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1. Full Text Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines
by Sipe, Jean D and Benson, Merrill D and Buxbaum, Joel N and Ikeda, Shu-ichi and Merlini, Giampaolo and Saraiva, Maria J. M and Westermark, Per and Medicinska fakulteten and Medicinska och farmaceutiska vetenskapsområdet and Institutionen för immunologi, genetik och patologi and Uppsala universitet and Klinisk och experimentell patologi
Amyloid, ISSN 1350-6129, 10/2016, Volume 23, Issue 4, pp. 209 - 213
The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XVth Symposium of the Society, 3 July-7 July 2016, Uppsala, Sweden,... 
inclusion body | nomenclature | amyloidosis | Amyloid fibril | amyloid protein | MEDICINE, RESEARCH & EXPERIMENTAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSTHYRETIN AMYLOIDOSIS | MEDICINE, GENERAL & INTERNAL | TRANSMISSION | SEMEN | DISEASE | SENILE SYSTEMIC AMYLOIDOSIS | Staining and Labeling - methods | Prealbumin - genetics | Guidelines as Topic | Apolipoprotein C-III - chemistry | Protein Precursors - chemistry | Humans | Apolipoprotein C-III - metabolism | tau Proteins - metabolism | Amyloidosis - diagnosis | Amyloidogenic Proteins - chemistry | Apolipoprotein C-III - genetics | Apolipoprotein C-II - genetics | tau Proteins - chemistry | Sequence Analysis, Protein | tau Proteins - genetics | Amyloidosis - genetics | Amyloidosis - classification | Prealbumin - chemistry | alpha-Synuclein - genetics | Apolipoprotein C-II - chemistry | Amyloidogenic Proteins - genetics | Biomarkers - metabolism | Gene Expression | Protein Precursors - genetics | Amyloidosis - pathology | Terminology as Topic | Protein Precursors - metabolism | alpha-Synuclein - chemistry | Amyloidogenic Proteins - metabolism | Prealbumin - metabolism | Apolipoprotein C-II - metabolism | Birefringence | Congo Red - chemistry | alpha-Synuclein - metabolism | Coloring Agents - chemistry | Index Medicus | Basic Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | Medicinska och farmaceutiska grundvetenskaper | Cell and Molecular Biology | Cell- och molekylärbiologi
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2. Full Text ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain
by Conicella, Alexander E and Zerze, Gül H and Mittal, Jeetain and Fawzi, Nicolas L
Structure, ISSN 0969-2126, 09/2016, Volume 24, Issue 9, pp. 1537 - 1549
RNA-binding protein TDP-43 mediates essential RNA processing but forms cytoplasmic neuronal inclusions via its C-terminal domain (CTD) in amyotrophic lateral... 
PROTEIN SECONDARY STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIQUID DROPLETS | DISORDERED PROTEINS | AMYLOIDOGENIC CORE REGION | DNA-BINDING PROTEIN | CELL BIOLOGY | IN-VITRO | BIOPHYSICS | SEQUENCE | RNA RECOGNITION | STRESS GRANULES | AGGREGATION | Protein Aggregates | Humans | Cytoplasmic Granules - chemistry | DNA-Binding Proteins - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Protein Domains | Binding Sites | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Amyotrophic Lateral Sclerosis - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Molecular Dynamics Simulation | Amino Acid Motifs | Amyotrophic Lateral Sclerosis - pathology | Cytoplasmic Granules - ultrastructure | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Kinetics | Mutation | Index Medicus
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3. Full Text Phosphorylation-Mediated Clearance of Amyloid-like Assemblies in Meiosis
by Carpenter, Kayla and Bell, Rachel Brietta and Yunus, Julius and Amon, Angelika and Berchowitz, Luke Edwin
Developmental Cell, ISSN 1534-5807, 05/2018, Volume 45, Issue 3, pp. 392 - 405.e6
Amyloids are fibrous protein assemblies that are often described as irreversible and intrinsically pathogenic. However, yeast cells employ amyloid-like... 
