Suchergebnisse - "Saccharomyces cerevisiae Proteins Metabolism"

Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4

Autoren: Sokołowski, Mikołaj Kwasna, Dominika Ravichandran, Keerthiraju E et al.

Quelle: Nucleic Acids Res

Schlagwörter: Models, Molecular, 0301 basic medicine, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae Proteins Genetics, Saccharomyces cerevisiae Proteins Metabolism, Ubiquitin-Activating Enzymes, Saccharomyces cerevisiae, Saccharomyces Cerevisiae Genetics, RNA, Transfer Chemistry, Ubiquitin-Activating Enzymes Genetics, 03 medical and health sciences, Sulfhydryl Compounds Metabolism, Protein Domains, RNA, Transfer, RNA, Transfer Metabolism, Saccharomyces cerevisiae Metabolism, Sulfhydryl Compounds, Nucleotidyltransferases Chemistry, Ubiquitins, Ubiquitin-Activating Enzymes Chemistry, 0303 health sciences, Nucleotidyltransferases Metabolism, Ubiquitin-Activating Enzymes Metabolism, Ubiquitins Genetics, Cryoelectron Microscopy, Ubiquitins Metabolism, Molecular and Structural Biology, Nucleotidyltransferases, Ubiquitins Chemistry, Sulfhydryl Compounds Chemistry, Mutation, Nucleotidyltransferases Genetics, Saccharomyces cerevisiae Proteins Chemistry, Protein Binding

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/39673271
https://ruj.uj.edu.pl/handle/item/499751
https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkae1111/7914207

Docking a flexible basket onto the core of the nuclear pore complex

Autoren: Edvinas Stankunas Alwin Köhler

Quelle: Nat Cell Biol
Nature Cell Biology

Schlagwörter: Nuclear Pore Complex Proteins, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins, 106023 Molekularbiologie, Nuclear Pore Complex Proteins/metabolism, Nuclear Pore, Saccharomyces cerevisiae, 106023 Molecular biology, Nuclear Pore/metabolism, Saccharomyces cerevisiae Proteins/metabolism, Article, Protein Binding

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/39138317

mRNA trafficking directs cell-size-scaling of mitochondria distribution and function

Autoren: Joshua J. Bradbury Georgia E. Hulmes Ranjith Viswanathan et al.

Quelle: Bradbury, J J, Hulmes, G E, Viswanathan, R, Costa, G, Lovegrove, H E & Herbert, S P 2025, 'mRNA trafficking directs cell-size-scaling of mitochondria distribution and function', Nature Communications, vol. 16, 7029. https://doi.org/10.1038/s41467-025-61940-6
Bradbury, J J, Hulmes, G E, Viswanathan, R, Costa, G, Lovegrove, H E & Herbert, S P 2025, 'mRNA trafficking directs cell-size-scaling of mitochondria distribution and function', Nature Communications, vol. 16, no. 1, pp. 7029. https://doi.org/10.1038/s41467-025-61940-6
Bradbury, J J, Hulmes, G E, Viswanathan, R, Costa, G, Lovegrove, H E & Herbert, S P 2025 ' mRNA trafficking directs cell-size-scaling of mitochondria distribution and function ' . https://doi.org/10.1101/2025.05.05.652164

Schlagwörter: Saccharomyces cerevisiae/metabolism, 3' Untranslated Regions/genetics, Mitochondria/metabolism, RNA, Messenger/metabolism, RNA, Humans, Messenger/metabolism, Saccharomyces cerevisiae Proteins/metabolism, RNA Transport, Cell Size

Dateibeschreibung: application/pdf

Zugangs-URL: https://research.manchester.ac.uk/en/publications/107b9a02-9026-4c47-9b23-73974ef8d0df
https://doi.org/10.1038/s41467-025-61940-6
https://pure.qub.ac.uk/en/publications/72058e32-f644-46f0-b607-3cb7c53e0805
https://research.manchester.ac.uk/en/publications/31374a9c-34df-4320-9446-452aa6eb2767
http://biorxiv.org/lookup/doi/10.1101/2025.05.05.652164
https://doi.org/10.1101/2025.05.05.652164

tRNA binding to Kti12 is crucial for wobble uridine modification by Elongator

Autoren: Scherf, David Hammermeister, Alexander Böhnert, Pauline et al.

