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2006, Advances in protein chemistry, ISBN 0120342731, Volume 73., vii, 320 p., [28] p of plates
Amyloids, Prions and Beta Proteins is the last volume of the three-part thematic series on Fibrous Proteins in the Advances in Protein Chemistry serial.... 
Proteins | Amyloid | Prions | Amyloid beta-protein
Book
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 10, pp. e26319 - e26319
Bacteria, fungi, protozoa, chromista and plants all harbor homologues of Hsp104, a AAA+ ATPase that collaborates with Hsp70 and Hsp40 to promote protein... 
YEAST | IN-VITRO | CAENORHABDITIS-ELEGANS | MOLECULAR CHAPERONES | MULTIDISCIPLINARY SCIENCES | AGGREGATED PROTEINS | ALPHA-SYNUCLEIN | SACCHAROMYCES-CEREVISIAE | HUNTINGTONS-DISEASE | HEAT-SHOCK-PROTEIN | NUCLEOTIDE EXCHANGE FACTORS | Mammals - metabolism | HSP40 Heat-Shock Proteins - metabolism | Biocatalysis | Humans | Adenosine Triphosphatases - metabolism | Rats | Substrate Specificity | HSP70 Heat-Shock Proteins - metabolism | HSP110 Heat-Shock Proteins - chemistry | Hydrolysis | Saccharomyces cerevisiae - metabolism | Cytosol - enzymology | Animals | Amyloid - metabolism | Cell-Free System | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Saccharomyces cerevisiae Proteins - metabolism | Conserved Sequence | Protein Binding | HSP70 Heat-Shock Proteins - chemistry | HeLa Cells | HSP110 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - chemistry | Heat shock proteins | Prions | Cells | Adenosine triphosphatase | Yeast | Parkinson's disease | Cell-free system | Homology | Activation | Biochemistry | Kinases | Synuclein | Cytosol | Machinery | Fungi | Protein folding | Bacteria | Amyloid | Trends | Prion protein | Movement disorders | Adenosine triphosphate | Protozoa | Neurodegenerative diseases | Disaggregation | Hsp70 protein | Hsp40 protein | Mammals | Substrates | Aggregates | Hsc70 protein | Mutation | Alzheimers disease | Endoplasmic reticulum | ATP | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2015, Volume 60, Issue 2, pp. 231 - 241
Phase-separated states of proteins underlie ribonucleoprotein (RNP) granules and nuclear RNA-binding protein assemblies that may nucleate protein inclusions... 
CELL-FREE FORMATION | PROTEIN | PHOSPHORYLATION | PRION-LIKE DOMAINS | PHASE-TRANSITIONS | TDP-43 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | FUS/TLS | ARGININE METHYLATION | ALPHA-SYNUCLEIN | CELL BIOLOGY | RNA-Binding Proteins - genetics | Humans | Molecular Sequence Data | RNA Polymerase II - metabolism | Cytoplasmic Granules - chemistry | Phase Transition | RNA-Binding Protein FUS - chemistry | Molecular Mimicry | Cytoplasmic Granules - metabolism | Escherichia coli - metabolism | Binding Sites | RNA Polymerase II - chemistry | RNA - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Prions - metabolism | Gene Expression | Rheology | RNA-Binding Proteins - chemistry | RNA-Binding Protein FUS - genetics | Recombinant Proteins - chemistry | RNA-Binding Protein FUS - metabolism | Recombinant Proteins - genetics | Prions - chemistry | RNA - chemistry | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | RNA Polymerase II - genetics | RNA-Binding Proteins - metabolism | Intrinsically Disordered Proteins - metabolism | Proteins | Nervous system diseases | Sarcoma | RNA | Physiological aspects | Fluorescence | Nuclear magnetic resonance spectroscopy | Molecular biology | Fluorescence microscopy | Cells | Protein binding | Analysis | Index Medicus
Journal Article
Journal Article
Journal of Cell Biology, ISSN 0021-9525, 2017, Volume 216, Issue 8, pp. 2295 - 2304
Disturbances in endoplasmic reticulum (ER) homeostasis create a condition termed ER stress. This activates the unfolded protein response (UPR), which alters... 
YEAST | OXIDATIVE STRESS | MOLECULAR CHAPERONES | GUANIDINE-HYDROCHLORIDE | MISFOLDED PROTEIN | MEMBRANE-PROTEIN | ENDOPLASMIC-RETICULUM | QUALITY-CONTROL | SACCHAROMYCES-CEREVISIAE | TRANSMEMBRANE PROTEIN | CELL BIOLOGY | Protein Aggregates | Basic-Leucine Zipper Transcription Factors - metabolism | Molecular Chaperones - metabolism | Membrane Glycoproteins - metabolism | Saccharomyces cerevisiae - genetics | Endoplasmic Reticulum - metabolism | Prion Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Endoplasmic Reticulum - pathology | Time Factors | Proteomics - methods | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | Molecular Chaperones - genetics | Protein-Serine-Threonine Kinases - genetics | Ubiquitin-Protein Ligases - metabolism | Repressor Proteins - genetics | Genotype | Basic-Leucine Zipper Transcription Factors - genetics | Saccharomyces cerevisiae Proteins - genetics | Unfolded Protein Response | Protein Aggregation, Pathological | Membrane Glycoproteins - genetics | Phenotype | Endoplasmic Reticulum Stress | Saccharomyces cerevisiae Proteins - metabolism | Mutation | Ubiquitin-Protein Ligases - genetics | Cellular proteins | Stress (Physiology) | Analysis | Prions | Stresses | Homeostasis | Agglomeration | Chaperones | Gene expression | Stress | Proteins | Degradation | Correlation analysis | Protein folding | Quality control | Amyloid | Prion protein | Protein interaction | Endoplasmic reticulum | Index Medicus
Journal Article
2001, Advances in protein chemistry, ISBN 012034257X, Volume 57., xiii, 405 p., [3] leaves of plates
Prion Proteins is "issue-oriented" and edited by a well-known authority in the field. Topics covered include structure, diversity, and energetics as well as... 