meiosis | gametogenesis | translation | neurodegeneration | amyloid-like assemblies | RNA-binding proteins | phosphorylation | RNA-BINDING PROTEINS | YEAST | CELL-FREE FORMATION | PROTEASOME | DEVELOPMENTAL BIOLOGY | AMYOTROPHIC-LATERAL-SCLEROSIS | CHROMOSOME SEGREGATION | STRESS | SACCHAROMYCES-CEREVISIAE | GRANULES | TRANSLATIONAL CONTROL | CELL BIOLOGY | Protein Aggregates | Meiosis - physiology | RNA-Binding Proteins - genetics | Phosphorylation | Protein-Serine-Threonine Kinases - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - metabolism | Amyloidogenic Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | RNA-Binding Proteins - metabolism | Amyloidogenic Proteins - genetics | RNA | Binding proteins | Protein kinases | Analysis | Protein binding | Index Medicus
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4. Full Text Polyglutamine-rich suppressors of huntingtin toxicity act upstream of Hsp70 and Sti1 in spatial quality control of amyloid-like proteins
by Wolfe, Katie J and Ren, Hong Yu and Trepte, Philipp and Cyr, Douglas M
PLoS ONE, ISSN 1932-6203, 05/2014, Volume 9, Issue 5, pp. e95914 - e95914
Protein conformational maladies such as Huntington Disease are characterized by accumulation of intracellular and extracellular protein inclusions containing... 
NEURONAL INTRANUCLEAR INCLUSIONS | EXPANDED POLYGLUTAMINE | UBIQUITIN-PROTEASOME SYSTEM | EXPANSION PROTEINS | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | MUTANT HUNTINGTIN | CASPASE CLEAVAGE | BODY FORMATION | SACCHAROMYCES-CEREVISIAE | TRANSCRIPTION FACTOR | Protein Aggregates | RNA-Binding Proteins - genetics | Ribonucleases - genetics | Saccharomyces cerevisiae - genetics | Humans | Huntington Disease - pathology | Molecular Sequence Data | Amyloidogenic Proteins - chemistry | Intracellular Signaling Peptides and Proteins - metabolism | Ribonucleases - metabolism | Saccharomyces cerevisiae - metabolism | Heat-Shock Proteins - genetics | Nerve Tissue Proteins - chemistry | Peptides - metabolism | Nuclear Proteins - deficiency | Nuclear Proteins - genetics | Transgenes | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Amyloidogenic Proteins - genetics | Gene Expression Regulation, Fungal | Protein Structure, Tertiary | Amino Acid Sequence | Peptides - chemistry | Signal Transduction | Heat-Shock Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | HSP70 Heat-Shock Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nuclear Localization Signals | Huntington Disease - metabolism | Nerve Tissue Proteins - genetics | HSP70 Heat-Shock Proteins - metabolism | Protein Interaction Mapping | Nerve Tissue Proteins - metabolism | Huntingtin Protein | Amyloidogenic Proteins - metabolism | Models, Biological | Plasmids | Saccharomyces cerevisiae Proteins - metabolism | Huntington Disease - genetics | Protein Binding | Proteins | Proline | Heat shock proteins | Huntington's chorea | Quality control | Transcription factors | Disease | Huntingtin | Toxicity | Spatial discrimination | Cytotoxicity | Biology | Agglomeration | Defense mechanisms | Nuclei | Cell cycle | Physiology | Localization | RNA processing | Trinucleotide repeat diseases | Polyglutamine | Benign | Hsp70 protein | Gene expression | Disease control | Suppressors | Intermediates | Ribonucleic acids | Prions | Intracellular | Protein interaction | Cytoplasm | Index Medicus
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5. Full Text The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins
by Wolfe, Katie J and Rena, Hong Yu and Trepte, Philipp and Cyr, Douglas M
Molecular Biology of the Cell, ISSN 1059-1524, 12/2013, Volume 24, Issue 23, pp. 3588 - 3602
Conformational diseases are associated with the conversion of normal proteins into aggregation-prone toxic conformers with structures similar to that of... 
