Acknowledgements requested in publications
« This work of the Interdisciplinary Thematic Institute IMCBio, as part of the ITI 2021-2028 program of the University of Strasbourg, CNRS and Inserm, was supported by IdEx Unistra (ANR-10-IDEX-0002), and by SFRI-STRAT’US project (ANR 20-SFRI-0012) and EUR IMCBio (ANR-17-EURE-0023) under the framework of the French Investments for the Future Program. »
2024
Wolff, Philippe; Labar, Geoffray; Lechner, Antony; Elder, Dany Van; Soin, Romuald; Gueydan, Cyril; Kruys, Véronique; Droogmans, Louis; Roovers, Martine
The gene encodes RlmQ, the 23S rRNA methyltransferase forming mG2574 in the A-site of the peptidyl transferase center Article de journal
Dans: RNA, vol. 30, no. 2, p. 105–112, 2024, ISSN: 1469-9001.
@article{pmid38071475,
title = {The gene encodes RlmQ, the 23S rRNA methyltransferase forming mG2574 in the A-site of the peptidyl transferase center},
author = {Philippe Wolff and Geoffray Labar and Antony Lechner and Dany Van Elder and Romuald Soin and Cyril Gueydan and Véronique Kruys and Louis Droogmans and Martine Roovers},
doi = {10.1261/rna.079853.123},
issn = {1469-9001},
year = {2024},
date = {2024-01-01},
urldate = {2024-01-01},
journal = {RNA},
volume = {30},
number = {2},
pages = {105--112},
abstract = {Ribosomal RNA contains many posttranscriptionally modified nucleosides, particularly in the functional parts of the ribosome. The distribution of these modifications varies from one organism to another. In , the model organism for Gram-positive bacteria, mass spectrometry experiments revealed the presence of 7-methylguanosine (mG) at position 2574 of the 23S rRNA, which lies in the A-site of the peptidyl transferase center of the large ribosomal subunit. Testing several mG methyltransferase candidates allowed us to identify the RlmQ enzyme, encoded by the open reading frame, as the MTase responsible for this modification. The enzyme methylates free RNA and not ribosomal 50S or 70S particles, suggesting that modification occurs in the early steps of ribosome biogenesis.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Quignon, E.; Ferhadian, D.; Hache, A.; Vivet-Boudou, V.; Isel, C.; Printz-Schweigert, A.; Donchet, A.; Crépin, T.; Marquet, R.
Structural Impact of the Interaction of the Influenza A Virus Nucleoprotein with Genomic RNA Segments Article de journal
Dans: Viruses, vol. 16, no. 3, p. 421, 2024, ISBN: 10.3390/v16030421.
@article{nokey,
title = {Structural Impact of the Interaction of the Influenza A Virus Nucleoprotein with Genomic RNA Segments},
author = {E. Quignon and D. Ferhadian and A. Hache and V. Vivet-Boudou and C. Isel and A. Printz-Schweigert and A. Donchet and T. Crépin and R. Marquet},
url = {https://www.mdpi.com/1999-4915/16/3/421},
isbn = {10.3390/v16030421},
year = {2024},
date = {2024-01-01},
urldate = {2024-01-01},
journal = {Viruses},
volume = {16},
number = {3},
pages = {421},
abstract = {Influenza A viruses (IAVs) possess a segmented genome consisting of eight viral RNAs (vRNAs) associated with multiple copies of viral nucleoprotein (NP) and a viral polymerase complex. Despite the crucial role of RNA structure in IAV replication, the impact of NP binding on vRNA structure is not well understood. In this study, we employed SHAPE chemical probing to compare the structure of NS and M vRNAs of WSN IAV in various states: before the addition of NP, in complex with NP, and after the removal of NP. Comparison of the RNA structures before the addition of NP and after its removal reveals that NP, while introducing limited changes, remodels local structures in both vRNAs and long-range interactions in the NS vRNA, suggesting a potentially biologically relevant RNA chaperone activity. In contrast, NP significantly alters the structure of vRNAs in vRNA/NP complexes, though incorporating experimental data into RNA secondary structure prediction proved challenging. Finally, our results suggest that NP not only binds single-stranded RNA but also helices with interruptions, such as bulges or small internal loops, with a preference for G-poor and C/U-rich regions.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
2023
Bahena-Ceron, Roberto; Teixeira, Chloe; Ponce, Jose R Jaramillo; Wolff, Philippe; Couzon, Florence; François, Pauline; Klaholz, Bruno; Vandenesch, François; Romby, Pascale; Moreau, Karen; Marzi, Stefano
RlmQ: A Newly Discovered rRNA Modification Enzyme Bridging RNA Modification and Virulence Traits in Article de journal
Dans: RNA, 2023, ISSN: 1469-9001.
