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1. Full Text Small molecules that target protein misfolding
by Gavrin, Lori Krim and Denny, Rajiah Aldrin and Saiah, Eddine
Journal of Medicinal Chemistry, ISSN 0022-2623, 12/2012, Volume 55, Issue 24, pp. 10823 - 10843
Protein misfolding is a process in which proteins are unable to attain or maintain their biologically active conformation. Factors contributing to protein... 
PHARMACOLOGICAL CHAPERONE ACTION | HEREDITARY SYSTEMIC AMYLOIDOSIS | CHEMISTRY, MEDICINAL | FAMILIAL AMYLOID POLYNEUROPATHY | CELL-SURFACE EXPRESSION | VASOPRESSIN TYPE-2 RECEPTOR | RETINOL-BINDING-PROTEIN | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | NEPHROGENIC DIABETES-INSIPIDUS | CU,ZN SUPEROXIDE-DISMUTASE | Proteostasis Deficiencies - metabolism | Small Molecule Libraries - pharmacology | Humans | alpha 1-Antitrypsin - physiology | Neurodegenerative Diseases - drug therapy | Receptors, Vasopressin - chemistry | Tumor Suppressor Protein p53 - physiology | alpha 1-Antitrypsin - chemistry | Amyloid - metabolism | Superoxide Dismutase - physiology | Prealbumin - chemistry | Proteins - physiology | Muramidase - chemistry | Models, Molecular | Neurodegenerative Diseases - metabolism | Prions - chemistry | Unfolded Protein Response | Protein Folding | Superoxide Dismutase - chemistry | Small Molecule Libraries - chemistry | Animals | Prions - physiology | Serum Amyloid A Protein - chemistry | Protein Binding | Receptors, Vasopressin - physiology | Protein Conformation | Tumor Suppressor Protein p53 - chemistry | Mutation | Proteins - chemistry | Proteostasis Deficiencies - drug therapy | Superoxide Dismutase-1 | Prealbumin - physiology | Serum Amyloid A Protein - physiology | Muramidase - physiology | Index Medicus
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2. Full Text Transthyretin Constitutes a Functional Component in Pancreatic β-Cell Stimulus-Secretion Coupling
by Essam Refai and Nancy Dekki and Shao-Nian Yang and Gabriela Imreh and Over Cabrera and Lina Yu and Guang Yang and Svante Norgren and Sophia M. Rössner and Luca Inverardi and Camillo Ricordi and Gunilla Olivecrona and Mats Andersson and Hans Jörnvall and Per-Olof Berggren and Lisa Juntti-Berggren and Medicinska fakulteten and Fysiologisk kemi and Institutionen för medicinsk biovetenskap and Umeå universitet
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2005, Volume 102, Issue 47, pp. 17020 - 17025
Transthyretin (TTR) is a transport protein for thyroxine and, in association with retinol-binding protein, for retinol, mainly existing as a tetramer in vivo.... 
Depolarization | Biological Sciences | Delta cells | Diabetes complications | Islet cells | Diabetes | Membrane potential | Insulin | Monomers | Type 1 diabetes mellitus | Apoptosis | Insulin release | channels | Type 1 diabetes | β-cell signal transduction | type 1 diabetes | ISLETS | beta-cell signal | transduction | MULTIDISCIPLINARY SCIENCES | apoptosis | PREALBUMIN | insulin release | DIABETIC CHILDREN | Ca2+ channels | GLUCOSE | CALCIUM | SERUM-PROTEINS | Insulin-Secreting Cells - physiology | Patch-Clamp Techniques | Animals | Calcium - physiology | Glucose - physiology | Humans | Mice, Obese | Mice | Potassium Chloride | Membrane Potentials - physiology | Prealbumin - physiology | Proteins | Cellular biology | Pancreas | Index Medicus | Prealbumin/physiology | Mice; Obese | Glucose/physiology | Insulin-Secreting Cells/physiology | Calcium/physiology | Membrane Potentials/physiology
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3. Full Text Transthyretin enhances nerve regeneration
by Fleming, Carolina E and Saraiva, Maria J and Sousa, Mónica M
Journal of Neurochemistry, ISSN 0022-3042, 10/2007, Volume 103, Issue 2, pp. 831 - 839
Mutations in transthyretin (TTR) are associated with familial amyloid polyneuropathy, a neurodegenerative disorder characterized by TTR deposition in the PNS.... 