Quelle: Nucleic Acids Res

Schlagwörter: Bäckerhefe, Anticodon Metabolism, Saccharomyces cerevisiae Proteins, Uridine Metabolism, Saccharomyces Cerevisiae Proteins Genetics, Killer Factors, Yeast Metabolism, Saccharomyces cerevisiae, Saccharomyces Cerevisiae Genetics, RNA, Transfer Chemistry, Killer Factors, Yeast, Saccharomyces cerevisia Metabolism, RNA, Transfer, RNA, Transfer Metabolism, Mutation, Transfer-RNS, Saccharomyces Cerevisiae Proteins Metabolism, RNA and RNA-protein complexes, Anticodon, Amino Acid Sequence, Uridin, Uridine, Saccharomyces Cerevisiae Proteins Chemistry, Protein Binding

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/40226916
https://ruj.uj.edu.pl/handle/item/559194
https://phaidra.vetmeduni.ac.at/o:4101
https://doi.org/10.1093/nar/gkaf296

Transcriptional heterogeneity shapes stress-adaptive responses in yeast

Autoren: Nadal-Ribelles, Mariona Solé Serra, Carme de Nadal, Eulalia et al.

Quelle: Nat Commun
Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona))
Dipòsit Digital de la UB
instname
Nature Communications, Vol 16, Iss 1, Pp 1-17 (2025)
Nature communications, vol. 16, no. 1, pp. 2631

Schlagwörter: Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae/physiology, Gene Expression Regulation, Fungal, Transcriptome/genetics, Adaptation, Physiological/genetics, Stress, Physiological/genetics, Saccharomyces cerevisiae Proteins/genetics, Saccharomyces cerevisiae Proteins/metabolism, Transcription, Genetic, Gene Expression Profiling, Signal Transduction/genetics, Osmotic Pressure, RNA-Seq, Genetic transcription, Science, Saccharomyces cerevisiae, Adaptation, Physiological, Article, Estrès (Fisiologia), Transcripció genètica, Stress, Physiological, Transcriptome, Stress (Physiology), Signal Transduction

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/40097446
https://hdl.handle.net/2445/219972
https://doaj.org/article/c3e42b85d2ea40f3af93523aa222cff2
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_C95B1063E3EA8
https://serval.unil.ch/notice/serval:BIB_C95B1063E3EA
https://serval.unil.ch/resource/serval:BIB_C95B1063E3EA.P001/REF.pdf

Autorepression of yeast Hsp70 cochaperones by intramolecular interactions involving their J-domains

Autoren: Mathieu E. Rebeaud Satyam Tiwari Bruno Fauvet et al.

Quelle: Cell Stress Chaperones
Cell stress & chaperones, vol. 29, no. 2, pp. 338-348

Schlagwörter: Adenosine Triphosphatases, Saccharomyces cerevisiae Proteins, Adenosine Triphosphate, Saccharomyces cerevisiae/metabolism, HSP40 Heat-Shock Proteins/metabolism, Saccharomyces cerevisiae Proteins/metabolism, Protein Binding, HSP70 Heat-Shock Proteins/metabolism, Molecular Chaperones/metabolism, Adenosine Triphosphatases/metabolism, Adenosine Triphosphate/metabolism, Autorepression, Coevolution, DNAJA, DNAJB, JDPs, HSP70 Heat-Shock Proteins, Saccharomyces cerevisiae, HSP40 Heat-Shock Proteins, Research Paper, Molecular Chaperones

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/38521349
https://serval.unil.ch/notice/serval:BIB_F1DAA741A6AE
https://serval.unil.ch/resource/serval:BIB_F1DAA741A6AE.P001/REF.pdf
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_F1DAA741A6AE7

Automated quantification of vacuole fusion and lipophagy in Saccharomyces cerevisiae from fluorescence and cryo-soft X-ray microscopy data using deep learning

Autoren: Jacob Marcus Egebjerg Maria Szomek Katja Thaysen et al.

