Evidence map›Paper›PMID 23141873›Full record

ReviewCurrent opinion in structural biology2012

Emerging themes in radical SAM chemistry.

Krista A Shisler, Joan B Broderick

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Mechanism of controlled radical initiation in radical SAM GTP 3',8-cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  8. Structures of the peptide-modifying radical SAM enzyme SuiB elucidate the basis of substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 2017
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  12. Density functional theory calculations on the active site of biotin synthase: mechanism of S transfer from the Fe(2)S(2) cluster and the role of 1st and 2nd sphere residues.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
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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.

Krista A ShislerDepartment of Chemistry & Biochemistry and the Astrobiology Biogeocatalysis Research Center, Montana State University, Bozeman, MT 59717, United States.
Joan B Broderick

Funding

Iron-Sulfur Clusters in Biological Radical GenerationR01GM054608 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI BRODERICK, JOAN B · 2001 to 2018
$4.7M
SPECTROSCOPIC STUDIES OF PYRUVATE FORMATE LYASE ACTIVASER29GM054608 · NIGMS · MICHIGAN STATE UNIVERSITY · PI BRODERICK, JOAN B. · 1997 to 2000
$102k
SPECTROSCOPIC STUDIES OF PYRUVATE FORMATE-LYASE ACTIVASER55GM054608 · NIGMS · AMHERST COLLEGE · PI BRODERICK, JOAN B. · 1996 to 1996
–
NIGMS NIH HHS GM54608NIGMS NIH HHS R01 GM054608NIGMS NIH HHS R29 GM054608
6 · The paper itself

Abstract

Enzymes in the radical SAM (RS) superfamily catalyze a wide variety of reactions through unique radical chemistry. The characteristic markers of the superfamily include a [4Fe-4S] cluster coordinated to the protein via a cysteine triad motif, typically CX(3)CX(2)C, with the fourth iron coordinated by S-adenosylmethionine (SAM). The SAM serves as a precursor for a 5'-deoxyadenosyl radical, the central intermediate in nearly all RS enzymes studied to date. The SAM-bound [4Fe-4S] cluster is located within a partial or full triosephosphate isomerase (TIM) barrel where the radical chemistry occurs protected from the surroundings. In addition to the TIM barrel and a RS [4Fe-4S] cluster, many members of the superfamily contain additional domains and/or additional Fe-S clusters. Recently characterized superfamily members are providing new examples of the remarkable range of reactions that can be catalyzed, as well as new structural and mechanistic insights into these fascinating reactions.

Indexed as

AnimalsBiocatalysisFree RadicalsOxidation-ReductionS-AdenosylmethionineFree RadicalsS-Adenosylmethionine

Identifiers

PMID23141873
PMCPMC4083504

What OpenQuestion holds

Textmetadata
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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.