@article{pmid38164596,
title = {RlmQ: A Newly Discovered rRNA Modification Enzyme Bridging RNA Modification and Virulence Traits in },
author = {Roberto Bahena-Ceron and Chloe Teixeira and Jose R Jaramillo Ponce and Philippe Wolff and Florence Couzon and Pauline François and Bruno Klaholz and François Vandenesch and Pascale Romby and Karen Moreau and Stefano Marzi},
doi = {10.1261/rna.079850.123},
issn = {1469-9001},
year = {2023},
date = {2023-12-01},
urldate = {2023-12-01},
journal = {RNA},
abstract = {rRNA modifications play crucial roles in fine-tuning the delicate balance between translation speed and accuracy, yet the underlying mechanisms remain elusive. Comparative analyses of the ribosomal RNA modifications in taxonomically distant bacteria could help define their general, as well as species-specific, roles. In this study, we identified a new methyltransferase, RlmQ, in responsible for the Gram-positive specific mG2601, which is not modified in (G2574). We also demonstrate the absence of methylation on C1989, equivalent to C1962, which is methylated at position 5 by the Gram-negative specific RlmI methyltransferase, a paralogue of RlmQ. Both modifications ( mG2601 and mC1962) are situated within the same tRNA accommodation corridor, hinting at a potential shared function in translation. Inactivation of Q causes the loss of methylation at G2601 and significantly impacts growth, cytotoxicity, and biofilm formation. These findings unravel the intricate connections between rRNA modifications, translation, and virulence in pathogenic Gram-positive bacteria.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Ponce, José R Jaramillo; Frugier, Magali
Plasmodium, the Apicomplexa Outlier When It Comes to Protein Synthesis Article de journal
Dans: Biomolecules, vol. 14, no. 1, p. 46, 2023, ISSN: 2218-273X.
@article{pmid38254646,
title = {Plasmodium, the Apicomplexa Outlier When It Comes to Protein Synthesis},
author = {José R Jaramillo Ponce and Magali Frugier},
doi = {10.3390/biom14010046},
issn = {2218-273X},
year = {2023},
date = {2023-12-01},
urldate = {2023-12-01},
journal = {Biomolecules},
volume = {14},
number = {1},
pages = {46},
abstract = {Plasmodium is an obligate intracellular parasite that has numerous interactions with different hosts during its elaborate life cycle. This is also the case for the other parasites belonging to the same phylum Apicomplexa. In this study, we bioinformatically identified the components of the multi-synthetase complexes (MSCs) of several Apicomplexa parasites and modelled their assembly using AlphaFold2. It appears that none of these MSCs resemble the two MSCs that we have identified and characterized in Plasmodium. Indeed, tRip, the central protein involved in the association of the two Plasmodium MSCs is different from its homologues, suggesting also that the tRip-dependent import of exogenous tRNAs is not conserved in other apicomplexan parasites. Based on this observation, we searched for obvious differences that could explain the singularity of Plasmodium protein synthesis by comparing tRNA genes and amino acid usage in the different genomes. We noted a contradiction between the large number of asparagine residues used in Plasmodium proteomes and the single gene encoding the tRNA that inserts them into proteins. This observation remains true for all the Plasmodia strains studied, even those that do not contain long asparagine homorepeats. },
keywords = {},
pubstate = {published},
tppubtype = {article}
}
A, Kairouani; D, Pontier; C, Picart; F, Mounet; Y, Martinez; L, Le-Bot; M, Fanuel; P, Hammann; L, Belmudes; R, Merret; J, Azevedo; M-C, Carpentier; D, Gagliardi; Y, Couté; R, Sibout; N, Bies-Etheve; T., Lagrange
Cell-type-specific control of secondary cell wall formation by Musashi-type translational regulators in Arabidopsis Actes
2023.