Prions
Book
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2011, Volume 108, Issue 17, pp. 6915 - 6920
Yeast Hsp104 and its bacterial homolog, ClpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases. Hsp104 and ClpB collaborate with the Hsp70 and DnaK... 
Proteins | Yeasts | Protein refolding | Plasmids | Prions | Escherichia coli | Adenosine triphosphatases | Cell aggregates | Heat tolerance | Chimeras | GrpE | M-domain | DnaJ | Nucleotide exchange factor | Hsp40 | CLPB | MECHANISM | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | MACHINERY | AGGREGATED PROTEINS | SACCHAROMYCES-CEREVISIAE | nucleotide exchange factor | DNAK | PRION PROPAGATION | N-TERMINAL DOMAIN | CHAPERONE SYSTEM | Protein Structure, Secondary | Endopeptidase Clp | Heat-Shock Proteins - metabolism | Escherichia coli Proteins - metabolism | HSP70 Heat-Shock Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Escherichia coli - chemistry | Recombinant Fusion Proteins | Saccharomyces cerevisiae - chemistry | HSP70 Heat-Shock Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Heat-Shock Proteins - genetics | Escherichia coli - genetics | Escherichia coli - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Escherichia coli Proteins - genetics | HSP70 Heat-Shock Proteins - chemistry | Escherichia coli Proteins - chemistry | Heat-Shock Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Heat shock proteins | Physiological aspects | Genetic aspects | Yeast fungi | Adenosine triphosphatase | Temperature | Yeast | Collaboration | Amino acids | Mutation | Cells | Index Medicus | Biological Sciences
Journal Article
Molecular Cell, ISSN 1097-2765, 03/2017, Volume 65, Issue 6, pp. 1044 - 1055.e5
Liquid-liquid phase separation (LLPS) of RNA-binding proteins plays an important role in the formation of multiple membrane-less organelles involved in RNA... 
LLPS | hnRNP | intrinsically disordered protein | FUS | protein aggregation | low complexity domain | prion-like domain | phase transition | amyotrophic lateral sclerosis | frontotemporal lobar degeneration | RNA-BINDING PROTEINS | NEURODEGENERATIVE DISEASE | IN-VITRO | PRION-LIKE DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | LIQUID DROPLETS | C-TERMINAL DOMAIN | HEXANUCLEOTIDE REPEAT | GGGGCC REPEAT | NUCLEOCYTOPLASMIC TRANSPORT | CELL BIOLOGY | Phosphorylation | Humans | Poly-ADP-Ribose Binding Proteins | RNA Helicases | Transfection | Time Factors | Cytoplasmic Granules - metabolism | Eukaryotic Initiation Factor-2 - metabolism | Protein Domains | C9orf72 Protein | Dipeptides - metabolism | Lipid Droplets - metabolism | RNA Recognition Motif Proteins | RNA - metabolism | Cytoplasmic Granules - pathology | Amyotrophic Lateral Sclerosis - genetics | Dipeptides - chemistry | Arginine - chemistry | Carrier Proteins - genetics | Amyotrophic Lateral Sclerosis - pathology | DNA Helicases | Carrier Proteins - metabolism | Proteins - metabolism | Intrinsically Disordered Proteins - chemistry | Eukaryotic Initiation Factor-2 - genetics | Amyotrophic Lateral Sclerosis - metabolism | HeLa Cells | Proteins - chemistry | Arginine - metabolism | Intrinsically Disordered Proteins - metabolism | Physiological aspects | Amino acids | Neurosciences | RNA | Binding proteins | Protein binding | Arginine | Glutamine | Index Medicus
Journal Article
2011, Topics in current chemistry, ISBN 3642240666, Volume 305.
Web Resource
Journal of Biological Chemistry, ISSN 0021-9258, 01/2013, Volume 288, Issue 3, pp. 1856 - 1870
Journal Article
Cell, ISSN 0092-8674, 09/2017, Volume 171, Issue 1, pp. 163 - 178.e19
Journal Article
1999, Methods in enzymology ; 309., ISBN 0121822109, Volume 309, xix, 820 p. : ill. ; 24 cm.
This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology... 
Amyloid | Protein folding | Prions | Cell aggregation | Proteins | Amyloid beta-protein
Book
Nature Communications, ISSN 2041-1723, 04/2015, Volume 6, Issue 1, pp. 6768 - 6768