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1. Full Text Liquid phase condensation in cell physiology and disease
by Shin, Yongdae and Brangwynne, Clifford P
Science (American Association for the Advancement of Science), ISSN 0036-8075, 09/2017, Volume 357, Issue 6357, p. eaaf4382
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Caenorhabditis elegans | Animals | Cell Physiological Phenomena | Phase Transition | Intranuclear Inclusion Bodies - metabolism | Intranuclear Inclusion Bodies - ultrastructure | Protein Aggregation, Pathological - metabolism | Transcription | Disease | Liquid phases | Agglomeration | Genomes | Biology | Condensation | Nuclei | Phase transitions | Proteins | Nucleoli | Secretory vesicles | Control | Condensates | Compartments | Biomolecules | Droplets | Assemblies | Adenosine triphosphate | Cajal bodies | Liquids | Molecular interactions | Ribonucleic acid--RNA | Organelles | Equilibrium | Disease control | Biological activity | Coalescing | Regulatory mechanisms (biology) | Cells (biology) | Intracellular | Protein interaction | ATP | Endoplasmic reticulum | Physicochemical properties | Cytoplasm | Nuclear reactions | Index Medicus
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2. Full Text Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
by Bernardi, Rosa and Pandolfi, Pier Paolo
Nature reviews. Molecular cell biology, ISSN 1471-0072, 12/2007, Volume 8, Issue 12, pp. 1006 - 1016
Life Sciences & Biomedicine | Science & Technology | Cell Biology | Transcription Factors - metabolism | Cell Nucleus Structures - chemistry | Intranuclear Inclusion Bodies - chemistry | Tumor Suppressor Proteins - metabolism | Animals | Cell Nucleus Structures - physiology | Humans | Nuclear Proteins - metabolism | Intranuclear Inclusion Bodies - physiology | Neoplasm Proteins - metabolism | Promyelocytic Leukemia Protein | Physiological aspects | Cellular proteins | Tumor suppressor genes | Genetic aspects | Research | Chronic myeloid leukemia | Index Medicus
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3. Full Text Nuclear inclusion bodies of mutant and wild-type p53 in cancer: a hallmark of p53 inactivation and proteostasis remodelling by p53 aggregation
by De Smet, Frederik and Rubio, Mirian Saiz and Hompes, Daphne and Naus, Evelyne and De Baets, Greet and Langenberg, Tobias and Hipp, Mark S and Houben, Bert and Claes, Filip and Charbonneau, Sarah and Blanco, Javier Delgado and Plaisance, Stephane and Ramkissoon, Shakti and Ramkissoon, Lori and Simons, Colinda and van den Brandt, Piet and Weijenberg, Matty and Van Engeland, Manon and Lambrechts, Sanina and Amant, Frederic and D'Hoore, Ane and Ligon, Keith L and Sagaert, Xavier and Schymkowitz, Joost and Rousseau, Frederic
The Journal of pathology, ISSN 0022-3417, 05/2017, Volume 242, Issue 1, pp. 24 - 38
nuclear inclusion bodies | UBIQUITIN-PROTEASOME SYSTEM | PROTEIN AGGREGATION | colon cancer | proteostasis | NEURODEGENERATIVE DISEASES | PML | CELLULAR-MODEL | p53 aggregation | glioblastoma | HEAT-SHOCK RESPONSE | A-BETA | MDM2 | HUNTINGTONS-DISEASE | GAIN | Pathology | Oncology | Life Sciences & Biomedicine | Science & Technology | Proteostasis Deficiencies - metabolism | Colonic Neoplasms - genetics | Proteostasis Deficiencies - etiology | Humans | Cytoplasm - metabolism | Colonic Neoplasms - metabolism | Tumor Suppressor Protein p53 - genetics | Glioblastoma - genetics | Glioblastoma - metabolism | Receptors, sigma - metabolism | Protein Aggregation, Pathological - genetics | Protein Aggregation, Pathological - etiology | Kaplan-Meier Estimate | Tumor Suppressor Protein p53 - metabolism | Heat-Shock Response - physiology | Colonic Neoplasms - complications | Heat-Shock Response - genetics | Proteostasis Deficiencies - genetics | Biopsy | Colonic Neoplasms - pathology | Glioblastoma - pathology | Glioblastoma - complications | Cell Line, Tumor | Mutation | Intranuclear Inclusion Bodies - metabolism | Protein Aggregation, Pathological - metabolism | Index Medicus
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4. Full Text JC Virus Inclusions in Progressive Multifocal Leukoencephalopathy: Scaffolding Promyelocytic Leukemia Nuclear Bodies Grow With Cell Cycle Transition Through an S-to-G2–Like State in Enlarging Oligodendrocyte Nuclei
by Shishido-Hara, Yukiko and Yazawa, Takuya and Nagane, Motoo and Higuchi, Kayoko and Abe-Suzuki, Shiho and Kurata, Morito and Kitagawa, Masanobu and Kamma, Hiroshi and Uchihara, Toshiki
Journal of neuropathology and experimental neurology, ISSN 0022-3069, 05/2014, Volume 73, Issue 5, pp. 442 - 453
Intranuclear viral inclusions | Cell stress | JC virus | PML-NBs | Cell cycle | Progressive multifocal leukoencephalopathy | Intranuclear Inclusion Bodies - virology | G2 Phase - physiology | Humans | JC Virus - ultrastructure | Leukoencephalopathy, Progressive Multifocal - virology | Oligodendroglia - virology | Cell Nucleus - ultrastructure | Oligodendroglia - ultrastructure | Intranuclear Inclusion Bodies - pathology | Oligodendroglia - pathology | Cell Nucleus - pathology | Cell Nucleus - virology | Cell Cycle - physiology | S Phase - physiology | Female | Aged | Leukoencephalopathy, Progressive Multifocal - pathology | Intranuclear Inclusion Bodies - ultrastructure | Index Medicus | Original
