Showing 1 - 20 results of 404 for search '"Saccharomyces cerevisiae metabolism"', query time: 2.46s Refine Results
1
Fruits of their labour: biotransformation reactions of yeasts during brewery fermentation

Authors: Natalia Svedlund, Simon Evering, Brian Gibson, Kristoffer Krogerus

Source: Svedlund, N, Evering, S, Gibson, B & Krogerus, K 2022, ' Fruits of their labour : Biotransformation reactions of yeasts during brewery fermentation ', Applied Microbiology and Biotechnology, vol. 106, no. 13-16, pp. 4929–4944 . https://doi.org/10.1007/s00253-022-12068-w

Subject Terms: Applied Microbiology and Biotechnology, General Medicine, Biotechnology, Beverages, Biotransformation, Fermentation, Polyfunctional thiol, Terpene, Yeast, β-glucosidase, β-lyase, Alcohols/metabolism, Fruit/metabolism, Flavoring Agents/metabolism, Yeasts/metabolism, Terpenes/metabolism, Beer, Saccharomyces cerevisiae/metabolism, Lyases/metabolism, Sulfhydryl Compounds/metabolism

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https://doi.org/10.1007/s00253-022-12068-w

2
mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells

Authors: Tomoyuki Hatano, Tzer Chyn Lim, Ingrid Billault-Chaumartin, Anubhav Dhar, Ying Gu, Teresa Massam-Wu, William Scott, Sushmitha Adishesha, Bernardo Chapa-y-Lazo, Luke Springall, Lavanya Sivashanmugam, Masanori Mishima, Sophie G. Martin, Snezhana Oliferenko, Saravanan Palani, Mohan K. Balasubramanian

Source: Journal of cell science, vol. 135, no. 18, pp. jcs260288

Subject Terms: Actin Cytoskeleton/metabolism, Actins/metabolism, Actomyosin/metabolism, Animals, Cell Cycle Proteins/metabolism, Cytokinesis, Fluorescent Dyes/metabolism, Mammals/metabolism, Protein Isoforms/metabolism, Saccharomyces cerevisiae/metabolism, Schizosaccharomyces/metabolism, Schizosaccharomyces pombe Proteins/metabolism, Single-Domain Antibodies/metabolism, Tropomyosin/genetics, Tropomyosin/metabolism, Actin, Live imaging, Tropomyosin, mNeonGreen, Nanobody, Cytokinesis, Ecology,Evolution & Ethology, Cell Biology, Cell Cycle & Chromosomes

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https://serval.unil.ch/notice/serval:BIB_E5AA6797B9AB

3
The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans

Authors: Daiß, Julia L., Pilsl, Michael, Straub, Kristina, Bleckmann, Andrea, Höcherl, Mona, Heiss, Florian B., Abascal-Palacios, Guillermo, Ramsay, Ewan Phillip, Tlučková, Katarina, Mars, Jean-Clement, Fürtges, Torben, Bruckmann, Astrid, Rudack, Till, Bernecky, Carrie, Lamour, Valérie, Panov, Konstantin, Vannini, Alessandro, Moss, Tom, Engel, Christoph

Contributors: Universität Regensburg (UR), Universidad del Pais Vasco / Euskal Herriko Unibertsitatea [Espagne] (UPV/EHU), Ikerbasque - Basque Foundation for Science, Université de Montréal (UdeM), Ruhr-Universität Bochum [Bochum], Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Queen's University [Belfast] (QUB), The institute of cancer research [London], Université Laval [Québec] (ULaval)

Source: Daiß, J L, Pilsl, M, Straub, K, Bleckmann, A, Höcherl, M, Heiss, F B, Abascal-Palacios, G, Ramsay, E P, Tlučková, K, Mars, J-C, Fürtges, T, Bruckmann, A, Rudack, T, Bernecky, C, Lamour, V, Panov, K, Vannini, A, Moss, T & Engel, C 2022, ' The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans ', Life Science Alliance, vol. 5, no. 11, e202201568 . https://doi.org/10.26508/lsa.202201568
Life Science Alliance
Life Science Alliance, Life Science Alliance LLC, 2022, 5 (11), pp.e202201568. ⟨10.26508/lsa.202201568⟩

