Evidence map›Paper›PMID 28167430›Full record

ReviewCurrent opinion in chemical biology2017

Vitamin B

Jennifer Bridwell-Rabb, Catherine L Drennan

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.3field-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

44 citing papers in PubMed, 121 citations in OpenAlex.

  1. Mechanistic insight into radicalNatural product reports · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Article
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  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Transcriptional Control ofApplied and environmental microbiology · 2023
    Article
  14. The action of topical application of Vitamin BInternational wound journal · 2023
    Article
  15. Cobalamin-Dependent RadicalACS bio & med chem Au · 2022
    Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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 2 institutions in 1 country.

Jennifer Bridwell-RabbDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. Electronic address: jb_rabb@mit.edu.
Catherine L DrennanDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. Electronic address: cdrennan@mit.edu.
Howard Hughes Medical Institute · USMassachusetts Institute of Technology · US

Funding

Complex Metallocluster Structure and AssemblyR01GM069857 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DRENNAN, CATHERINE L · 2004 to 2017
$3.1M
Structural Investigation of Enzymes that Utilize Cobalamin and AdoMet CofactorsF32GM108189 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BRIDWELL-RABB, JENNIFER D · 2014 to 2015
$109k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM108189NIGMS NIH HHS R01 GM069857
6 · The paper itself

Abstract

The ability of cobalamin to coordinate different upper axial ligands gives rise to a diversity of reactivity. Traditionally, adenosylcobalamin is associated with radical-based rearrangements, and methylcobalamin with methyl cation transfers. Recently, however, a new role for adenosylcobalamin has been discovered as a light sensor, and a methylcobalamin-dependent enzyme has been identified that is suggested to transfer a methyl anion. Additionally, recent studies have provided a wealth of new information about a third class of cobalamin-dependent enzymes that do not appear to use an upper ligand. They function in reductive dehalogenations and epoxide reduction reactions. Finally, mechanistic details are beginning to emerge about the cobalamin-dependent S-adenosylmethionine radical enzyme superfamily for which the role of cobalamin has been largely enigmatic.

Indexed as

Vitamin B 12CobamidesEnzymesLightS-AdenosylmethioninecobamamideCobamidesEnzymesS-AdenosylmethionineVitamin B 12

Identifiers

PMID28167430
PMCPMC5540639
OpenAlexW2583865628

What OpenQuestion holds

Textmetadata
LicenceTDM
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.