Evidence map›Paper›PMID 41659594›Full record

ArticlebioRxiv : the preprint server for biology2026

Native Mass Spectrometry-Based Proteomics Reveals the Mechanism of Hemophore Release by Pathogenic

Andrew K Goring, Lindsey R Lyman, Jordan Ford, Jingjing Huang, Christopher Mullen, Rafael D Melani, Michael P Schmitt, Robert T Clubb, Joseph A Loo

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

9 authors.

Andrew K GoringDepartment of Chemistry and Biochemistry, University of California, Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095, USA.ORCID 0000-0003-4220-6472
Lindsey R LymanLaboratory of Respiratory and Special Pathogens, Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20903, USA.
Jordan FordDepartment of Chemistry and Biochemistry, University of California, Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095, USA.
Jingjing HuangThermo Fischer Scientific, 355 River Oaks Pkwy, San Jose, CA 95134, USA.
Christopher MullenThermo Fischer Scientific, 355 River Oaks Pkwy, San Jose, CA 95134, USA.
Rafael D MelaniThermo Fischer Scientific, 355 River Oaks Pkwy, San Jose, CA 95134, USA.
Michael P SchmittLaboratory of Respiratory and Special Pathogens, Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20903, USA.
Robert T ClubbDepartment of Chemistry and Biochemistry, University of California, Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095, USA.
Joseph A LooDepartment of Chemistry and Biochemistry, University of California, Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095, USA.

Funding

Research Training in Cell and Molecular BiologyT32GM145388 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Jorge Torres · 2022 to 2026
$5.2M
Molecular basis of heme scavenging by Gram-positive bacteriaR01AI161828 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Robert Thompson Clubb · 2021 to 2026
$3.0M
UCLA Dentist-Scientist and Oral Health-Researcher Training ProgramT90DE030860 · NIDCR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TON-THAT, HUNG, WONG, DAVID T · 2021 to 2025
$2.1M
Advancing Mass Spectrometry Analyses of Proteins, Assemblies, and ProteoformsR35GM145286 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Joseph A Loo · 2022 to 2026
$1.9M
NIAID NIH HHS R01 AI161828NIDCR NIH HHS T90 DE030860NIGMS NIH HHS R35 GM145286NIGMS NIH HHS T32 GM145388
6 · The paper itself

Abstract

Iron is an essential micronutrient for nearly all forms of life, including pathogenic microbes that must acquire it from their host during infection. At the host-pathogen interface, humans restrict microbial access to iron through nutritional immunity, which many pathogens overcome by secreting hemophores that scavenge extracellular heme (iron protoporphyrin IX). However, identifying hemophores and other ligand-binding proteins in complex proteomes remains challenging using conventional peptide-based bottom-up mass spectrometry (MS). Here, we introduce ProteoMIX (Proteome Analysis by Mixing), a function-based native top-down proteomics workflow that combines slow-mixing mode native MS with charge reduction to identify ligand-binding proteins directly from complex mixtures. Applying ProteoMIX to the

Indexed as

Bacterial pathogenesisConserved Region (CR) domainCorynebacterium diphtheriaehemehemophoreironnative mass spectrometryProteome Analysis by Mixing (ProteoMIX)

Identifiers

PMID41659594
PMCPMC12873794

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.