Subject Terms: Animals, RNA Polymerase I - genetics - metabolism, DNA, Saccharomyces cerevisiae - metabolism, RNA Precursors, Transcription Factors - metabolism, Humans, SDG 3 - Good Health and Well-being, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], 570 Biowissenschaften, Biologie, ddc:570, Health, Toxicology and Mutagenesis, Plant Science, Biochemistry, Genetics and Molecular Biology (miscellaneous), Ecology

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https://pure.qub.ac.uk/en/publications/3f49ef04-8066-4a34-951f-d75e806488a5

4
Phosphoregulation of the autophagy machinery by kinases and phosphatases

Authors: Babu Raman, Mariya Licheva, Claudine Kraft, Fulvio Reggiori

Source: Licheva, M, Raman, B, Kraft, C & Reggiori, F 2022, ' Phosphoregulation of the autophagy machinery by kinases and phosphatases ', Autophagy, vol. 18, no. 1, pp. 104-123 . https://doi.org/10.1080/15548627.2021.1909407

Subject Terms: Autophagosome, macroautophagy, PAS, phagophore, posttranslational modification, Autophagy/physiology, Autophagy-Related Proteins/metabolism, Humans, Phosphoric Monoester Hydrolases/metabolism, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/metabolism, Cell Biology, Molecular Biology, Autophagy, Protein network, Cell biology, Function (biology), Kinase, Biology, Saccharomyces cerevisiae, biology.organism_classification, Phosphatase, Cellular differentiation

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5
Full humanization of the glycolytic pathway in Saccharomyces cerevisiae

Authors: Boonekamp, Francine J, Knibbe, Ewout, Vieira-Lara, Marcel A, Wijsman, Melanie, Luttik, Marijke A H, van Eunen, Karen, Ridder, Maxime den, Bron, Reinier, Almonacid Suarez, Ana Maria, van Rijn, Patrick, Wolters, Justina C, Pabst, Martin, Daran, Jean-Marc, Bakker, Barbara M, Daran-Lapujade, Pascale

Contributors: Molecular Cell Physiology, AIMMS, Nanotechnology and Biophysics in Medicine (NANOBIOMED), Restoring Organ Function by Means of Regenerative Medicine (REGENERATE), Center for Liver, Digestive and Metabolic Diseases (CLDM)

Source: Cell Reports, 39(13)
Cell Reports, 39(13):111010. Cell Press
Cell reports, 39(13):111010. CELL PRESS

Subject Terms: Animals, Glycolysis, Hexokinase/genetics, Humans, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/genetics, Synthetic Biology, adaptive laboratory evolution, CP: Metabolism, hexokinase, humanized yeast model, moonlighting function, pathway transplantation, Saccharomyces cerevisiae, General Biochemistry, Genetics and Molecular Biology

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7
Fruits of their labour

Source: Applied Microbiology and Biotechnology. 106(13-16):4944-4944

Subject Terms: Beverages, Biotransformation, Fermentation, Polyfunctional thiol, Terpene, Yeast, β-glucosidase, β-lyase, Alcohols/metabolism, Fruit/metabolism, Flavoring Agents/metabolism, Yeasts/metabolism, Terpenes/metabolism, Beer, Saccharomyces cerevisiae/metabolism, Lyases/metabolism, Sulfhydryl Compounds/metabolism

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https://doi.org/10.1007/s00253-022-12068-w

8
Towards a molecular mechanism underlying mitochondrial protein import through the TOM and TIM23 complexes

Authors: Ian Collinson, Xia Liu, Mark S. Dillingham, William J. Allen, Holly C Ford, Gonçalo C. Pereira

Source: Ford, H C, Allen, W J, Pereira, G C, Liu, X, Dillingham, M S & Collinson, I 2022, ' Towards a molecular mechanism underlying mitochondrial protein import through the TOM and TIM23 complexes ', eLife, vol. 11, e75426 . https://doi.org/10.7554/eLife.75426

