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humans (264) 264
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1. Full Text Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
by Chiti, Fabrizio and Dobson, Christopher M
Annual Review of Biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 27 - 68
Peptides and proteins have been found to possess an inherent tendency to convert from their native functional states into intractable amyloid aggregates. This... 
amyloidosis | quality control | protein aggregation | protein homeostasis | conformational diseases | chaperones | functional amyloid | Protein aggregation | Quality control | Functional amyloid | Amyloidosis | Chaperones | Protein homeostasis | Conformational diseases | FIBRIL FORMATION | NUCLEATED CONFORMATIONAL CONVERSION | SOLID-STATE NMR | STOP-CODON MUTATION | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAMILIAL BRITISH DEMENTIA | ALPHA-SYNUCLEIN AGGREGATION | BETA PRECURSOR PROTEIN | APOLIPOPROTEIN AII GENE | HUMAN PRION PROTEIN | Proteostasis Deficiencies - metabolism | Molecular Chaperones - metabolism | History, 21st Century | Parkinson Disease - history | Humans | Proteostasis Deficiencies - history | Protein Aggregation, Pathological - history | Drugs, Investigational | Parkinson Disease - drug therapy | Amyloid - chemistry | Diabetes Mellitus, Type 2 - metabolism | Diabetes Mellitus, Type 2 - history | Molecular Targeted Therapy | Alzheimer Disease - pathology | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Protein Aggregation, Pathological - prevention & control | Parkinson Disease - metabolism | Immunoglobulin Light-chain Amyloidosis | Amyloid - genetics | Alzheimer Disease - history | Parkinson Disease - pathology | Amyloidosis - pathology | Amyloidosis - history | Gene Expression Regulation | Molecular Chaperones - genetics | Proteostasis Deficiencies - pathology | Alzheimer Disease - drug therapy | Amyloidosis - drug therapy | Protein Folding | Proteostasis Deficiencies - prevention & control | Alzheimer Disease - metabolism | Protein Conformation | Diabetes Mellitus, Type 2 - pathology | Proteostasis Deficiencies - drug therapy | Diabetes Mellitus, Type 2 - drug therapy | Amyloidosis - metabolism | Protein Aggregation, Pathological - metabolism | Physiological aspects | Development and progression | Genetic aspects | Protein folding | Amyloid beta-protein
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2. Full Text In vivo aspects of protein folding and quality control
by Balchin, David and Hayer-Hartl, Manajit and Hartl, F. Ulrich
Science, ISSN 0036-8075, 07/2016, Volume 353, Issue 6294, pp. aac4354 - aac4354
Most proteins must fold into unique three-dimensional structures to perform their biological functions. In the crowded cellular environment, newly synthesized... 
EUKARYOTIC CHAPERONIN TRIC/CCT | HSP70 CHAPERONE | HSP90 MOLECULAR CHAPERONE | NASCENT CHAIN | TRIGGER FACTOR | MULTIDISCIPLINARY SCIENCES | REAL-TIME OBSERVATION | CONFORMATIONAL DYNAMICS | MISFOLDED PROTEINS | NEURODEGENERATIVE DISEASES | SUBSTRATE RECOGNITION | Protein Aggregates | Proteostasis Deficiencies - metabolism | Protein Biosynthesis | Humans | Ribosomes - chemistry | Homeostasis | Molecular Chaperones - chemistry | Neurodegenerative Diseases - metabolism | HSP72 Heat-Shock Proteins - chemistry | Molecular Targeted Therapy | Neurodegenerative Diseases - drug therapy | Protein Aggregation, Pathological - drug therapy | Protein Folding | Proteostasis Deficiencies - genetics | Proteolysis | Cytosol - metabolism | Protein Conformation | Proteostasis Deficiencies - drug therapy | Protein Aggregation, Pathological - metabolism | Aging - metabolism | Molecular biology | Protein folding | Polypeptides | Index Medicus | Proteins | Networks | Cellular | Molecular structure | Constants | Folding | Three dimensional | Diseases
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3. Full Text Preventing proteostasis diseases by selective inhibition of a phosphatase regulatory subunit
by Das, Indrajit and Krzyzosiak, Agnieszka and Schneider, Kim and Wrabetz, Lawrence and D'Antonio, Maurizio and Barry, Nicholas and Sigurdardottir, Anna and Bertolotti, Anne
Science, ISSN 0036-8075, 04/2015, Volume 348, Issue 6231, pp. 239 - 242
Protein phosphorylation regulates virtually all biological processes. Although protein kinases are popular drug targets, targeting protein phosphatases remains... 