@proceedings{nokey,
title = {Cell-type-specific control of secondary cell wall formation by Musashi-type translational regulators in Arabidopsis},
author = {Kairouani A and Pontier D and Picart C and Mounet F and Martinez Y and Le-Bot L and Fanuel M and Hammann P and Belmudes L and Merret R and Azevedo J and Carpentier M-C and Gagliardi D and Couté Y and Sibout R and Bies-Etheve N and Lagrange T. },
doi = {10.7554/eLife.88207.3},
year = {2023},
date = {2023-09-29},
urldate = {2023-09-29},
journal = {eLife},
abstract = {Deciphering the mechanism of secondary cell wall/SCW formation in plants is key to understanding their development and the molecular basis of biomass recalcitrance. Although transcriptional regulation is essential for SCW formation, little is known about the implication of post-transcriptional mechanisms in this process. Here we report that two bonafide RNA-binding proteins homologous to the animal translational regulator Musashi, MSIL2 and MSIL4, function redundantly to control SCW formation in Arabidopsis. MSIL2/4 interactomes are similar and enriched in proteins involved in mRNA binding and translational regulation. MSIL2/4 mutations alter SCW formation in the fibers, leading to a reduction in lignin deposition, and an increase of 4-O-glucuronoxylan methylation. In accordance, quantitative proteomics of stems reveal an overaccumulation of glucuronoxylan biosynthetic machinery, including GXM3, in the msil2/4 mutant stem. We showed that MSIL4 immunoprecipitates GXM mRNAs, suggesting a novel aspect of SCW regulation, linking post-transcriptional control to the regulation of SCW biosynthesis genes.},
keywords = {},
pubstate = {published},
tppubtype = {proceedings}
}
2017
Miao, Z; Adamiak, R W; Antczak, M; Batey, R T; Becka, A J; Biesiada, M; Boniecki, M J; Bujnicki, J M; Chen, S J; Cheng, C Y; Chou, F C; Ferre-D'Amare, A R; Das, R; Dawson, W K; Ding, F; Dokholyan, N V; Dunin-Horkawicz, S; Geniesse, C; Kappel, K; Kladwang, W; Krokhotin, A; Lach, G E; Major, F; Mann, T H; Magnus, M; Pachulska-Wieczorek, K; Patel, D J; Piccirilli, J A; Popenda, M; Purzycka, K J; Ren, A; Rice, G M; J., Jr. Santalucia; Sarzynska, J; Szachniuk, M; Tandon, A; Trausch, J J; Tian, S; Wang, J; Weeks, K M; B., Williams; Xiao, Y; Xu, X; Zhang, D; Zok, T; Westhof, E
RNA-Puzzles Round III: 3D RNA structure prediction of five riboswitches and one ribozyme Article de journal
Dans: Rna, vol. 23, no. 5, p. 655-672, 2017, ISBN: 28138060, (1469-9001 (Electronic) 1355-8382 (Linking) Journal Article Research Support, Non-U.S. Gov't Research Support, N.I.H., Extramural).