Subject Terms: ATP hydrolysis, Translocase of the outer membrane, Chemistry, Mitochondrion, Cell biology, Cytosol, Molecular machine, Translocase, biology.protein, biology, Luciferase, Mitochondrial DNA, Carrier Proteins/metabolism, Luciferases, Mitochondrial Precursor Protein Import Complex Proteins/metabolism, Mitochondrial Proteins/metabolism, Protein Transport, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/metabolism, General Immunology and Microbiology, General Biochemistry, Genetics and Molecular Biology, General Medicine, General Neuroscience

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https://doi.org/10.1101/2021.08.30.458282

9
Quantitative global studies reveal differential translational control by start codon context across the fungal kingdom

Authors: Frédérique Moyrand, Prashanthi Natarajan, Corinne Maufrais, Guilhem Janbon, Laura R. Tuck, Jade Sales-Lee, Frank Feuerbach, Hiten D. Madhani, Luciana de Oliveira, Wallace Ewj

Contributors: Centre for Synthetic and Systems Biology (Ssynthsys), University of Edinburgh, Hub Bioinformatique et Biostatistique - Bioinformatics and Biostatistics HUB, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Biologie des ARN des Pathogènes fongiques - RNA Biology of Fungal Pathogens, Institut Pasteur [Paris], Department of Biochemistry and Biophysics [San Francisco], University of California, Génétique des Interactions macromoléculaires, Chan Zuckerberg BioHub [San Francisco, CA], This work in the Madhani lab was supported by grants from the US National Institutes of Health [R01AI120464, R01GM71801 to H.D.M.], H.D.M. is an Investigator of the Chan-Zuckerberg Biohub, E.W.J.W. is a Sir Henry Dale Fellow, supported by a Sir Henry Dale Fellowship jointly funded by the Wellcome Trust and the Royal Society [208779/Z/17/Z], L.T. is supported by a Wellcome-University of Edinburgh ISSF3 award, This work in the Janbon lab was supported by an Infect-ERA grant (project Cryptoview). Funding for open access charge: University of Edinburgh., We thank members of the Wallace, Janbon, and Madhani labs for helpful discussions and comments on the manuscript. We thank Juan Mata for sharing intermediate data related to (59). We are grateful to J. Weissman (UCSF) for advice on ribosome profiling. We thank three anonymous reviewers for their helpful comments., University of California (UC)

Source: Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2020, 48 (5), pp.2312-2331. ⟨10.1093/nar/gkaa060⟩
Nucleic Acids Research, 2020, 48 (5), pp.2312-2331. ⟨10.1093/nar/gkaa060⟩
Wallace, E W J, Maufrais, C, Sales Lee, J, Tuck, L, de Oliveira, L, Feuerbach, F, Moyrand, F, Natarajan, P, Madhani, H D & Janbon, G 2020, ' Quantitative global studies reveal differential translational control by start codon context across the fungal kingdom ', Nucleic Acids Research, vol. 48, no. 5, pp. 2312-2331 . https://doi.org/10.1093/nar/gkaa060

Subject Terms: Genetics, Translation (biology), Biology, Transfer RNA, Open reading frame, Gene, Ribosome, Context (language use), Start codon, Kozak consensus sequence, MESH: Amino Acyl-tRNA Synthetases / genetics, MESH: Amino Acyl-tRNA Synthetases / metabolism, MESH: Genome, Fungal, MESH: Neurospora crassa / genetics, MESH: Neurospora crassa / metabolism, MESH: Open Reading Frames, MESH: Peptide Chain Initiation, Translational, MESH: Saccharomyces cerevisiae / genetics, MESH: Saccharomyces cerevisiae / metabolism, MESH: Schizosaccharomyces / genetics, MESH: Schizosaccharomyces / metabolism, MESH: Species Specificity, MESH: Candida albicans / genetics, MESH: Candida albicans / metabolism, MESH: Chromosome Mapping, MESH: Codon, Initiator / chemistry, MESH: Codon, Initiator / metabolism, MESH: Cryptococcus / genetics, MESH: Cryptococcus / metabolism, MESH: Gene Expression Regulation, Fungal, [SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology, [SDV.GEN]Life Sciences [q-bio]/Genetics, Data Resources and Analyses