INDUCED GENE-EXPRESSION | HOMEOSTASIS | UNFOLDED PROTEIN RESPONSE | MEMORY | GUANABENZ | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | ALS | DEATH | STRESS | TRANSGENIC MICE | Phosphorylation | Guanabenz - chemical synthesis | Humans | Molecular Targeted Therapy | Amyotrophic Lateral Sclerosis - drug therapy | Enzyme Inhibitors - pharmacokinetics | Enzyme Inhibitors - toxicity | Charcot-Marie-Tooth Disease - metabolism | Disease Models, Animal | Guanabenz - analogs & derivatives | Endoplasmic Reticulum Stress - drug effects | Enzyme Inhibitors - metabolism | Signal Transduction | Cells, Cultured | Enzyme Inhibitors - pharmacology | Mice, Transgenic | Charcot-Marie-Tooth Disease - drug therapy | Charcot-Marie-Tooth Disease - pathology | Protein Folding | Guanabenz - pharmacology | Guanabenz - toxicity | Proteostasis Deficiencies - prevention & control | Amyotrophic Lateral Sclerosis - pathology | Protein Phosphatase 1 - antagonists & inhibitors | Animals | Amyotrophic Lateral Sclerosis - metabolism | Guanabenz - metabolism | Mice | HeLa Cells | Proteostasis Deficiencies - drug therapy | Prevention | Homeostasis | Phosphatases | Health aspects | Proteins | Government regulations | Pathways | Kinases | Diseases | Defects
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4. Full Text Chemical kinetics for drug discovery to combat protein aggregation diseases
by Arosio, Paolo and Vendruscolo, Michele and Dobson, Christopher M and Knowles, Tuomas P.J
Trends in Pharmacological Sciences, ISSN 0165-6147, 2014, Volume 35, Issue 3, pp. 127 - 135
Highlights • Protein misfolding diseases largely lack effective pharmaceutical treatments. • Compounds with the ability to interfere with protein aggregation... 
Advanced Basic Science | neurodegenerative diseases | inhibition mechanism | therapeutics | aggregation kinetics | FIBRIL FORMATION | SICKLE HEMOGLOBIN POLYMERIZATION | ALZHEIMERS-DISEASE | CONGO RED | ALPHA-B-CRYSTALLIN | AMYLOID-BETA-PROTEIN | NUCLEATION MECHANISM | PEPTIDE | PHARMACOLOGY & PHARMACY | INHIBITORS | MOLECULAR-MECHANISMS | Proteostasis Deficiencies - metabolism | Proteins - metabolism | Protein Folding - drug effects | Humans | Models, Molecular | Kinetics | Neurodegenerative Diseases - metabolism | Proteins - chemistry | Proteostasis Deficiencies - drug therapy | Neurodegenerative Diseases - drug therapy | Drug Discovery | Proteins - antagonists & inhibitors | Chemical reaction, Rate of | Analysis
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5. Full Text Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease?
by Tipping, Kevin W and van Oosten-Hawle, Patricija and Hewitt, Eric W and Radford, Sheena E
Trends in Biochemical Sciences, ISSN 0968-0004, 12/2015, Volume 40, Issue 12, pp. 719 - 727
The formation of amyloid fibres is a hallmark of amyloid disorders. Nevertheless, the lack of correlation between fibre load and disease as observed, for... 
amyloid | transmission | disease | fibres | Fibres | Amyloid | Disease | Transmission | IN-VITRO | TRANSMISSION | PROTEIN MISFOLDING DISEASES | FIBRILS | MECHANISM | ALPHA-SYNUCLEIN AGGREGATION | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEGRADATION | NUCLEATION | OLIGOMERS | Alzheimer Disease - etiology | Proteostasis Deficiencies - metabolism | Animals | Amyloid - metabolism | Humans | Alzheimer Disease - metabolism | Alzheimer Disease - drug therapy | Amyloid - chemistry | Proteostasis Deficiencies - drug therapy | Protein Aggregation, Pathological | Index Medicus
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