Evidence map›Paper›PMID 42886775›Full record

ArticleScience advances2026

Substrate-bound structures of yeast ALA synthase reveal protein dynamics initiating heme biosynthesis.

Jenny U Tran, Thyandra A Martinez, Christopher Jurich, Margaret R Josling, Julian M Zhang, Pedro H Ayres-Galhardo, Jens Meiler, Zhongyue J Yang, Jason A MacGurn, Breann L Brown

Abstract read
In one paragraph

Article in Science advances, 2026. 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

10 authors.

Jenny U TranDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.ORCID 0000-0003-0041-5700
Thyandra A MartinezDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA.
Christopher JurichDepartment of Chemistry, Vanderbilt University, Nashville, TN, USA.ORCID 0000-0001-6592-7980
Margaret R JoslingDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
Julian M ZhangDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
Pedro H Ayres-GalhardoDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA.ORCID 0009-0000-2380-5539
Jens MeilerDepartment of Chemistry, Vanderbilt University, Nashville, TN, USA.ORCID 0000-0001-8945-193X
Zhongyue J YangDepartment of Chemistry, Vanderbilt University, Nashville, TN, USA.ORCID 0000-0003-0395-6617
Jason A MacGurnDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA.ORCID 0000-0001-5063-259X
Breann L BrownDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.ORCID 0000-0001-8109-4472

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Vivian Stojanoff · 2019 to 2026
$38.6M
Chemistry-Biology Interface Training GrantT32GM065086 · NIGMS · VANDERBILT UNIVERSITY · PI BACHMANN, BRIAN O, SULIKOWSKI, GARY ALLEN · 2002 to 2022
$7.0M
Off the beaten path(way): Spatiotemporal investigation of protein assemblies controlling mitochondrial metabolismDP2GM146255 · NIGMS · VANDERBILT UNIVERSITY · PI BROWN, BREANN · 2021 to 2024
$2.3M
Deciphering the ubiquitin code in stress signaling and membrane traffickingR35GM144112 · NIGMS · VANDERBILT UNIVERSITY · PI Jason A MacGurn · 2022 to 2026
$2.2M
NIGMS NIH HHS DP2 GM146255NIGMS NIH HHS P30 GM133893NIGMS NIH HHS R35 GM144112NIGMS NIH HHS T32 GM065086
6 · The paper itself

Abstract

Heme is an essential prosthetic group involved in multiple biological processes in nearly all organisms. Heme biosynthesis is initiated by the pyridoxal 5'-phosphate-dependent enzyme aminolevulinic acid synthase (ALAS). Mutations in ALAS cause multiple hematological diseases. Despite sharing approximately 70% sequence similarity, ALAS homologs exhibit distinct expression and regulatory mechanisms. However, the molecular basis for their functional divergence remains poorly understood. Here, we used x-ray crystallography and molecular dynamics simulations to elucidate the structure and dynamics of

Indexed as

5-Aminolevulinate SynthetaseHemeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCrystallography, X-RayMolecular Dynamics SimulationProtein BindingProtein ConformationSubstrate Specificity5-Aminolevulinate SynthetaseHemeSaccharomyces cerevisiae Proteins

Identifiers

PMID42886775
PMCPMC13674496

What OpenQuestion holds

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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.