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https://doi.org/10.1093/nar/gkaa060

10
Endocytosis in plants: Peculiarities and roles in the regulated trafficking of plant metal transporters

Authors: Grégory Vert, Rumen Ivanov

Contributors: Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], Signalisation Cellulaire et Ubiquitination, Laboratoire de Recherche en Sciences Végétales (LRSV), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), ANR-13-JSV2-0004,Ubi63,Exploration du role de la polyubiquitination K63 en utilisant les plantes comme modèle(2013), ANR-10-LABX-0041,TULIP,Towards a Unified theory of biotic Interactions: the roLe of environmental(2010), ANR-11-IDEX-0002,UNITI,Université Fédérale de Toulouse(2011)

Source: Biology of the Cell
Biology of the Cell, Wiley, 2021, 113 (1), pp.1-13. ⟨10.1111/boc.202000118⟩

Subject Terms: degradation, endocytosis, IRT1, metal, ubiquitin, MESH: Animals, MESH: Arabidopsis / metabolism, MESH: Arabidopsis Proteins / metabolism, MESH: Biological Transport, MESH: Cation Transport Proteins / metabolism, MESH: Cell Membrane / metabolism, MESH: Endocytosis, MESH: Iron / metabolism, MESH: Mammals / metabolism, MESH: Saccharomyces cerevisiae / metabolism, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Cell Biology, General Medicine, Endomembrane system, Endocytic recycling, Biology, Endocytic cycle, Endocytosis, Receptor signaling, Transporter, Cell biology, Ubiquitin, biology.protein, Transmembrane protein

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https://hal.archives-ouvertes.fr/hal-03403467

11
Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding

Authors: Taschner, Michael, Basquin, Jérôme, Steigenberger, Barbara, Schäfer, Ingmar B, Soh, Young-Min, Basquin, Claire, Lorentzen, Esben, Räschle, Markus, Scheltema, Richard A, Gruber, Stephan, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics

Source: Taschner, M, Basquin, J, Steigenberger, B, Schäfer, I B, Soh, Y M, Basquin, C, Lorentzen, E, Räschle, M, Scheltema, R A & Gruber, S 2021, ' Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding ', EMBO Journal, vol. 40, no. 15, e107807 . https://doi.org/10.15252/embj.2021107807
The EMBO journal, vol. 40, no. 15, pp. e107807
The EMBO Journal
EMBO Journal, 40(15), 1. Nature Publishing Group

Subject Terms: Smc5/6, chromosome segregation, cohesion, condensin, loop extrusion, Neuroscience(all), Molecular Biology, Biochemistry, Genetics and Molecular Biology(all), Immunology and Microbiology(all), Adenosine Triphosphate/metabolism, Cell Cycle Proteins/chemistry, Cell Cycle Proteins/genetics, Cell Cycle Proteins/metabolism, Chromosomal Proteins, Non-Histone/chemistry, Chromosomal Proteins, Non-Histone/genetics, Chromosomal Proteins, Non-Histone/metabolism, Cryoelectron Microscopy, Crystallography, X-Ray, DNA, Fungal/metabolism, Hydrolysis, Multiprotein Complexes/chemistry, Multiprotein Complexes/metabolism, Protein Conformation, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/chemistry, Saccharomyces cerevisiae Proteins/genetics, Saccharomyces cerevisiae Proteins/metabolism, Article, Articles, DNA Replication, Repair & Recombination, Structural Biology, General Immunology and Microbiology, General Biochemistry, Genetics and Molecular Biology, General Neuroscience, DNA, chemistry.chemical_compound, chemistry, DNA Folding, Biophysics, Binding site, Cysteine, ATP hydrolysis, ATPase, biology.protein, biology, DNA repair, Smc5-Smc6 complex, Biochemistry, Genetics and Molecular Biology(all)

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12
Pkh1p-Ypk1p and Pkh1p-Sch9p Pathways Are Activated by Acetic Acid to Induce a Mitochondrial-Dependent Regulated Cell Death

Authors: Filipa Mendes, Manuela Côrte-Real, Vítor Costa, Susana R. Chaves, António Rego

