark 1,6-anhydromuramyl moiety in the reaction products. LTs are essential for numerous cellular processes, including cell-wall maturation, peptidoglycan recycling, cell division, and the assembly of multiprotein complexes. Their functional diversity underscores their biological significance. Family 3 LTs are distinguished by their EF-hand Ca

Identifiers

PMID41141816
PMCPMC12547810

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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.