Quelle: Autophagy
Autophagy 20 2024, p. 902 922

Schlagwörter: 0301 basic medicine, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae, tomography, Fluorescence/methods, X-ray, 03 medical and health sciences, Saccharomyces cerevisiae/metabolism, Deep Learning, Autophagy, lipophagy, Tomography, 2. Zero hunger, Microscopy, 0303 health sciences, Tomography, X-Ray, segmentation, Vacuoles/metabolism, Deep learning, Lipid Droplets, Saccharomyces cerevisiae Proteins/metabolism, 3. Good health, Data Management and Analysis, Microscopy, Fluorescence, X-Ray/methods, Lipid Droplets/metabolism, Vacuoles, Toolbox, Niemann-Pick disease

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/37908116
https://www.helmholtz-berlin.de/pubbin/oai_publication?VT=1&ID=110319

Not4-dependent targeting of MMF1 mRNA to mitochondria limits its expression via ribosome pausing, Egd1 ubiquitination, Caf130, no-go-decay and autophagy

Autoren: Chen, Siyu Allen, George Edward Panasenko, Olesya et al.

Quelle: Nucleic Acids Res

Schlagwörter: Autophagy / genetics, Saccharomyces cerevisiae Proteins, RNA, Messenger / metabolism, Ribosomes / metabolism, Saccharomyces cerevisiae, Ribosomes / genetics, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins / genetics, Autophagy, Saccharomyces cerevisiae / metabolism, RNA, Messenger, Mitochondrial Proteins / genetics, Molecular Biology, Saccharomyces cerevisiae Proteins / metabolism, Membrane Proteins / genetics, RNA, Messenger / genetics, Mitochondria / metabolism, Ubiquitination, Membrane Proteins, Mitochondria, Mitochondria / genetics, Mitochondrial Proteins / metabolism, Saccharomyces cerevisiae / genetics, Ribosomes

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/37094076
https://archive-ouverte.unige.ch/unige:172792
https://doi.org/10.1093/nar/gkad299

SMC motor proteins extrude DNA asymmetrically and can switch directions.

Autoren: Barth, R. Davidson, I.F. van der Torre, J. et al.

Quelle: Cell, vol. 188, no. 3, pp. 749-763.e21

Schlagwörter: Cell Cycle Proteins/metabolism, Chromosomal Proteins, Non-Histone/metabolism, Cohesins, DNA/metabolism, DNA/chemistry, Saccharomyces cerevisiae Proteins/metabolism, Saccharomyces cerevisiae/metabolism, DNA loop extrusion, NIPBL, SMC complexes, SMC5/6, cohesin, condensin, single molecule visualization

Dateibeschreibung: application/pdf

Relation: info:eu-repo/semantics/altIdentifier/pmid/39824185; info:eu-repo/semantics/altIdentifier/eissn/1097-4172; info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_B69B6AD180D59; https://serval.unil.ch/notice/serval:BIB_B69B6AD180D5; https://serval.unil.ch/resource/serval:BIB_B69B6AD180D5.P001/REF.pdf

Verfügbarkeit: https://serval.unil.ch/notice/serval:BIB_B69B6AD180D5
https://doi.org/10.1016/j.cell.2024.12.020
https://serval.unil.ch/resource/serval:BIB_B69B6AD180D5.P001/REF.pdf
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_B69B6AD180D59

Divergent Morphologies and Common Signaling Features of Active and Inactive Oncogenic RHOA Mutants in Yeast

Autoren: Wang, Chenwei Ohnuki, Shinsuke Savchenko, Anna et al.