Contributors: Instituto de Investigação e Inovação em Saúde

Source: Oxidative Medicine and Cellular Longevity, Vol 2020 (2020)
Oxidative Medicine and Cellular Longevity

Subject Terms: Cytology, QH573-671, Research Article, Article Subject, Cell Biology, Aging, General Medicine, Biochemistry, Chemistry, Cytochrome c, biology.protein, biology, Cell biology, Phosphorylation, Mitochondrion, Apoptosis, Endoplasmic reticulum, Cell fate determination, Ceramide, chemistry.chemical_compound, Sphingolipid, Acetic Acid / metabolism, Cell Death, Mitochondria / metabolism, Protein Serine-Threonine Kinases / metabolism, Saccharomyces cerevisiae / metabolism, Saccharomyces cerevisiae Proteins / metabolism

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https://doaj.org/article/937feb243626486fa560f1ae5e69691d

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13
A newly characterized vacuolar serine carboxypeptidase, Atg42/Ybr139w, is required for normal vacuole function and the terminal steps of autophagy in the yeast Saccharomyces cerevisiae

Authors: Aileen R. Ariosa, Muriel Mari, Daniel J. Klionsky, Katherine R. Parzych

Contributors: Center for Liver, Digestive and Metabolic Diseases (CLDM)

Source: Molecular Biology of the Cell
Molecular Biology of the Cell, 29(9), 1089-1099. AMER SOC CELL BIOLOGY
Parzych, K R, Ariosa, A, Mari, M & Klionsky, D J 2018, ' A newly characterized vacuolar serine carboxypeptidase, Atg42/Ybr139w, is required for normal vacuole function and the terminal steps of autophagy in the yeast Saccharomyces cerevisiae ', Molecular Biology of the Cell, vol. 29, no. 9, pp. 1089-1099 . https://doi.org/10.1091/mbc.E17-08-0516

Subject Terms: Articles, Membrane Trafficking, macromolecular substances, PROTEIN-KINASE-A, TARGETING PATHWAY, PUTATIVE LIPASE, BUDDING YEAST, BIOSYNTHESIS, TRANSPORT, CYTOPLASM, MUTANTS, BIOGENESIS, INDUCTION, Cell Biology, Molecular Biology, Vacuole, Cell biology, Zymogen activation, Lysosome, medicine.anatomical_structure, medicine, Cytoplasm, Saccharomyces cerevisiae, biology.organism_classification, biology, Autophagy, Cytosol, Yeast, Autophagy/physiology, Carboxypeptidases/metabolism, Lysosomes/metabolism, Protein Biosynthesis, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/metabolism, Vacuoles/metabolism

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http://europepmc.org/articles/PMC5921575

14
Methylselenol Produced In Vivo from Methylseleninic Acid or Dimethyl Diselenide Induces Toxic Protein Aggregation in Saccharomyces cerevisiae

Authors: Katarzyna Bierla, Marc Dauplais, Joanna Szpunar, Ryszard Lobinski, Coralie Maizeray, Roxane Lestini, Pierre Plateau, Myriam Lazard

Contributors: Laboratoire de Biochimie de l'Ecole polytechnique (BIOC), École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS), Institut des sciences analytiques et de physico-chimie pour l'environnement et les materiaux (IPREM), Université de Pau et des Pays de l'Adour (UPPA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie Structurale de la Cellule (BIOC), Université de Pau et des Pays de l'Adour (UPPA)-Centre National de la Recherche Scientifique (CNRS)

Source: International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2021, 22 (5), pp.2241. ⟨10.3390/ijms22052241⟩
International Journal of Molecular Sciences, MDPI, 2021, 22 (5), pp.1-21. ⟨10.3390/ijms22052241⟩
Volume 22
Issue 5
International Journal of Molecular Sciences, Vol 22, Iss 2241, p 2241 (2021)