CO-CHAPERONES | ATPASE ACTIVITY | MOLECULAR CHAPERONES | PSI+ PRION | IN-VIVO | YEAST PRIONS | GUANIDINE-HYDROCHLORIDE | MISFOLDED PROTEINS | SACCHAROMYCES-CEREVISIAE | PRION TOXICITY | CELL BIOLOGY | Green Fluorescent Proteins - metabolism | HSP40 Heat-Shock Proteins - metabolism | Molecular Weight | Heat-Shock Proteins - metabolism | Humans | Cytosol - drug effects | Mutant Proteins - metabolism | Amyloidogenic Proteins - toxicity | HSP70 Heat-Shock Proteins - metabolism | Prions - toxicity | Nerve Tissue Proteins - toxicity | Cell Nucleus - metabolism | Chemical Fractionation | Models, Biological | Protein Binding - drug effects | Saccharomyces cerevisiae Proteins - metabolism | HSP90 Heat-Shock Proteins - metabolism | Cytosol - metabolism | Cell Nucleus - drug effects | Saccharomyces cerevisiae Proteins - toxicity | Index Medicus
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6. Full Text Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles
by Hennig, Sven and Kong, Geraldine and Mannen, Taro and Sadowska, Agata and Kobelke, Simon and Blythe, Amanda and Knott, Gavin J and Iyer, K Swaminathan and Ho, Diwei and Newcombe, Estella A and Hosoki, Kana and Goshima, Naoki and Kawaguchi, Tetsuya and Hatters, Danny and Trinkle-Mulcahy, Laura and Hirose, Tetsuro and Bond, Charles S and Fox, Archa H
Journal of Cell Biology, ISSN 0021-9525, 08/2015, Volume 210, Issue 4, pp. 529 - 39
Prion-like domains (PLDs) are low complexity sequences found in RNA binding proteins associated with the neurodegenerative disorder amyotrophic lateral... 
NONCODING RNA | CELL-FREE FORMATION | NUCLEAR-BODIES | COMPLEXES | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | MUTATIONS | IDENTIFICATION | GRANULES | EXPRESSION | CELL BIOLOGY | Prions - metabolism | Humans | RNA-Binding Proteins - chemistry | Amyloidogenic Proteins - chemistry | Prions - chemistry | Protein Interaction Maps | Cell Nucleus - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Protein Binding | HeLa Cells | Intracellular Signaling Peptides and Proteins - physiology | Hydrogels - chemistry | RNA-Binding Proteins - metabolism | RNA | Binding proteins | Prions | Analysis | Protein binding | RNA-protein interactions | Neurodegeneration | Neurobiology | Amyotrophic lateral sclerosis | Phase transitions | Binding sites | Index Medicus
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7. Full Text A hydrophobic low-complexity region regulates aggregation of the yeast pyruvate kinase Cdc19 into amyloid-like aggregates in vitro
by Grignaschi, Erica and Cereghetti, Gea and Grigolato, Fulvio and Kopp, Marie R. G and Caimi, Stefano and Faltova, Lenka and Saad, Shady and Peter, Matthias and Arosio, Paolo
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 29, pp. 11424 - 11432
Cells form stress granules (SGs) upon stress stimuli to protect sensitive proteins and RNA from degradation. In the yeast Saccharomyces cerevisiae, specific... 
protein-nucleic acid interaction | FIBRIL FORMATION | DOMAIN | RNA | MECHANISM | stress granule | cell compartmentalization | amyloidogenic protein | PHASE-TRANSITIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | functional amyloids | protein self-assembly | GRANULES | hydrophobic-hydrophilic interface | INSULIN | protein aggregation | LAG PHASE | KINETICS | PROTEIN-MISFOLDING DISEASES | protein-protein interaction | A42 | Protein Aggregates | Saccharomyces cerevisiae Proteins - ultrastructure | Peptide Fragments - metabolism | Pyruvate Kinase - metabolism | Humans | Cell Cycle Proteins - metabolism | Pyruvate Kinase - chemistry | Cell Cycle Proteins - ultrastructure | Saccharomyces cerevisiae - ultrastructure | Amyloid - chemistry | Amyloid - ultrastructure | Saccharomyces cerevisiae - chemistry | Cell Cycle Proteins - chemistry | Saccharomyces cerevisiae - metabolism | Insulin - metabolism | Amyloid - metabolism | Pyruvate Kinase - ultrastructure | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Protein Structure, Quaternary | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus | Aβ42 | Molecular Biophysics
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8. Full Text Amyloidogenic Oligomerization Transforms Drosophila Orb2 from a Translation Repressor to an Activator
by Khan, Mohammed Repon and Li, Liying and Pérez-Sánchez, Consuelo and Saraf, Anita and Florens, Laurence and Slaughter, Brian D and Unruh, Jay R and Si, Kausik
Cell, ISSN 0092-8674, 12/2015, Volume 163, Issue 6, pp. 1468 - 1483
Memories are thought to be formed in response to transient experiences, in part through changes in local protein synthesis at synapses. In , the amyloidogenic... 