Quelle: Wang, C, Ohnuki, S, Savchenko, A, Aburatani, H, Yoshida, S, Hatakeyama, R & Ohya, Y 2025, 'Divergent Morphologies and Common Signaling Features of Active and Inactive Oncogenic RHOA Mutants in Yeast', Cells, vol. 14, no. 18, 1439. https://doi.org/10.3390/cells14181439

Schlagwörter: CalMorph, RHO1, RHOA, cancer, yeast morphology, Saccharomyces cerevisiae/genetics metabolism drug effects, rhoA GTP-Binding Protein/genetics metabolism, Signal Transduction, Mutation/genetics, Saccharomyces cerevisiae Proteins/metabolism genetics, Phenotype, rho GTP-Binding Proteins/genetics metabolism

Relation: info:eu-repo/semantics/altIdentifier/pissn/2073-4409

Verfügbarkeit: https://cris.maastrichtuniversity.nl/en/publications/6ca00513-7248-4c13-bac1-ea3cb4e60926
https://doi.org/10.3390/cells14181439

Seipin governs phosphatidic acid homeostasis at the inner nuclear membrane

Autoren: Anete Romanauska Edvinas Stankunas Maya Schuldiner et al.

Quelle: Nat Commun
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Nature Communications

Schlagwörter: Saccharomyces cerevisiae Proteins, Nuclear Envelope, Science, Phosphatidic Acids, Saccharomyces cerevisiae, Biosensing Techniques, Endoplasmic Reticulum, Article, Mitochondrial Proteins, Saccharomyces cerevisiae/metabolism, 106023 Molekularbiologie, Triglycerides/metabolism, GTP-Binding Protein gamma Subunits, Homeostasis, Endoplasmic Reticulum/metabolism, Triglycerides, Nuclear Envelope/metabolism, Phosphatidic Acids/metabolism, Lipid Droplets, 106023 Molecular biology, Saccharomyces cerevisiae Proteins/metabolism, Lipid Metabolism, GTP-Binding Protein gamma Subunits/metabolism, Lipid Droplets/metabolism, Mutation

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/39622802
https://doaj.org/article/33a363b2bf4d4162a5b440976abae7c6
https://ucrisportal.univie.ac.at/de/publications/1171964c-141f-4188-867f-4aebc9bf92bf
https://doi.org/10.1038/s41467-024-54811-z

Loss of cytoplasmic actin filaments raises nuclear actin levels to drive INO80C-dependent chromosome fragmentation

Autoren: Hurst, Verena Gerhold, Christian B Tarashev, Cleo V D et al.

Weitere Verfasser: Hurst, Verena Gerhold, Christian B Tarashev, Cleo V D et al.

Quelle: Nat Commun
Nature Communications, Vol 15, Iss 1, Pp 1-22 (2024)
Nature communications, vol. 15, no. 1, pp. 9910
Nature Communications, 15 (1)

Schlagwörter: Cell Nucleus, 0301 basic medicine, Cytoplasm, 0303 health sciences, Saccharomyces cerevisiae Proteins, DNA Repair, Science, Nuclear Proteins, 610 Medicine & health, Saccharomyces cerevisiae, Article, Actins, Actin Cytoskeleton, Bleomycin, 03 medical and health sciences, Chromosomes, Fungal, 11493 Department of Quantitative Biomedicine, Saccharomyces cerevisiae Proteins/metabolism, Saccharomyces cerevisiae Proteins/genetics, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae/genetics, Actins/metabolism, Actin Cytoskeleton/metabolism, Chromosomes, Fungal/metabolism, Chromosomes, Fungal/genetics, Cell Nucleus/metabolism, Cytoplasm/metabolism

Dateibeschreibung: application/pdf; application/application/pdf; s41467_024_54141_0.pdf - application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/39548059
https://doaj.org/article/c6eea7d7981e47d3bf6b2e622889e3f4
https://serval.unil.ch/resource/serval:BIB_58530123ACF6.P001/REF.pdf
https://serval.unil.ch/notice/serval:BIB_58530123ACF6
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_58530123ACF69
http://hdl.handle.net/20.500.11850/718994

TORC2 inhibition triggers yeast chromosome fragmentation through misregulated Base Excision Repair of clustered oxidation events

Autoren: Kenji Shimada Cleo V. D. Tarashev Stephanie Bregenhorn et al.