Subject Terms: Inorganic Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Computer Science Applications, Spectroscopy, Molecular Biology, General Medicine, Catalysis, Enzyme, chemistry.chemical_classification, chemistry, Metabolite, chemistry.chemical_compound, Glutathione, Glutathione reductase, Thioredoxin reductase, Selenium, chemistry.chemical_element, Cytotoxicity, Biochemistry, Thioredoxin, methylselenol, diselenide, methylseleninic acid, thiol/disulfide exchange, redox equilibrium, Saccharomyces cerevisiae metabolism, toxicity, protein aggregation, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, [SDV.TOX]Life Sciences [q-bio]/Toxicology, [CHIM.MATE]Chemical Sciences/Material chemistry, [CHIM.POLY]Chemical Sciences/Polymers, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, M methylselenol, Article, lcsh:Biology (General), lcsh:QH301-705.5, lcsh:Chemistry, lcsh:QD1-999

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https://doi.org/10.3390/ijms22052241

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16
FACT mediates cohesin function on chromatin

Authors: Luis Aragón, Mohammad M. Karimi, Pilar Gutiérrez-Escribano, Francisco Antequera, Mar Sánchez, Axel Cournac, Luciana Lazar-Stefanita, Jonay García-Luis, Adam Jarmuz, Romain Koszul, Marian Dore, Holger B. Kramer, Sara Serrate González, Alicia García, Alex Montoya, Agnès Thierry

Contributors: Wellcome Trust, Medical Research Council (UK), European Commission, European Research Council, Agence Nationale de la Recherche (France), Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), MRC London Institute of Medical Sciences (LMC), Régulation spatiale des Génomes - Spatial Regulation of Genomes, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Instituto de Biología Funcional y Genómica [Salamanca, Spain] (IBFG), Universidad de Salamanca-Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), The work in the L.A. laboratory was supported by a Wellcome Trust Senior Investigator award to L.A. (100955, ‘Functional dissection of mitotic chromatin’) and the London Institute of Medical Research (LMS), which receives its core funding from the UK Medical Research Council. This research was further supported by funding from The European Research Council (R.K.), Agence Nationale pour la Recherche (R.K.) and the the Spanish Ministerio de Economía, Industria y Competitividad (BFU2017-89622-P, F.A.)., We thank the members of the L.A., R.K. and P.A. laboratories for fruitful discussions and advice.

Source: Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, Nature Publishing Group, 2019, 26 (10), pp.970-979. ⟨10.1038/s41594-019-0307-x⟩
Nature structural & molecular biology

Subject Terms: biological phenomena, cell phenomena, and immunity, Chromosome condensation, Chromatin remodelling, Nuclear organization, MESH: Cell Cycle Proteins / metabolism, MESH: Chromatin / metabolism, MESH: Chromosomal Proteins, Non-Histone / metabolism, MESH: DNA-Binding Proteins / metabolism, MESH: High Mobility Group Proteins / metabolism, MESH: Protein Interaction Maps, MESH: Saccharomyces cerevisiae / cytology, MESH: Saccharomyces cerevisiae / metabolism, MESH: Saccharomyces cerevisiae Proteins / metabolism, MESH: Transcriptional Elongation Factors / metabolism, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Article, Molecular Biology, Structural Biology, Chromosome, Chromatin, Histone, biology.protein, biology, Cohesin, Metaphase, Nucleosome, Chromosome segregation, Chemistry, Establishment of sister chromatid cohesion, Cell biology

Access URL: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ff873f2a495cde66beec1322917ac14
http://hdl.handle.net/10261/203767

17
SNARE-mediated membrane fusion arrests at pore expansion to regulate the volume of an organelle

Authors: Massimo D'Agostino, Herre Jelger Risselada, Laura J Endter, Véronique Comte‐Miserez, Andreas Mayer

Contributors: D'Agostino, Massimo, Risselada, Herre Jelger, Endter, Laura J, Comte-Miserez, Véronique, Mayer, Andreas

Source: The EMBO journal, vol. 37, no. 19

Subject Terms: Membrane Fusion, Molecular Dynamics Simulation, SNARE Proteins/chemistry, SNARE Proteins/genetics, SNARE Proteins/metabolism, Saccharomyces cerevisiae/chemistry, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/chemistry, Saccharomyces cerevisiae Proteins/genetics, Saccharomyces cerevisiae Proteins/metabolism, Vacuoles/chemistry, Vacuoles/genetics, Vacuoles/metabolism, SNAREs, endosomes, lysosomes, membrane fusion, vacuoles, General Immunology and Microbiology, General Biochemistry, Genetics and Molecular Biology, Molecular Biology, General Neuroscience, Vacuole, Osmotic pressure, Fusion, Endosome, Lipid bilayer fusion, Biology, Biophysics, Organelle, SNARE complex assembly, Membrane, Articles, SNARE, endosome, lysosome

