Evidence map›Paper›PMID 40395558›Full record

ReviewQRB discovery2025

An integrated structural and biophysical approach to study carbon metabolism in

Evelyn Y-W Huang, Francis Kuang, Haozhe Wu, Chai Xin Yu, Xiaoxu Chen, Glenda Vasku, Le Thao Anh Nguyen, Katherine J Jeppe, Anna K Coussens, Brooke X C Kwai and 1 more

Abstract readReview
In one paragraph

Review in QRB discovery, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

11 authors.

Evelyn Y-W HuangSchool of Chemistry and Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia.ORCID https://orcid.org/0000-0002-3071-9759
Francis KuangSchool of Chemistry and Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia.ORCID https://orcid.org/0009-0001-0478-1567
Haozhe WuSchool of Chemistry and Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia.ORCID https://orcid.org/0009-0006-2495-2841
Chai Xin YuSchool of Chemistry and Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia.ORCID https://orcid.org/0000-0001-7482-1248
Xiaoxu ChenSchool of Chemistry and Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia.ORCID https://orcid.org/0009-0001-0661-5423
Glenda VaskuSchool of Chemistry and Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia.ORCID https://orcid.org/0009-0009-3891-9980
Le Thao Anh NguyenSchool of Chemistry and Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia.ORCID https://orcid.org/0009-0004-6304-1800
Katherine J JeppeMonash Proteomics and Metabolomics Platform, Monash University, Melbourne, VIC, Australia.ORCID https://orcid.org/0000-0003-2284-5090
Anna K CoussensInfectious Diseases and Immune Defence Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, VIC, Australia.ORCID https://orcid.org/0000-0002-7086-2621
Brooke X C KwaiMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia.ORCID https://orcid.org/0000-0001-6378-9633
Ivanhoe K H LeungSchool of Chemistry and Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia.ORCID https://orcid.org/0000-0003-0633-6771

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metabolic enzymes are the catalysts that drive the biochemical reactions essential for sustaining life. Many of these enzymes are tightly regulated by feedback mechanisms. To fully understand their roles and modulation, it is crucial to investigate the relationship between their structure, catalytic mechanism, and function. In this perspective, by using three examples from our studies on

Indexed as

biological reaction kineticsNMRNMR biophysical chemistrystructural biologyX-ray protein crystallography

Identifiers

PMID40395558
PMCPMC12088919

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.