Quelle: Nat Commun
Nature Communications, Vol 15, Iss 1, Pp 1-20 (2024)
Nature communications, vol. 15, no. 1, pp. 9908
Nature Communications

Schlagwörter: 0301 basic medicine, 0303 health sciences, Saccharomyces cerevisiae Proteins, Excision Repair, DNA Repair, Science, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins/metabolism, Saccharomyces cerevisiae Proteins/genetics, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae/drug effects, DNA Breaks, Double-Stranded/drug effects, Chromosomes, Fungal/genetics, Chromosomes, Fungal/metabolism, Oxidation-Reduction, Actins/metabolism, Replication Protein A, Article, Actins, 03 medical and health sciences, DNA Breaks, Double-Stranded, Chromosomes, Fungal

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/39548071
https://doaj.org/article/ea98c450fa2d473d92ee49d1c6d4073b
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_B602144F75158
https://serval.unil.ch/notice/serval:BIB_B602144F7515
https://serval.unil.ch/resource/serval:BIB_B602144F7515.P001/REF.pdf
https://hdl.handle.net/11250/3187565

Chapter Eighteen - The MitoLuc assay for the analysis of the mechanism of mitochondrial protein import

Autoren: Needs, Hope I Yan, Youmian Niemi, Natalie M et al.

Quelle: Needs, H I, Yan, Y, Niemi, N M & Collinson, I 2024, ' Chapter Eighteen-The MitoLuc assay for the analysis of the mechanism of mitochondrial protein import ', Methods in Enzymology, vol. 706, pp. 407-436 . https://doi.org/10.1016/bs.mie.2024.07.033

Schlagwörter: Protein Transport, Mitochondrial Proteins/metabolism, Saccharomyces cerevisiae/metabolism, Mitochondrial Membrane Transport Proteins/metabolism, Mitochondria/metabolism, Mitochondrial Precursor Protein Import Complex Proteins/metabolism, Humans, Luciferases/metabolism, Saccharomyces cerevisiae Proteins/metabolism

Dateibeschreibung: application/pdf

Zugangs-URL: https://hdl.handle.net/1983/50d80384-e9a6-41db-b19d-df170cd0253b
https://research-information.bris.ac.uk/ws/files/433201607/Needs_etal_MitoLuc_ME_2024_revised_final_accepted.pdf

Phase-separated ribosome-nascent chain complexes in genotoxic stress response

Autoren: Németh-Szatmári, Orsolya Nagy-Mikó, Bence Györkei, Ádám et al.

Quelle: RNA

Schlagwörter: Saccharomyces cerevisiae Proteins, QH426 Genetics / genetika, Phase separation, RecQ Helicases / genetics, Ribonucleoproteins / genetics, Ribosomes / metabolism, Saccharomyces cerevisiae, DNA damage response, Ribosomes / genetics, Assemblysomes, Saccharomyces cerevisiae Proteins / genetics, Saccharomyces cerevisiae / metabolism, Humans, Edetic Acid, RNA / metabolism, Saccharomyces cerevisiae Proteins / metabolism, Sgs1, QH3011 Biochemistry / biokémia, RecQ Helicases, 01.06. Biológiai tudományok, Articles, Ribonucleoproteins, Saccharomyces cerevisiae / genetics, Edetic Acid / metabolism, RNA, örökléstan, Ribosomes, BLM, DNA Damage

Dateibeschreibung: application/pdf; text

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/37460154
https://archive-ouverte.unige.ch/unige:172793
https://doi.org/10.1261/rna.079755.123

A small signaling domain controls PPIP5K phosphatase activity in phosphate homeostasis

Autoren: Pierre Raia Kitaik Lee Simon M. Bartsch et al.