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https://serval.unil.ch/notice/serval:BIB_5A00C7C05A19

18
Real-time quantification of protein expression at the single-cell level via dynamic protein synthesis translocation reporters

Authors: Aymoz, Delphine, Wosika, Victoria, Durandau, Eric, Pelet, Serge

Source: Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Nature Communications
Nature Communications, vol. 7, pp. 11304

Subject Terms: Science, food and beverages, fungi, Article, Gene Expression Regulation, Fungal, Genes, Reporter, Glycerol/metabolism, Glycerol-3-Phosphate Dehydrogenase (NAD+)/genetics, Glycerol-3-Phosphate Dehydrogenase (NAD+)/metabolism, Green Fluorescent Proteins/genetics, Green Fluorescent Proteins/metabolism, Luminescent Proteins/genetics, Luminescent Proteins/metabolism, Membrane Transport Proteins/genetics, Membrane Transport Proteins/metabolism, Protein Biosynthesis, Protein Processing, Post-Translational, Protein Transport, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/genetics, Saccharomyces cerevisiae Proteins/metabolism, Single-Cell Analysis/methods, Time Factors

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Access URL: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::cf3f73a1480b063dc36edcd7a177b363
https://doaj.org/article/985c22e4d7a44ff48c0c5e471df76961

20
Antisense transcriptional interference mediates condition-specific gene repression in budding yeast

Authors: Antonia Doyen, Alain Jacquier, Thomas Kergrohen, Alicia Nevers, Gwenael Badis, Christophe Malabat, Bertrand Néron

Contributors: Génétique des Interactions macromoléculaires, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC), Centre de Bioinformatique, Biostatistique et Biologie Intégrative (C3BI), Pasteur Institute, the Centre National de la Recherche Scientifique and the Agence Nationale pour la Recherche [ANR-14-CE-10-0014-01, 2014], A.N. received Fellowships from the French Ministry of Research and from the Fondation pour la Recherche Médicale [FDT20160435375, 2016]. Funding for open access charge: Agence Nationale pour la Recherche [ANR-14-CE-10-0014-01, 2014]., We thank Frank Feuerbach for providing strains LMA2811 and LMA2819. We thank Bernard Turcotte, Cosmin Saveanu and Micheline Fromont-Racine for discussions and critical reading of the manuscript. We acknowledge Jean Yves Coppee and Caroline Proux for the facilities and expertise of the Transcriptomic Platform (PF2) for cDNA libraries sequencing., Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris]

Source: Nucleic Acids Research
Nucleic Acids Research, 2018, 46 (12), pp.6009-6025. ⟨10.1093/nar/gky342⟩
Nucleic Acids Research, Oxford University Press, 2018, 46 (12), pp.6009-6025. ⟨10.1093/nar/gky342⟩

Subject Terms: MESH: Gene Deletion, MESH: Gene Expression Regulation, Fungal, MESH: RNA Helicases/genetics, MESH: RNA Polymerase II/metabolism, MESH: RNA, Antisense/biosynthesis, MESH: Saccharomyces cerevisiae/genetics, MESH: Saccharomyces cerevisiae/metabolism, MESH: Saccharomyces cerevisiae Proteins/genetics, MESH: Transcription Initiation Site, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Gene, Sense (molecular biology), Transcription (biology), Genetics, Biology, Mutant, Regulation of gene expression, Messenger RNA, Psychological repression, Transcriptional noise, medicine.disease, medicine, Gene regulation, Chromatin and Epigenetics, Promoter, Transcriptome, Cell biology, Chromatin, Gene expression

Access URL: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6025e7be12b7d285ac756d69d1201269
https://hal.archives-ouvertes.fr/hal-02349600

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