Evidence map›Paper›PMID 40401103›Full record

ArticleACS catalysis2025

α-Hydrazino Acids Inhibit Pyridoxal Phosphate-Dependent Decarboxylases via "Catalytically Correct" Ketoenamine Tautomers: A Special Motif for Chemical Biology and Drug Discovery?

Jonathan M Baine, Yoan Duhoo, Tzanko Doukov, Ambroise Desfosses, Giovanni Bisello, Matthew L Beio, Olivia Bauer, Massimiliano Perduca, Maria Bacia-Verloop, Mariarita Bertoldi and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS catalysis, 2025. 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
–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

2 citing papers in PubMed.

  1. A cloaked glutamate decarboxylase sustains the GABA shunt inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
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

13 authors.

Jonathan M BaineDepartment of Chemistry, University of Nebraska, Lincoln, Nebraska 68588, United States.ORCID https://orcid.org/0009-0006-6065-8447
Yoan Duhoo1 Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.ORCID https://orcid.org/0000-0002-6643-1693
Tzanko DoukovStanford Synchrotron Radiation Lightsource, Stanford University, Menlo Park, California 94025, United States.ORCID https://orcid.org/0000-0001-8625-2572
Ambroise Desfosses1 Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.ORCID https://orcid.org/0000-0002-6525-5042
Giovanni BiselloDepartment of Neuroscience, Biomedicine and Movement Sciences, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy.ORCID https://orcid.org/0000-0002-3803-9555
Matthew L BeioDepartment of Chemistry, University of Nebraska, Lincoln, Nebraska 68588, United States.ORCID https://orcid.org/0009-0006-4540-7279
Olivia BauerDepartments of Chemistry and Biochemistry, University of Georgia, Athens, Georgia 30602, United States.ORCID https://orcid.org/0000-0001-5759-5461
Massimiliano PerducaDepartment of Neuroscience, Biomedicine and Movement Sciences, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy.ORCID https://orcid.org/0000-0001-8291-0523
Maria Bacia-Verloop1 Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.ORCID https://orcid.org/0009-0007-0036-8373
Mariarita BertoldiDepartment of Neuroscience, Biomedicine and Movement Sciences, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy.ORCID https://orcid.org/0000-0002-2337-9928
Robert S PhillipsDepartments of Chemistry and Biochemistry, University of Georgia, Athens, Georgia 30602, United States.ORCID https://orcid.org/0000-0001-8710-562X
Irina Gutsche1 Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.ORCID https://orcid.org/0000-0002-1908-3921
David B BerkowitzDepartment of Chemistry, University of Nebraska, Lincoln, Nebraska 68588, United States.ORCID https://orcid.org/0000-0001-7550-0112

Funding

Targeted mass spectrometry approaches to understand CART processing and recepter interactionsP20GM113126 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI RAZAVI RIZI, MOHAMMAD · 2016 to 2025
$20.8M
Structural and proton dynamics of pyridoxal-5’-phosphate dependent enzymes Resubmission (Equipment Supplement)R01GM137008 · NIGMS · UNIVERSITY OF GEORGIA · PI KOVALEVSKYI, ANDRII Y, MUELLER, LEONARD J · 2020 to 2023
$2.8M
EXTRAMURAL RES FACILITIES CONSTRC06RR016544 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI PAUL, PREM S · 2001 to 2001
$2.0M
NCRR NIH HHS C06 RR016544NIGMS NIH HHS P20 GM113126NIGMS NIH HHS R01 GM137008
6 · The paper itself

Abstract

We present evidence that supports a 'correct hydrazone tautomer/Dunathan alignment model' for how α-hydrazino analogues of α-amino acids inhibit PLP enzymes. Described is the asymmetric synthesis of l- and d-α-hydrazino acid l-lysine analogues and their inhibition of

Identifiers

PMID40401103
PMCPMC12091041

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.