Crystal structures of the phosphorylation mimics of human cytosolic branched chain aminotransferase.

Elizabeth S Dare, Robert H Newman, Myra E Conway, Ming Dong

Abstract read

In one paragraph

Article in Archives of biochemistry and biophysics, 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

–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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

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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

4 authors.

Elizabeth S DareDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, NC, USA.

Robert H NewmanDepartment of Biology, North Carolina A&T State University, Greensboro, NC, USA.

Myra E ConwayCollege of Health, Psychology and Social Care, University of Derby, Derby, UK.

Ming DongDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, NC, USA. Electronic address: dongm@uncw.edu.

Funding

Studying the ERK phosphorylation of the BCAT proteinSC2GM139698 · NIGMS · NORTH CAROLINA AGRI & TECH ST UNIV · PI DONG, MING · 2021 to 2023

$420k

NIGMS NIH HHS SC2 GM139698

6 · The paper itself

Abstract

The phosphorylation sites of the human cytosolic Branched Chain Aminotransferase (hBCATc) mediated by mitogen-activated protein kinase (MAPK)/extracellular-signal-regulated-kinase 2 (ERK2, also known as MAPK1) were mapped. The crystal structures of the phosphorylation mimics at T33 and T36 were determined. The modified transaminase activity of these variants was analyzed. Although there were no major conformational changes in the phosphorylation mimics of hBCAT, a regional conformational change at the interdomain loop was observed mainly in mutant T33E. Consistently, when the catalytic turnovers of the T33E and T36E mutants were comparable to the wild type of hBCATc, the K

Indexed as

CytosolMitogen-Activated Protein Kinase 1TransaminasesCrystallography, X-RayHumansModels, MolecularPhosphorylationProtein Conformationbranched-chain-amino-acid transaminaseMAPK1 protein, humanMitogen-Activated Protein Kinase 1TransaminasesCXXC motifhBCATcInterdomain loopPhosphorylationTransaminase

Identifiers

PMID40414328

DOI10.1016/j.abb.2025.110479

PMCPMC13191307

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LicenceCC BY-NC-ND

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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.