Weitere Verfasser: Pierre Raia Kitaik Lee Simon M. Bartsch et al.

Quelle: Nat Commun
Nature Communications, Vol 16, Iss 1, Pp 1-20 (2025)

Schlagwörter: Models, Molecular, Phosphoric Monoester Hydrolases / chemistry, Arabidopsis, Crystallography, X-Ray, Substrate Specificity, Arabidopsis Proteins / genetics, Saccharomyces cerevisiae Proteins / genetics, Catalytic Domain, Saccharomyces cerevisiae / metabolism, Homeostasis, Phosphotransferases (Phosphate Group Acceptor) / genetics, Zinc / metabolism, Saccharomyces cerevisiae Proteins / metabolism, Saccharomyces cerevisiae / enzymology, Phosphates / metabolism, 10179 Institute of Medical Microbiology, Phosphotransferases (Phosphate Group Acceptor) / metabolism, Phosphoric Monoester Hydrolases / genetics, Arabidopsis / enzymology, Phosphotransferases (Phosphate Group Acceptor) / chemistry, Zinc, Arabidopsis / genetics, Saccharomyces cerevisiae / genetics, Enzyme mechanisms, Saccharomyces cerevisiae Proteins / chemistry, Permeation and transport, Inositol Phosphates / metabolism, Signal Transduction, ddc:500, Saccharomyces cerevisiae Proteins, Science, Inositol Phosphates, Phosphoric Monoester Hydrolases / metabolism, 610 Medicine & health, Saccharomyces cerevisiae, Article, Phosphates, 500 Naturwissenschaften und Mathematik, Protein Domains, Arabidopsis / metabolism, X-ray crystallography, Phosphotransferases (Phosphate Group Acceptor), Arabidopsis Proteins, Arabidopsis Proteins / metabolism, Phosphoric Monoester Hydrolases, Phosphates / chemistry, Plant signalling, Mutation, Arabidopsis Proteins / chemistry, 570 Life sciences, biology

Dateibeschreibung: application/pdf; ZORA275946.pdf - application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/39966396
https://doaj.org/article/5db6f334eae74ff9889eb7889ef52ca5
https://archive-ouverte.unige.ch/unige:183666
https://doi.org/10.1038/s41467-025-56937-0

Distinct TORC1 signalling branches regulate Adc17 proteasome assembly chaperone expression

Autoren: Williams, TD Joshua, I Soubigou, F et al.

Quelle: J Cell Sci

Schlagwörter: 0301 basic medicine, Proteasome Endopeptidase Complex, Saccharomyces cerevisiae Proteins, Proteasome assembly chaperone, Saccharomyces cerevisiae, name=Cell Biology, 03 medical and health sciences, Saccharomyces cerevisiae/metabolism, Cell Wall, Gene Expression Regulation, Fungal, Transcription Factors/metabolism, Cell Wall/metabolism, 0303 health sciences, Molecular Chaperones/metabolism, Actin cytoskeleton, Saccharomyces cerevisiae Proteins/metabolism, Slt2 kinase, Proteasome Endopeptidase Complex/metabolism, Fungal, Gene Expression Regulation, TORC1 signalling, Mpk1 kinase, Research Article, Molecular Chaperones, Signal Transduction, Transcription Factors

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/38949052
https://ora.ox.ac.uk/objects/uuid:3c8fbd44-218d-415f-8e75-abb5e752cb32
https://doi.org/10.1242/jcs.261892

A co-transcriptional ribosome assembly checkpoint controls nascent large ribosomal subunit maturation

Autoren: Zahra A. Sanghai Rafal Piwowarczyk Arnaud Vanden Broeck et al.

