ArticleJournal of bacteriology2010
Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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.
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.
Who cites it
21 citing papers in PubMed, 47 citations in OpenAlex.
- Subtractive proteomics and reverse-vaccinology approaches for novel drug targets and designing a chimeric vaccine againstFrontiers in immunology · 2025Article
- The Function of Two Radical-SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the [Fe]-Hydrogenase Cofactor.Angewandte Chemie (International ed. in English) · 2022Article
- Proteomic Analysis of Methanococcus voltae Grown in the Presence of Mineral and Nonmineral Sources of Iron and Sulfur.Microbiology spectrum · 2022Article
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
- C3'-Deoxygenation of Paromamine Catalyzed by a Radical S-Adenosylmethionine Enzyme: Characterization of the Enzyme AprD4 and Its Reductase Partner AprD3.Angewandte Chemie (International ed. in English) · 2016Article
- Chemical and Biological Reduction of the Radical SAM Enzyme 7-Carboxy-7-deazaguanine [corrected] Synthase.Biochemistry · 2015Article
- Non-canonical active site architecture of the radical SAM thiamin pyrimidine synthase.Nature communications · 2015Article
- Radical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.The Journal of biological chemistry · 2015Review
- Radical S-adenosylmethionine enzymes.Chemical reviews · 2014Review
- Glycyl radical activating enzymes: structure, mechanism, and substrate interactions.Archives of biochemistry and biophysics · 2014Review
- Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism.Nature chemical biology · 2014Article
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- Emerging themes in radical SAM chemistry.Current opinion in structural biology · 2012Review
- The methylthiolation reaction mediated by the Radical-SAM enzymes.Biochimica et biophysica acta · 2012Review
- Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase.The Journal of biological chemistry · 2011Article
- Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation.Journal of the American Chemical Society · 2011Article
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- More than 200 genes required for methane formation from H₂ and CO₂ and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus.Archaea (Vancouver, B.C.) · 2011Article
- Mechanistic and functional versatility of radical SAM enzymes.F1000 biology reports · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genetic context, phylogeny, and biochemistry of a gene flanking the H(2)-forming methylene-H(4)-methanopterin dehydrogenase gene (hmdA), here designated hmdB, indicate that it is a new member of the radical S-adenosylmethionine enzyme superfamily. In contrast to the characteristic CX(3)CX(2)C or CX(2)CX(4)C motif defining this family, HmdB contains a unique CX(5)CX(2)C motif.
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What OpenQuestion holds
Registered trials
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.