IN-VITRO | LONG-TERM-MEMORY | MESSENGER-RNA | NEURONAL ISOFORM | PERSISTENCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | POLYADENYLATION | APLYSIA CPEB | PRION | SYNAPTIC PLASTICITY | PROTEIN-SYNTHESIS | CELL BIOLOGY | Protein Structure, Tertiary | Protein Biosynthesis | Transcription Factors - chemistry | Memory, Long-Term | mRNA Cleavage and Polyadenylation Factors - metabolism | mRNA Cleavage and Polyadenylation Factors - chemistry | Amyloidogenic Proteins - chemistry | Drosophila Proteins - chemistry | Drosophila Proteins - metabolism | Drosophila melanogaster - metabolism | Transcription Factors - metabolism | Amyloidogenic Proteins - metabolism | Animals | Polyadenylation | Serine Endopeptidases - genetics | Mice | Drosophila Proteins - genetics | 3' Untranslated Regions | RNA-Binding Proteins - metabolism | Oligomers | RNA | Analysis | Drosophila | Protein biosynthesis | Genetic translation | Protein binding | Index Medicus
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9. Full Text Regulated Formation of an Amyloid-like Translational Repressor Governs Gametogenesis
by Berchowitz, Luke E and Kabachinski, Greg and Walker, Margaret R and Carlile, Thomas M and Gilbert, Wendy V and Schwartz, Thomas U and Amon, Angelika
Cell, ISSN 0092-8674, 10/2015, Volume 163, Issue 2, pp. 406 - 418
Message-specific translational control is required for gametogenesis. In yeast, the RNA-binding protein Rim4 mediates translational repression of numerous... 
RNA-BINDING PROTEINS | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEIOSIS | DISEASE | AGGREGATES IN-VITRO | PRION | SACCHAROMYCES-CEREVISIAE | GRANULES | DOMAINS | OLIGOMERS | CELL BIOLOGY | Protein Biosynthesis | Gametogenesis | Mice, Inbred C57BL | RNA-Binding Proteins - chemistry | Gene Expression Regulation | Male | Amyloidogenic Proteins - chemistry | Meiosis | Saccharomyces cerevisiae Proteins - genetics | Amyloidogenic Proteins - metabolism | Animals | Cyclin B - genetics | Sodium Dodecyl Sulfate - pharmacology | Saccharomyces cerevisiae Proteins - metabolism | Mice | Saccharomyces cerevisiae | RNA-Binding Proteins - metabolism | Protein Aggregates - drug effects | Saccharomyces cerevisiae Proteins - chemistry | Development and progression | Glycoproteins | Alzheimer's disease | Protein binding | Index Medicus
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10. Full Text Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins
by Flavin, William P and Bousset, Luc and Green, Zachary C and Chu, Yaping and Skarpathiotis, Stratos and Chaney, Michael J and Kordower, Jeffrey H and Melki, Ronald and Campbell, Edward M
Acta Neuropathologica, ISSN 0001-6322, 10/2017, Volume 134, Issue 4, pp. 629 - 653
Numerous pathological amyloid proteins spread from cell to cell during neurodegenerative disease, facilitating the propagation of cellular pathology and... 