Quelle: Nat Struct Mol Biol

Schlagwörter: Ribosomal Proteins, Ribosome Subunits, Small, Eukaryotic, Ribosome Subunits, Large/metabolism, Saccharomyces cerevisiae Proteins, Cryoelectron Microscopy, Saccharomyces cerevisiae, Ribosome Subunits, Small, Eukaryotic/metabolism, Ribosome Subunits, Large, Eukaryotic, Saccharomyces cerevisiae Proteins/metabolism, Biochimie, biophysique & biologie moléculaire, Life sciences, Article, RNA, Ribosomal/metabolism, Saccharomyces cerevisiae/metabolism, RNA, Ribosomal, Sciences du vivant, Ribosomal Proteins/metabolism, Ribosome Subunits, Large, Eukaryotic/metabolism, Ribosome Subunits, Large, Biochemistry, biophysics & molecular biology

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/37037974

­­Atg9 interactions via its transmembrane domains are required for phagophore expansion during autophagy

Autoren: Sabrina Chumpen Ramirez Rubén Gómez-Sánchez Pauline Verlhac et al.

Quelle: Autophagy
Chumpen Ramirez, S, Gómez-Sánchez, R, Verlhac, P, Hardenberg, R, Margheritis, E, Cosentino, K, Reggiori, F & Ungermann, C 2023, 'Atg9 interactions via its transmembrane domains are required for phagophore expansion during autophagy', Autophagy, vol. 19, no. 5, pp. 1459-1478. https://doi.org/10.1080/15548627.2022.2136340

Schlagwörter: 0301 basic medicine, membrane contact site, Saccharomyces cerevisiae Proteins, Autophagosome, Autophagy-Related Proteins, Saccharomyces cerevisiae, Endoplasmic Reticulum, 03 medical and health sciences, Saccharomyces cerevisiae/metabolism, Autophagy, Humans, Autophagosomes/metabolism, lipid transfer, Endoplasmic Reticulum/metabolism, phagophore, Cryoelectron Microscopy, Autophagy-Related Proteins/metabolism, Autophagosomes, Membrane Proteins, Saccharomyces cerevisiae Proteins/metabolism, Lipids, scramblase, Autophagy/genetics, Membrane Proteins/metabolism, Research Paper

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/36354155
https://pure.au.dk/portal/en/publications/0a82622f-9058-4d37-931c-4c08c4289f37
http://www.scopus.com/inward/record.url?scp=85141984373&partnerID=8YFLogxK
https://doi.org/10.1080/15548627.2022.2136340
https://pure.au.dk/portal/en/publications/0a82622f-9058-4d37-931c-4c08c4289f37
https://pure.au.dk/ws/files/401873087/Atg9_interactions_via_its_transmembrane_domains_are_required_for_phagophore_expansion_during_autophagy.pdf

DNA segment capture by Smc5/6 holo-complexes

Autoren: Michael Taschner Stephan Gruber

Quelle: Nat Struct Mol Biol
Nature structural & molecular biology, vol. 30, no. 5, pp. 619-628
Nature Structural & Molecular Biology

Schlagwörter: 0301 basic medicine, 03 medical and health sciences, Saccharomyces cerevisiae Proteins, DNA Repair, Chromosomal Proteins, Non-Histone, Multiprotein Complexes, Cell Cycle Proteins, DNA, Saccharomyces cerevisiae, Article, Chromosomes, Multiprotein Complexes/genetics, DNA/chemistry, Chromosomes/metabolism, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae/metabolism, Cell Cycle Proteins/metabolism, Saccharomyces cerevisiae Proteins/genetics, Saccharomyces cerevisiae Proteins/metabolism, Chromosomal Proteins, Non-Histone/metabolism

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/37012407
https://serval.unil.ch/resource/serval:BIB_E4AD008053CC.P001/REF.pdf
https://serval.unil.ch/notice/serval:BIB_E4AD008053CC
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_E4AD008053CC3