نتائج البحث - "chemistry [Saccharomyces cerevisiae Proteins]"

1

Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2

المؤلفون: Andreas Schmitt, ShengQi Xiang, Henning Urlaub, Romina V. Hofele, Markus Zweckstetter, Filippo Favretto, Piotr Neumann, Florian Hamann, Ralf Ficner

المصدر: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America 117(6), 2948-2956 (2020). doi:10.1073/pnas.1907960117

وصف الملف: application/pdf; application/xhtml+xml

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25489a886498558306d0df62dea4e879Test
http://europepmc.org/articles/PMC7022188Test

2

Mammalian amyloidogenic proteins promote prion nucleation in yeast

المؤلفون: Ina Vorberg, Pavithra Chandramowlishwaran, Meng Sun, Carmen Nussbaum-Krammer, Anastasiya V Grizel, Yury O. Chernoff, Kristin L Casey, Aleksandr A. Rubel, Andrey V. Romanyuk, Julia V. Sopova

المصدر: The journal of biological chemistry 293(9), 3436-3450 (2018). doi:10.1074/jbc.M117.809004

مصطلحات موضوعية: 0301 basic medicine, Amyloid, Saccharomyces cerevisiae Proteins, animal diseases, Protein domain, Nucleation, metabolism [Amyloid beta-Peptides], Protein aggregation, metabolism [Peptide Termination Factors], Biochemistry, Protein Aggregates, 03 medical and health sciences, Amyloid disease, Protein Domains, Humans, metabolism [Peptide Fragments], Molecular Biology, metabolism [Amyloid], Amyloid beta-Peptides, Chemistry, Molecular Bases of Disease, chemistry [Saccharomyces cerevisiae Proteins], amyloid beta-protein (1-40), Cell Biology, metabolism [Saccharomyces cerevisiae Proteins], amyloid beta-protein (1-42), chemistry [Peptide Termination Factors], Peptide Fragments, Yeast, nervous system diseases, Cell biology, 030104 developmental biology, ddc:540, Proteome, Protein folding, SUP35 protein, S cerevisiae, Peptide Termination Factors

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ff3d4fc9f56554126697b81a6eddca8Test
https://doi.org/10.1074/jbc.m117.809004Test

3

Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells

المؤلفون: Shu Liu, Yvonne Duernberger, Katrin Riemschoss, Benedetta Bolognesi, Annika Hornberger, Oleksandra Buravlova, Stephan A. Müller, Lydia Paulsen, Ina Vorberg, Philipp von Eisenhart-Rothe, Stefan F. Lichtenthaler, André Hossinger, Gian Gaetano Tartaglia, Verena Arndt, Sebastian Hogl, Nieves Lorenzo-Gotor

المصدر: Life Science Alliance
Recercat. Dipósit de la Recerca de Catalunya
instname
Life science alliance 2(4), e201800280 (2019). doi:10.26508/lsa.201800280

مصطلحات موضوعية: metabolism [Cytoskeleton], Health, Toxicology and Mutagenesis, Glutamine, animal diseases, Plant Science, Protein aggregation, metabolism [Peptide Termination Factors], Mice, 0302 clinical medicine, Asparagine, Cytoskeleton, Research Articles, 0303 health sciences, Ecology, biology, Chemistry, food and beverages, RNA-Binding Proteins, chemistry [Saccharomyces cerevisiae Proteins], Animals, Cell Line, Tumor, Cytoplasmic Granules, DNA-Binding Proteins, Gene Ontology, Peptide Termination Factors, Prions, Protein Domains, Proteolysis, Saccharomyces cerevisiae Proteins, chemistry [Peptide Termination Factors], Cell biology, ddc, Protein folding, metabolism [DNA-Binding Proteins], Research Article, Saccharomyces cerevisiae, metabolism [RNA-Binding Proteins], Fibril, Biochemistry, Genetics and Molecular Biology (miscellaneous), 03 medical and health sciences, Stress granule, ddc:570, 030304 developmental biology, fungi, Colocalization, chemistry [Prions], metabolism [Saccharomyces cerevisiae Proteins], biology.organism_classification, metabolism [Cytoplasmic Granules], Cytosol, metabolism [Prions], SUP35 protein, S cerevisiae, 030217 neurology & neurosurgery

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::519833838ae0f8065a48060f79452133Test
http://hdl.handle.net/10230/42509Test

4

Retention and splicing complex (RES) – the importance of cooperativity

المؤلفون: Markus Zweckstetter, Piotr Wysoczanski

المصدر: RNA Biology
RNA biology 13(2), 128-133 (2015). doi:10.1080/15476286.2015.1096484