Pathology | α-Synuclein | Neurosciences | Medicine & Public Health | Huntingtin | Endocytic vesicle rupture | Galectin 3 | Tau | Lewy body | AUTOPHAGY | PATHOLOGY | LEWY-BODY | NEUROBLASTOMA-CELLS | NEUROSCIENCES | NEURODEGENERATIVE DISEASES | CLINICAL NEUROLOGY | TRANSMISSION | LYSOSOMAL MEMBRANE PERMEABILIZATION | FIBRILS | OLFACTORY-BULB | PATHOLOGICAL ALPHA-SYNUCLEIN | alpha-Synuclein | PARKINSONS-DISEASE | Unilamellar Liposomes | Parkinson Disease - pathology | Humans | Cells, Cultured | Rats | Male | Fluoresceins | Phosphatidylglycerols | Autophagy | Brain - metabolism | Amyloidogenic Proteins - metabolism | Animals | Neurons - ultrastructure | Transport Vesicles - metabolism | Brain - pathology | Female | Biological Transport - physiology | Neurons - metabolism | Parkinson Disease - metabolism | Lewy Bodies - metabolism | Lewy Bodies - pathology | alpha-Synuclein - metabolism | Transport Vesicles - ultrastructure | Medicine, Experimental | Medical research | Nervous system diseases | Glycoproteins | Neuroimaging | Parkinson's disease | Polyglutamine | Disease | Neurodegenerative diseases | Vesicle fusion | Synuclein | Lewy bodies | Proteins | Endocytosis | Tau protein | β-Amyloid | Intracellular | Trinucleotide repeat diseases | Movement disorders | Index Medicus | Life Sciences | Cognitive Sciences | Neurons and Cognition | Psychology and behavior | Neurobiology
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11. Full Text The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates
by Wang, Yi-Ting and Kuo, Pan-Hsien and Chiang, Chien-Hao and Liang, Jhe-Ruei and Chen, Yun-Ru and Wang, Shuying and Shen, James C. K and Yuan, Hanna S
Journal of Biological Chemistry, ISSN 0021-9258, 03/2013, Volume 288, Issue 13, pp. 9049 - 9057
TDP-43 is the major pathological protein identified in the cellular inclusions in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. The... 
AMYLOID FIBRILS | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR FACTOR TDP-43 | SOLUTION SCATTERING | NEURONAL INCLUSIONS | CFTR EXON-9 | AMYOTROPHIC-LATERAL-SCLEROSIS | MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | DNA-BINDING PROTEIN-43 | CELLULAR TOXICITY | Protein Structure, Tertiary | DNA-Binding Proteins - physiology | Peptides - chemistry | Protein Structure, Secondary | Humans | Chromatography - methods | Glutathione Transferase - metabolism | Neurodegenerative Diseases - metabolism | Protein Folding | Amino Acid Motifs | DNA-Binding Proteins - metabolism | Amyloidogenic Proteins - metabolism | Frontotemporal Lobar Degeneration - metabolism | Glycine - chemistry | X-Rays | Amyotrophic Lateral Sclerosis - metabolism | Protein Denaturation | Protein Binding | Thiazoles - chemistry | Scattering, Radiation | Circular Dichroism | DNA, Complementary - metabolism | Dimerization | Index Medicus | Aggregation | Protein Structure and Folding | Neurodegenerative Diseases | Protein Self-assembly | Protein Structure
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12. Full Text Generating extracellular amyloid aggregates using E. coli cells
by Sivanathan, Viknesh and Hochschild, Ann
Genes and Development, ISSN 0890-9369, 12/2012, Volume 26, Issue 23, pp. 2659 - 2667
Diverse proteins are known to be capable of forming amyloid aggregates, self-seeding fibrillar assemblies that may be biologically functional or pathological.... 
Sup35 | Yeast prions | Amyloid | Curli | Huntingtin | Protein export | PROTEIN | FIBRIL-FORMING SEGMENTS | SEQUENCE DETERMINANTS | PSI+ PRION | POLYMERIZATION | DEVELOPMENTAL BIOLOGY | SACCHAROMYCES-CEREVISIAE | PREDICTION | CELL BIOLOGY | IN-VITRO | amyloid | curli | protein export | huntingtin | GENETICS & HEREDITY | INHERITANCE | yeast prions | YEAST PRION | Prions - metabolism | Prions - genetics | Peptide Termination Factors - genetics | Amyloidogenic Proteins - analysis | Humans | Bacterial Proteins - genetics | Amyloidogenic Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Molecular Biology - methods | Nerve Tissue Proteins - genetics | Peptide Termination Factors - metabolism | Nerve Tissue Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Huntingtin Protein | Amyloidogenic Proteins - metabolism | Escherichia coli - genetics | Escherichia coli - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Bacterial Proteins - metabolism | Peptide Termination Factors - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Cultures (Biology) | Escherichia coli | Physiological aspects | Protein biosynthesis | Glycoproteins | Research | Methods | Index Medicus | Methodology | Resource
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13. Full Text Effect of position-specific single-point mutations and biophysical characterization of amyloidogenic peptide fragments identified from lattice corneal dystrophy patients
by Anandalakshmi, Venkatraman and Murugan, Elavazhagan and Leng, Eunice Goh Tze and Ting, Lim Wei and Chaurasia, Shyam S and Yamazaki, Toshio and Nagashima, Toshio and George, Benjamin Lawrence and Peh, Gary Swee Lim and Pervushin, Konstantin and Lakshminarayanan, Rajamani and Mehta, Jodhbir S
Biochemical Journal, ISSN 0264-6021, 05/2017, Volume 474, Issue 10, pp. 1705 - 1725
Corneal stromal dystrophies are a group of genetic disorders that may be caused by mutations in the transforming growth factor beta-induced (TGFBI) gene which... 
