Evidence map›Paper›PMID 35485745›Full record

ReviewMetallomics : integrated biometal science2022

The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.

Francesca A Vaccaro, Catherine L Drennan

Open access · hybridAbstract readReview
In one paragraph

Review in Metallomics : integrated biometal science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. ATP-Triggered Fe(CN)Journal of the American Chemical Society · 2024
    Article
  9. Structural Determinants ofbioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

2 authors at 1 institution in 1 country.

Francesca A VaccaroDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA, USA.
Catherine L DrennanDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA, USA.
Massachusetts Institute of Technology · US

Funding

Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Structural Basis of Metallocofactor Delivery and RepairF31GM131648 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI VACCARO, FRANCESCA · 2019 to 2023
$167k
Howard Hughes Medical InstituteNIGMS NIH HHS F31 GM131648NIGMS NIH HHS R35 GM126982NIH HHS R35 GM126982
6 · The paper itself

Abstract

Metalloenzymes catalyze a diverse set of challenging chemical reactions that are essential for life. These metalloenzymes rely on a wide range of metallocofactors, from single metal ions to complicated metallic clusters. Incorporation of metal ions and metallocofactors into apo-proteins often requires the assistance of proteins known as metallochaperones. Nucleoside triphosphate hydrolases (NTPases) are one important class of metallochaperones and are found widely distributed throughout the domains of life. These proteins use the binding and hydrolysis of nucleoside triphosphates, either adenosine triphosphate or guanosine triphosphate, to carry out highly specific and regulated roles in the process of metalloenzyme maturation. Here, we review recent literature on NTPase metallochaperones and describe the current mechanistic proposals and available structural data. By using representative examples from each type of NTPase, we also illustrate the challenges in studying these complicated systems. We highlight open questions in the field and suggest future directions. This minireview is part of a special collection of articles in memory of Professor Deborah Zamble, a leader in the field of nickel biochemistry.

Indexed as

MetallochaperonesMetalloproteinsAdenosine TriphosphateHydrolasesMetalsN-Glycosyl HydrolasesNucleosidesNucleoside-TriphosphatasePolyphosphatesAdenosine TriphosphateHydrolasesMetallochaperonesMetalloproteinsMetalsN-Glycosyl HydrolasesNucleosidesNucleoside-TriphosphatasePolyphosphatestriphosphoric acidATPasesGTPasesmetallochaperonesmetallocofactorsmetalloenzyme maturationmetals in biology

Identifiers

PMID35485745
PMCPMC9164220
OpenAlexW4225153985

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.