@article{nokey,
title = {RNA-Puzzles Round III: 3D RNA structure prediction of five riboswitches and one ribozyme},
author = {Z Miao and R W Adamiak and M Antczak and R T Batey and A J Becka and M Biesiada and M J Boniecki and J M Bujnicki and S J Chen and C Y Cheng and F C Chou and A R Ferre-D'Amare and R Das and W K Dawson and F Ding and N V Dokholyan and S Dunin-Horkawicz and C Geniesse and K Kappel and W Kladwang and A Krokhotin and G E Lach and F Major and T H Mann and M Magnus and K Pachulska-Wieczorek and D J Patel and J A Piccirilli and M Popenda and K J Purzycka and A Ren and G M Rice and Jr. Santalucia J. and J Sarzynska and M Szachniuk and A Tandon and J J Trausch and S Tian and J Wang and K M Weeks and Williams B. and Y Xiao and X Xu and D Zhang and T Zok and E Westhof},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=28138060},
doi = {10.1261/rna.060368.116},
isbn = {28138060},
year = {2017},
date = {2017-01-01},
journal = {Rna},
volume = {23},
number = {5},
pages = {655-672},
abstract = {RNA-Puzzles is a collective experiment in blind 3D RNA structure prediction. We report here a third round of RNA-Puzzles. Five puzzles, 4, 8, 12, 13, 14, all structures of riboswitch aptamers and puzzle 7, a ribozyme structure, are included in this round of the experiment. The riboswitch structures include biological binding sites for small molecules (S-adenosyl methionine, cyclic diadenosine monophosphate, 5-amino 4-imidazole carboxamide riboside 5'-triphosphate, glutamine) and proteins (YbxF), and one set describes large conformational changes between ligand-free and ligand-bound states. The Varkud satellite ribozyme is the most recently solved structure of a known large ribozyme. All puzzles have established biological functions and require structural understanding to appreciate their molecular mechanisms. Through the use of fast-track experimental data, including multidimensional chemical mapping, and accurate prediction of RNA secondary structure, a large portion of the contacts in 3D have been predicted correctly leading to similar topologies for the top ranking predictions. Template-based and homology-derived predictions could predict structures to particularly high accuracies. However, achieving biological insights from de novo prediction of RNA 3D structures still depends on the size and complexity of the RNA. Blind computational predictions of RNA structures already appear to provide useful structural information in many cases. Similar to the previous RNA-Puzzles Round II experiment, the prediction of non-Watson-Crick interactions and the observed high atomic clash scores reveal a notable need for an algorithm of improvement. All prediction models and assessment results are available at http://ahsoka.u-strasbg.fr/rnapuzzles/.},
note = {1469-9001 (Electronic)
1355-8382 (Linking)
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
2016
Chandrasekhara, C; Mohannath, G; Blevins, T; Pontvianne, F; Pikaard, C S
Chromosome-specific NOR inactivation explains selective rRNA gene silencing and dosage control in Arabidopsis Article de journal
Dans: Genes Dev, vol. 30, no. 2, p. 177-90, 2016, ISBN: 26744421, (1549-5477 (Electronic) 0890-9369 (Linking) Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't).
@article{nokey,
title = {Chromosome-specific NOR inactivation explains selective rRNA gene silencing and dosage control in Arabidopsis},
author = {C Chandrasekhara and G Mohannath and T Blevins and F Pontvianne and C S Pikaard},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=26744421},
doi = {10.1101/gad.273755.115},
isbn = {26744421},
year = {2016},
date = {2016-01-01},
journal = {Genes Dev},
volume = {30},
number = {2},
pages = {177-90},
abstract = {In eukaryotes, scores of excess ribosomal RNA (rRNA) genes are silenced by repressive chromatin modifications. Given the near sequence identity of rRNA genes within a species, it is unclear how specific rRNA genes are reproducibly chosen for silencing. Using Arabidopsis thaliana ecotype (strain) Col-0, a systematic search identified sequence polymorphisms that differ between active and developmentally silenced rRNA gene subtypes. Recombinant inbred mapping populations derived from three different ecotype crosses were then used to map the chromosomal locations of silenced and active RNA gene subtypes. Importantly, silenced and active rRNA gene subtypes are not intermingled. All silenced rRNA gene subtypes mapped to the nucleolus organizer region (NOR) on chromosome 2 (NOR2). All active rRNA gene subtypes mapped to NOR4. Using an engineered A. thaliana line in which a portion of Col-0 chromosome 4 was replaced by sequences of another ecotype, we show that a major rRNA gene subtype silenced at NOR2 is active when introgressed into the genome at NOR4. Collectively, these results reveal that selective rRNA gene silencing is not regulated gene by gene based on mechanisms dependent on subtle gene sequence variation. Instead, we propose that a subchromosomal silencing mechanism operates on a multimegabase scale to inactivate NOR2.},
note = {1549-5477 (Electronic)
0890-9369 (Linking)
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Hematy, K; Bellec, Y; Podicheti, R; Bouteiller, N; Anne, P; Morineau, C; Haslam, R P; Beaudoin, F; Napier, J A; Mockaitis, K; Gagliardi, D; Vaucheret, H; Lange, H; Faure, J D
The Zinc-Finger Protein SOP1 Is Required for a Subset of the Nuclear Exosome Functions in Arabidopsis Article de journal
Dans: PLoS Genet, vol. 12, no. 2, p. e1005817, 2016, ISBN: 26828932, (1553-7404 (Electronic) 1553-7390 (Linking) Journal Article Research Support, Non-U.S. Gov't).
