Evidence map›Paper›PMID 39012171›Full record

ArticleBiochemistry2024

A Noble Metal Substitution Leads to B

Markus Ruetz, Romila Mascarenhas, Florian Widner, Christoph Kieninger, Markos Koutmos, Bernhard Kräutler, Ruma Banerjee

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. An unusual Co-S bond links BProceedings of the National Academy of Sciences of the United States of America · 2025
    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

7 authors.

Markus RuetzORCID 0000-0001-9540-7310
Romila MascarenhasORCID 0000-0002-5099-3528
Florian Widner
Christoph Kieninger
Markos Koutmos
Bernhard KräutlerORCID 0000-0002-2222-0587
Ruma BanerjeeORCID 0000-0001-8332-3275

Funding

REACTION MECHANISMS OF MAMMALIAN B12-DEPENDENT ENZYMESR01DK045776 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI RUMA V BANERJEE · 1998 to 2026
$9.7M
Vitamin B12 trafficking and selectivity in gut bacteriaR00GM143482 · NIGMS · UNIVERSITY OF OREGON · PI Romila Nina Mascarenhas · 2024 to 2026
$747k
NIDDK NIH HHS R01 DK045776NIGMS NIH HHS R00 GM143482
6 · The paper itself

Abstract

In mammals, cobalamin is an essential cofactor that is delivered by a multitude of chaperones in an elaborate trafficking pathway to two client enzymes, methionine synthase and methylmalonyl-CoA mutase (MMUT). Rhodibalamins, the rhodium analogs of cobalamins, have been described as antimetabolites due to their ability to inhibit bacterial growth. In this study, we have examined the reactivity of adenosylrhodibalamin (AdoRhbl) with two key human chaperones, MMACHC (also known as CblC) and adenosyltransferase (MMAB, also known as ATR), and with the human and

Indexed as

Vitamin B 12Alkyl and Aryl TransferasesBacterial ProteinsHumansMethylmalonyl-CoA MutaseModels, MolecularMolecular ChaperonesMolecular MimicryMycobacterium tuberculosisRhodiumAlkyl and Aryl TransferasesATP-corrinoid adenosyltransferaseBacterial Proteinscob(I)alamin adenosyltransferaseMethylmalonyl-CoA MutaseMolecular ChaperonesRhodiumVitamin B 12

Identifiers

PMID39012171
PMCPMC11540531

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.