ArticleMolecules (Basel, Switzerland)2021
The Methionine 549 and Leucine 552 Residues of Friedelin Synthase from
Bruna F Mazzeu, Tatiana M Souza-Moreira, Andrew A Oliveira, Melissa Remlinger, Lidiane G Felippe, Sandro R Valentini, Rafael V C Guido, Cleslei F Zanelli, Maysa Furlan
Open access · goldAbstract read
In one paragraphArticle in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 46% of its field
1 · What the graph read from itWhat 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 registryThe trial behind it
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3 · Its place in the literatureWho cites it
0 citing papers in PubMed, 4 citations in OpenAlex.
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4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
9 authors at 2 institutions in 1 country.
Bruna F MazzeuInstituto de Química, Universidade Estadual Paulista-UNESP, CP 355, Araraquara 14800-900, SP, Brazil.
Tatiana M Souza-MoreiraInstituto de Química, Universidade Estadual Paulista-UNESP, CP 355, Araraquara 14800-900, SP, Brazil.ORCID 0000-0001-8198-5232 Andrew A OliveiraCentro de Pesquisa e Inovação em Biodiversidade e Fármacos, Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos 13563-120, SP, Brazil.ORCID 0000-0002-4092-8546 Melissa RemlingerInstituto de Química, Universidade Estadual Paulista-UNESP, CP 355, Araraquara 14800-900, SP, Brazil.
Lidiane G FelippeInstituto de Química, Universidade Estadual Paulista-UNESP, CP 355, Araraquara 14800-900, SP, Brazil.
Sandro R ValentiniFaculdade de Ciências Farmacêuticas, Universidade Estadual Paulista-UNESP, Rod. Araraquara-Jaú km 1, Araraquara 14800-903, SP, Brazil.
Rafael V C GuidoCentro de Pesquisa e Inovação em Biodiversidade e Fármacos, Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos 13563-120, SP, Brazil.ORCID 0000-0002-7187-0818 Cleslei F ZanelliFaculdade de Ciências Farmacêuticas, Universidade Estadual Paulista-UNESP, Rod. Araraquara-Jaú km 1, Araraquara 14800-903, SP, Brazil.
Maysa FurlanInstituto de Química, Universidade Estadual Paulista-UNESP, CP 355, Araraquara 14800-900, SP, Brazil.
Universidade Estadual Paulista (Unesp) · BRUniversidade de São Paulo · BR
Funding
Conselho Nacional de Desenvolvimento Científico e Tecnológico INCT-CNPq - 2014/465637-0.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior Finance Code 001Fundação de Amparo à Pesquisa do Estado de São Paulo CIBFar-2013/07600-3, INCT-FAPESP-2014/50926-0, #2014/03819-3, #2011/10379-1 and #2014/25705-0.
6 · The paper itselfAbstract
Friedelin, a pentacyclic triterpene found in the leaves of the Celastraceae species, demonstrates numerous biological activities and is a precursor of quinonemethide triterpenes, which are promising antitumoral agents. Friedelin is biosynthesized from the cyclization of 2,3-oxidosqualene, involving a series of rearrangements to form a ketone by deprotonation of the hydroxylated intermediate, without the aid of an oxidoreductase enzyme. Mutagenesis studies among oxidosqualene cyclases (OSCs) have demonstrated the influence of amino acid residues on rearrangements during substrate cyclization: loss of catalytic activity, stabilization, rearrangement control or specificity changing. In the present study, friedelin synthase from
Indexed as
Alkyl and Aryl TransferasesAmino Acid SubstitutionBiosynthetic PathwaysCyclizationGenes, PlantLeucineLupanesMaytenusMethionineModels, MolecularMutagenesis, Site-DirectedOleanolic AcidPentacyclic TriterpenesPlant ProteinsProtein Structure, SecondaryRecombinant ProteinsAlkyl and Aryl Transferasesalpha-amyrinbeta-amyrinfriedelinLeucineLupanesMethionineOleanolic AcidPentacyclic TriterpenesPlant ProteinsRecombinant ProteinsTriterpenesCelastraceaefriedelin synthaseLeu552PheMaytenus ilicifoliaMet549SerSaccharomyces cerevisiaesite-directed mutation
Identifiers
PMID34833897
PMCPMC8617677
OpenAlexW3213653722
What OpenQuestion holds
Textmetadata
LicenceCC BY
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