@article{nokey,
title = {The Zinc-Finger Protein SOP1 Is Required for a Subset of the Nuclear Exosome Functions in Arabidopsis},
author = {K Hematy and Y Bellec and R Podicheti and N Bouteiller and P Anne and C Morineau and R P Haslam and F Beaudoin and J A Napier and K Mockaitis and D Gagliardi and H Vaucheret and H Lange and J D Faure},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=26828932},
doi = {10.1371/journal.pgen.1005817},
isbn = {26828932},
year = {2016},
date = {2016-01-01},
journal = {PLoS Genet},
volume = {12},
number = {2},
pages = {e1005817},
abstract = {Correct gene expression requires tight RNA quality control both at transcriptional and post-transcriptional levels. Using a splicing-defective allele of PASTICCINO2 (PAS2), a gene essential for plant development, we isolated suppressor mutations modifying pas2-1 mRNA profiles and restoring wild-type growth. Three suppressor of pas2 (sop) mutations modified the degradation of mis-spliced pas2-1 mRNA species, allowing the synthesis of a functional protein. Cloning of the suppressor mutations identified the core subunit of the exosome SOP2/RRP4, the exosome nucleoplasmic cofactor SOP3/HEN2 and a novel zinc-finger protein SOP1 that colocalizes with HEN2 in nucleoplasmic foci. The three SOP proteins counteract post-transcriptional (trans)gene silencing (PTGS), which suggests that they all act in RNA quality control. In addition, sop1 mutants accumulate some, but not all of the misprocessed mRNAs and other types of RNAs that are observed in exosome mutants. Taken together, our data show that SOP1 is a new component of nuclear RNA surveillance that is required for the degradation of a specific subset of nuclear exosome targets.},
note = {1553-7404 (Electronic)
1553-7390 (Linking)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Riley, L G; Rudinger-Thirion, J; Schmitz-Abe, K; Thorburn, D R; Davis, R L; Teo, J; Arbuckle, S; Cooper, S T; Campagna, D R; Frugier, M; Markianos, K; Sue, C M; Fleming, M D; Christodoulou, J
LARS2 Variants Associated with Hydrops, Lactic Acidosis, Sideroblastic Anemia, and Multisystem Failure Article de journal
Dans: JIMD Rep, vol. 28, p. 49-57, 2016, ISBN: 26537577, (2192-8304 (Print) 2192-8304 (Linking) Journal Article).