مصطلحات موضوعية: 0301 basic medicine, Protein Folding, Cooperativity, Plasma protein binding, genetics [Carrier Proteins], Pml1 protein, S cerevisiae, RNA Precursors, Genetics, genetics [Spliceosomes], chemistry [Ribonucleoprotein, U2 Small Nuclear], genetics [Amino Acid Sequence], chemistry [Carrier Proteins], chemistry [Saccharomyces cerevisiae Proteins], Molecular machine, RES complex, RNA splicing, genetics [RNA Precursors], genetics [RNA Splicing], genetics [Saccharomyces cerevisiae], Protein folding, IST3 protein, S cerevisiae, Protein Binding, Spliceosome, NMR spectroscopy, spliceosome, structure, Saccharomyces cerevisiae Proteins, Macromolecular Substances, RNA Splicing, Saccharomyces cerevisiae, Biology, Biophysical Phenomena, 03 medical and health sciences, Splicing factor, ddc:570, Amino Acid Sequence, genetics [Saccharomyces cerevisiae Proteins], Molecular Biology, Point of View, Binding Sites, chemistry [Macromolecular Substances], Cell Biology, Ribonucleoprotein, U2 Small Nuclear, Bud13 protein, S cerevisiae, Protein Structure, Tertiary, 030104 developmental biology, genetics [Ribonucleoprotein, U2 Small Nuclear], Biophysics, Spliceosomes, Protein Multimerization, Carrier Proteins

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7375670f58e51a40f22f5a13089e342bTest
http://europepmc.org/articles/PMC4829318Test

5

The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation

المؤلفون: Judith Gunzelmann, Elmar Schiebel, Diana Rüthnick, Annett Neuner, Wanlu Zhang, Tien-chen Lin, Ursula Jäkle

المصدر: eLife, Vol 7 (2018)
eLife 7, e39932 (2018). doi:10.7554/eLife.39932

مصطلحات موضوعية: 0301 basic medicine, TOG domain protein, Saccharomyces cerevisiae Proteins, QH301-705.5, metabolism [Microtubules], microtubule nucleation, Science, Nucleation, Microtubules, General Biochemistry, Genetics and Molecular Biology, Spindle pole body, chemistry [Microtubule-Associated Proteins], 03 medical and health sciences, Protein Domains, Microtubule, Tubulin, metabolism [Mutant Proteins], Biology (General), Receptor, Cytoplasmic microtubule, Polymerase, Stu2, Microtubule nucleation, γ-TuSC, General Immunology and Microbiology, biology, Chemistry, Protein Stability, General Neuroscience, General Medicine, metabolism [Microtubule-Associated Proteins], chemistry [Saccharomyces cerevisiae Proteins], metabolism [Tubulin], metabolism [Saccharomyces cerevisiae Proteins], 030104 developmental biology, STU2 protein, S cerevisiae, Cytoplasm, biology.protein, Biophysics, Medicine, Mutant Proteins, Protein Multimerization, ddc:600, Microtubule-Associated Proteins, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2710c9e0f0a80ae68016b45784b09e0Test
https://pubmed.ncbi.nlm.nih.gov/30222109Test

6

RNA polymerase II clustering through carboxy-terminal domain phase separation

المؤلفون: Anders S. Hansen, Marc Boehning, Xavier Darzacq, Claire Dugast-Darzacq, Markus Zweckstetter, Marija Rankovic, Hervé Marie-Nelly, Taekyung Yu, Goran Kokic, David T. McSwiggen, Patrick Cramer, Gina M. Dailey

المصدر: Nature structural & molecular biology 25(9), 833-840 (2018). doi:10.1038/s41594-018-0112-y
Nature Structural & Molecular Biology
Nature Structural and Molecular Biology

مصطلحات موضوعية: 0301 basic medicine, Repetitive Sequences, Amino Acid, Saccharomyces cerevisiae Proteins, viruses, RNA polymerase II, Saccharomyces cerevisiae, chemistry [RNA Polymerase II], environment and public health, cyclin-dependent kinase-activating kinase, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Structural Biology, Transcription (biology), RNA polymerase, ddc:570, Humans, Amino Acid Sequence, Phosphorylation, Molecular Biology, Gene, biology, fungi, enzymology [Saccharomyces cerevisiae], chemistry [Saccharomyces cerevisiae Proteins], metabolism [Saccharomyces cerevisiae Proteins], Yeast, Cyclin-Dependent Kinases, Cell biology, Chromatin, enzymes and coenzymes (carbohydrates), 030104 developmental biology, chemistry, metabolism [Cyclin-Dependent Kinases], health occupations, biology.protein, metabolism [RNA Polymerase II], CTD, RNA Polymerase II, Cyclin-Dependent Kinase-Activating Kinase, 030217 neurology & neurosurgery