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5. Full Text Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1
by Dellaire, Graham and Eskiw, Christopher H and Dehghani, Hesam and Ching, Reagan W and Bazett-Jones, David P
Journal of cell science, ISSN 0021-9533, 03/2006, Volume 119, Issue 6, pp. 1034 - 1042
Electron spectroscopic imaging | Mitosis | Nuclear bodies | Proteasome inhibition | PML | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Transcription Factors - physiology | Humans | Neoplasm Proteins - physiology | Antigens, Nuclear - physiology | SUMO-1 Protein - physiology | Intranuclear Inclusion Bodies - physiology | G1 Phase - physiology | Autoantigens - physiology | Tumor Suppressor Proteins - physiology | Mitosis - physiology | Nuclear Matrix - physiology | Chromatin - physiology | Nuclear Matrix - ultrastructure | Nuclear Proteins - physiology | HeLa Cells | Intranuclear Inclusion Bodies - ultrastructure | Promyelocytic Leukemia Protein | Index Medicus
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6. Full Text Emerging role of PML nuclear bodies in innate immune signaling
by Scherer, Myriam and Stamminger, Thomas
Journal of virology, ISSN 0022-538X, 2016, Volume 90, Issue 13, pp. 5850 - 5854
Life Sciences & Biomedicine | Science & Technology | Virology | Virus Diseases - immunology | Signal Transduction | Humans | Immunity, Innate | Viral Proteins - metabolism | Animals | Virus Replication | Gene Expression Regulation, Viral | Promyelocytic Leukemia Protein - metabolism | Mice | Virus Physiological Phenomena | Cytomegalovirus - physiology | Intranuclear Inclusion Bodies - metabolism | Index Medicus
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7. Full Text Metabotropic glutamate receptor 5 knockout promotes motor and biochemical alterations in a mouse model of Huntington's disease
by Ribeiro, Fabiola M and DeVries, Rebecca A and Hamilton, Alison and Guimaraes, Isabella M and Cregan, Sean P and Pires, Rita G.W and Ferguson, Stephen S.G
Human molecular genetics, ISSN 0964-6906, 04/2014, Volume 23, Issue 8, pp. 2030 - 2042
Biochemistry & Molecular Biology | Genetics & Heredity | Life Sciences & Biomedicine | Science & Technology | Motor Activity - physiology | Cell Proliferation | Huntington Disease - pathology | Motor Activity - drug effects | Gene Expression Profiling | Immunoenzyme Techniques | Receptor, Metabotropic Glutamate 5 - physiology | Real-Time Polymerase Chain Reaction | Disease Models, Animal | Serotonin Plasma Membrane Transport Proteins - physiology | RNA, Messenger - genetics | Cells, Cultured | Intranuclear Inclusion Bodies - genetics | Receptor, Metabotropic Glutamate 5 - antagonists & inhibitors | Reverse Transcriptase Polymerase Chain Reaction | Huntington Disease - metabolism | Blotting, Western | Intranuclear Inclusion Bodies - pathology | Mice, Knockout | Animals | Huntington Disease - genetics | Mice | Pyridines - pharmacology | Thiazoles - pharmacology | Intranuclear Inclusion Bodies - metabolism | Index Medicus
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8. Full Text Sigma-1 receptor is involved in degradation of intranuclear inclusions in a cellular model of Huntington's disease
by Miki, Yasuo and Tanji, Kunikazu and Mori, Fumiaki and Wakabayashi, Koichi
Neurobiology of disease, ISSN 0969-9961, 2014, Volume 74, pp. 25 - 31
Neurology | Neuronal nuclear inclusions | Endoplasmic reticulum-associated degradation | Endoplasmic reticulum chaperone | Huntington's disease | Sigma-1 receptor | Ubiquitin–proteasome system | Ubiquitin-proteasome system | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Immunohistochemistry | Humans | Endoplasmic Reticulum - metabolism | Cytoplasm - metabolism | Receptors, sigma - antagonists & inhibitors | Cell Nucleus - metabolism | Transfection | Endoplasmic Reticulum - drug effects | Membrane Transport Modulators - pharmacology | Receptors, sigma - metabolism | Cell Survival - physiology | Cell Survival - drug effects | Enzyme Inhibitors - pharmacology | Fatty Acids, Unsaturated - pharmacology | Receptors, sigma - agonists | Receptors, sigma - genetics | Huntington Disease - metabolism | Nerve Tissue Proteins - genetics | Blotting, Western | Nerve Tissue Proteins - metabolism | Huntingtin Protein | Karyopherins - metabolism | Intranuclear Inclusion Bodies - drug effects | Receptors, Cytoplasmic and Nuclear - antagonists & inhibitors | RNA, Small Interfering | HeLa Cells | Mutation | Cell Nucleus - drug effects | Oligopeptides - pharmacology | Cytoplasm - drug effects | Karyopherins - antagonists & inhibitors | Intranuclear Inclusion Bodies - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism | Ubiquitin | Analysis | Index Medicus
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