Evidence map›Paper›PMID 35584675›Full record

ArticleCell reports2022

Zng1 is a GTP-dependent zinc transferase needed for activation of methionine aminopeptidase.

Miriam Pasquini, Nicolas Grosjean, Kim K Hixson, Carrie D Nicora, Estella F Yee, Mary Lipton, Ian K Blaby, John D Haley, Crysten E Blaby-Haas

Open access · goldAbstract read
PubMed Publisher
In one paragraph

Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
5.0field-weighted citation impact, top 3% of its field
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

39 citing papers in PubMed, 53 citations in OpenAlex.

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  10. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
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  13. Zinc-metallochaperones ofMicrobiology spectrum · 2025
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  14. Exploring metalloproteome remodeling in calprotectin-stressedbioRxiv : the preprint server for biology · 2025
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  15. Zinc Alleviates Gut Barrier Dysfunction by Promoting the Methylation of AKT.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  18. The Arcana of Zinc.The Journal of nutrition · 2025
    Review
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Miriam PasquiniBiology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
Nicolas GrosjeanBiology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
Kim K HixsonThe Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Carrie D NicoraBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Estella F YeeNational Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY 11973, USA.
Mary LiptonThe Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Ian K BlabyBiology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
John D HaleyDepartment of Pathology and Biological Mass Spectrometry Facility, Stony Brook University, Stony Brook, NY 11794, USA.
Crysten E Blaby-HaasBiology Department, Brookhaven National Laboratory, Upton, NY 11973, USA; Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794, USA. Electronic address: cblaby@bnl.gov.
Brookhaven National Laboratory · USPacific Northwest National Laboratory · USStony Brook University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolution of zinc (Zn) as a protein cofactor altered the functional landscape of biology, but dependency on Zn also created an Achilles' heel, necessitating adaptive mechanisms to ensure Zn availability to proteins. A debated strategy is whether metallochaperones exist to prioritize essential Zn-dependent proteins. Here, we present evidence for a conserved family of putative metal transferases in human and fungi, which interact with Zn-dependent methionine aminopeptidase type I (MetAP1/Map1p/Fma1). Deletion of the putative metal transferase in Saccharomyces cerevisiae (ZNG1; formerly YNR029c) leads to defective Map1p function and a Zn-deficiency growth defect. In vitro, Zng1p can transfer Zn

Indexed as

Saccharomyces cerevisiae ProteinsTransferasesZincAminopeptidasesGTP PhosphohydrolasesGuanosine TriphosphateHumansMetalsMethionineNitrogenous Group TransferasesSaccharomyces cerevisiaeAminopeptidasesGTP PhosphohydrolasesGuanosine TriphosphateMetalsMETAP1 protein, humanMethionineNitrogenous Group TransferasesSaccharomyces cerevisiae ProteinsTransferasesZincZNG1B protein, humanZNG1 protein, S cerevisiaeCBWDCobWCOG0523CP: Molecular biologyGTPaseinsertaseMetAPNMEnutrient limitationzinc homeostasis

Identifiers

PMID35584675
OpenAlexW4280627703

What OpenQuestion holds

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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.