Mutually exclusive pathways for biosynthesis of polyamine homospermidine dependent on putrescine or agmatine.

Bin Li, Hamid R Baniasadi, Jue Liang, Margaret A Phillips, Anthony J Michael

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 2026. 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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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

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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

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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

5 authors.

Bin LiDepartment of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA.

Hamid R BaniasadiDepartment of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA.

Jue LiangDepartment of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA.

Margaret A PhillipsDepartment of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA.

Anthony J MichaelDepartment of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA. Electronic address: anthony.michael@utsouthwestern.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Homospermidine is a structural analog of spermidine, a polyamine that is essential for growth and cell proliferation in eukaryotes. The eukaryotic enzyme deoxyhypusine synthase (DHS) can synthesize homospermidine directly from spermidine and putrescine. Nonhomologous bacterial homospermidine synthase (HSS) synthesizes homospermidine directly from two molecules of putrescine. SpeY is a homolog of DHS in bacteria that is essential for homospermidine biosynthesis in a cyanobacterium. Recently, it was shown in the bacterial hyperthermophile Thermus thermophilus, that SpeY couples two molecules of agmatine produced by arginine decarboxylase to form N

Indexed as

agmatinaseagmatineagmatine deiminaseagmatine ureohydrolasearginine decarboxylasedeoxyhypusine synthasehomospermidinehomospermidine synthaseneofunctionalizationornithine decarboxylaseputrescine

Identifiers

PMID42665092

DOI10.1016/j.jbc.2026.113510

PMCPMC13625781

What OpenQuestion holds

Textmetadata

Read underepoch 390

Registered trials

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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.