@article{nokey,
title = {LARS2 Variants Associated with Hydrops, Lactic Acidosis, Sideroblastic Anemia, and Multisystem Failure},
author = {L G Riley and J Rudinger-Thirion and K Schmitz-Abe and D R Thorburn and R L Davis and J Teo and S Arbuckle and S T Cooper and D R Campagna and M Frugier and K Markianos and C M Sue and M D Fleming and J Christodoulou},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=26537577},
doi = {10.1007/8904_2015_515},
isbn = {26537577},
year = {2016},
date = {2016-01-01},
journal = {JIMD Rep},
volume = {28},
pages = {49-57},
abstract = {Pathogenic variants in mitochondrial aminoacyl-tRNA synthetases result in a broad range of mitochondrial respiratory chain disorders despite their shared role in mitochondrial protein synthesis. LARS2 encodes the mitochondrial leucyl-tRNA synthetase, which attaches leucine to its cognate tRNA. Sequence variants in LARS2 have previously been associated with Perrault syndrome, characterized by premature ovarian failure and hearing loss (OMIM #615300). In this study, we report variants in LARS2 that are associated with a severe multisystem metabolic disorder. The proband was born prematurely with severe lactic acidosis, hydrops, and sideroblastic anemia. She had multisystem complications with hyaline membrane disease, impaired cardiac function, a coagulopathy, pulmonary hypertension, and progressive renal disease and succumbed at 5 days of age. Whole exome sequencing of patient DNA revealed compound heterozygous variants in LARS2 (c.1289C>T; p.Ala430Val and c.1565C>A; p.Thr522Asn). The c.1565C>A (p.Thr522Asn) LARS2 variant has previously been associated with Perrault syndrome and both identified variants are predicted to be damaging (SIFT, PolyPhen). Muscle and liver samples from the proband did not display marked mitochondrial respiratory chain enzyme deficiency. Immunoblotting of patient muscle and liver showed LARS2 levels were reduced in liver and complex I protein levels were reduced in patient muscle and liver. Aminoacylation assays revealed p.Ala430Val LARS2 had an 18-fold loss of catalytic efficiency and p.Thr522Asn a 9-fold loss compared to wild-type LARS2. We suggest that the identified LARS2 variants are responsible for the severe multisystem clinical phenotype seen in this baby and that mutations in LARS2 can result in variable phenotypes.},
note = {2192-8304 (Print)
2192-8304 (Linking)
Journal Article},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Schalk, C; Drevensek, S; Kramdi, A; Kassam, M; Ahmed, I; Cognat, V; Graindorge, S; Bergdoll, M; Baumberger, N; Heintz, D; Bowler, C; Genschik, P; Barneche, F; Colot, V; Molinier, J
DNA DAMAGE BINDING PROTEIN2 Shapes the DNA Methylation Landscape Article de journal
Dans: Plant Cell, vol. 28, no. 9, p. 2043-2059, 2016, ISBN: 27531226, (1532-298X (Electronic) 1040-4651 (Linking) Journal Article).
@article{nokey,
title = {DNA DAMAGE BINDING PROTEIN2 Shapes the DNA Methylation Landscape},
author = {C Schalk and S Drevensek and A Kramdi and M Kassam and I Ahmed and V Cognat and S Graindorge and M Bergdoll and N Baumberger and D Heintz and C Bowler and P Genschik and F Barneche and V Colot and J Molinier},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=27531226},
doi = {10.1105/tpc.16.00474},
isbn = {27531226},
year = {2016},
date = {2016-01-01},
journal = {Plant Cell},
volume = {28},
number = {9},
pages = {2043-2059},
abstract = {In eukaryotes, DNA repair pathways help to maintain genome integrity and epigenomic patterns. However, the factors at the nexus of DNA repair and chromatin modification/remodeling remain poorly characterized. Here, we uncover a previously unrecognized interplay between the DNA repair factor DNA DAMAGE BINDING PROTEIN2 (DDB2) and the DNA methylation machinery in Arabidopsis thaliana Loss-of-function mutation in DDB2 leads to genome-wide DNA methylation alterations. Genetic and biochemical evidence indicate that at many repeat loci, DDB2 influences de novo DNA methylation by interacting with ARGONAUTE4 and by controlling the local abundance of 24-nucleotide short interfering RNAs (siRNAs). We also show that DDB2 regulates active DNA demethylation mediated by REPRESSOR OF SILENCING1 and DEMETER LIKE3. Together, these findings reveal a role for the DNA repair factor DDB2 in shaping the Arabidopsis DNA methylation landscape in the absence of applied genotoxic stress.},
note = {1532-298X (Electronic)
1040-4651 (Linking)
Journal Article},
keywords = {},
pubstate = {published},
tppubtype = {article}
}