GENE-MUTATIONS | INDUCED PROTEIN TGFBIP | GROWTH-FACTOR-BETA | IN-VITRO | FIBRILS | NMR CHEMICAL-SHIFTS | KERATOEPITHELIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIGH3 GENE | CELL-ADHESION | AGGREGATION | Cornea - ultrastructure | Up-Regulation | Humans | Transforming Growth Factor beta1 - metabolism | Corneal Dystrophies, Hereditary - genetics | Eye Proteins - chemistry | Amyloidogenic Proteins - chemistry | Amyloid - chemistry | Chromatography, High Pressure Liquid | Transforming Growth Factor beta - chemistry | Amyloid - ultrastructure | Tandem Mass Spectrometry | Transforming Growth Factor beta1 - chemistry | Spectrometry, Mass, Electrospray Ionization | Amyloid - metabolism | Corneal Dystrophies, Hereditary - pathology | Nuclear Magnetic Resonance, Biomolecular | Cornea - cytology | Cornea - pathology | Protein Interaction Domains and Motifs | Eye Proteins - genetics | Protein Stability | Circular Dichroism | Peptide Fragments - genetics | Protein Aggregation, Pathological - genetics | Amyloidogenic Proteins - genetics | Amyloid - genetics | Microscopy, Electron, Transmission | Peptide Fragments - metabolism | Cells, Cultured | Transforming Growth Factor beta1 - genetics | Corneal Dystrophies, Hereditary - metabolism | Cornea - metabolism | Point Mutation | Amyloidogenic Proteins - metabolism | Peptide Fragments - chemistry | Transforming Growth Factor beta - genetics | Eye Proteins - metabolism | Kinetics | Transforming Growth Factor beta - metabolism | Protein Aggregation, Pathological - metabolism | Amino Acid Substitution | Index Medicus | corneal dystrophy | amyloid | amino acid substitution | β-sheet propensity | protein aggregation | TGFBIp
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14. Full Text Aβ-induced Golgi fragmentation in Alzheimer's disease enhances Aβ production
by Gunjan Joshi and Youjian Chi and Zheping Huang and Yanzhuang Wang
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2014, Volume 111, Issue 13, pp. 4748 - 4748
Golgi fragmentation occurs in neurons of patients with Alzheimer's disease (AD), but the underlying molecular mechanism causing the defects and the subsequent... 
PNAS Plus: Significance Statements | NEUROFIBRILLARY TANGLES | APOPTOSIS | GM130 | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | AMYLOID PRECURSOR PROTEIN | CLEAVAGE | Golgi stacking | GRASP65 | GRASP55 | APP processing | CISTERNAL STACKING | IN-VIVO | APPARATUS | amyloidogenic | Cricetulus | Amyloid beta-Peptides - pharmacology | Humans | Protein Transport - drug effects | Alzheimer Disease - pathology | Neurons - ultrastructure | Membrane Proteins - metabolism | Neurons - metabolism | Phosphorylation - drug effects | Golgi Apparatus - ultrastructure | CHO Cells | Cricetinae | Amyloid beta-Peptides - biosynthesis | Mice, Inbred C57BL | Cells, Cultured | Mice, Transgenic | Mutant Proteins - metabolism | Hippocampus - pathology | Enzyme Activation - drug effects | Cyclin-Dependent Kinase 5 - metabolism | Animals | Carrier Proteins - metabolism | Presenilin-1 - metabolism | Alzheimer Disease - metabolism | Golgi Apparatus - metabolism | Mice | Protein Kinase Inhibitors - pharmacology | Index Medicus
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