nerve regeneration | neurite outgrowth | peripheral nervous system | transthyretin | Peripheral nervous system | Nerve regeneration | Neurite outgrowth | Transthyretin | POLYNEUROPATHY | BIOCHEMISTRY & MOLECULAR BIOLOGY | RETINOL-BINDING-PROTEIN | THYROXINE | DORSAL-ROOT GANGLION | NEUROSCIENCES | PLASMA RETINOL | NEURONS | MICE | Sciatic Nerve - physiology | Prealbumin - genetics | Sciatic Nerve - pathology | Nerve Crush | Rats | Behavior, Animal - physiology | Neural Conduction - physiology | Ganglia, Spinal - cytology | PC12 Cells | Psychomotor Performance - physiology | Cerebellum - pathology | Mice, Knockout | Animals | Nerve Fibers - physiology | Nerve Regeneration - drug effects | Mice | Prealbumin - physiology | Comparative studies | Neurology | Biochemistry | Mutation | Transgenic animals | Rodents | Index Medicus
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4. Full Text Transthyretin influences spatial reference memory
by Sousa, João Carlos and Sousa, Nuno and Marques, Fernanda and Dias-Ferreira, Eduardo and Cerqueira, João José and Palha, Joana Almeida
Neurobiology of Learning and Memory, ISSN 1074-7427, 2007, Volume 88, Issue 3, pp. 381 - 385
Transthyretin (TTR) is a plasma and cerebrospinal fluid carrier for thyroxine and retinol, described also to sequester the amyloid beta peptide. TTR levels... 
Aging | Cerebrospinal fluid | Memory | Transthyretin | memory | transthyretin | RATS | CEREBROSPINAL-FLUID | NEUROSCIENCES | PREFRONTAL CORTEX | PSYCHOLOGY | PSYCHOLOGY, MULTIDISCIPLINARY | METABOLISM | cerebrospinal fluid | MOUSE MODEL | BEHAVIORAL SCIENCES | MICE | aging | RETINOL | ALZHEIMERS | Prealbumin - genetics | Prealbumin - cerebrospinal fluid | Age Factors | Maze Learning - physiology | Spatial Behavior - physiology | Male | Reaction Time - physiology | Mice, Knockout | Space Perception - physiology | Animals | Analysis of Variance | Cognition - physiology | Mice | Prealbumin - analysis | Prealbumin - physiology | Memory - physiology | Cerebrospinal fluid proteins | Body fluids | Neurosciences | Rodents | Animal memory | Animal cognition | Index Medicus
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5. Full Text Transthyretin Internalization by Sensory Neurons Is Megalin Mediated and Necessary for Its Neuritogenic Activity
by Fleming, Carolina E and Mar, Fernando Milhazes and Franquinho, Filipa and Saraiva, Maria J and Sousa, Monica M
Journal of Neuroscience, ISSN 0270-6474, 03/2009, Volume 29, Issue 10, pp. 3220 - 3232
Mutated transthyretin (TTR) causes familial amyloid polyneuropathy, a neurodegenerative disorder characterized by TTR deposition in the peripheral nervous... 
RETROGRADE AXONAL-TRANSPORT | FAMILIAL AMYLOID POLYNEUROPATHY | PERIPHERAL-NERVES | RECEPTOR FAMILY | REGENERATION | DORSAL-ROOT GANGLIA | RENAL UPTAKE | SCHWANN-CELLS | PROXIMAL TUBULE | NEUROSCIENCES | NERVE GROWTH-FACTOR | Low Density Lipoprotein Receptor-Related Protein-2 - deficiency | Nerve Regeneration - genetics | Prealbumin - genetics | Prealbumin - deficiency | Low Density Lipoprotein Receptor-Related Protein-2 - physiology | Humans | Nerve Regeneration - physiology | Cells, Cultured | Ganglia, Spinal - cytology | Neurites - metabolism | Endocytosis - physiology | Mice, Knockout | Neurogenesis - genetics | Animals | Sensory Receptor Cells - cytology | Prealbumin - metabolism | Neurogenesis - physiology | Endocytosis - genetics | Mice | Sensory Receptor Cells - metabolism | Ganglia, Spinal - growth & development | Low Density Lipoprotein Receptor-Related Protein-2 - biosynthesis | Prealbumin - physiology | Ganglia, Spinal - metabolism | Index Medicus
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6. Full Text Transthyretin Is a Key Regulator of Myoblast Differentiation
by Lee, Eun Ju and Bhat, Abdul R and Kamli, Majid Rasool and Pokharel, Smritee and Chun, Tahoon and Lee, Yong-Ho and Nahm, Sang-Seop and Nam, Joo Hyun and Hong, Seong Koo and Yang, Bohsuk and Chung, Ki Young and Kim, Sang Hoon and Choi, Inho
PLoS ONE, ISSN 1932-6203, 05/2013, Volume 8, Issue 5, pp. e63627 - e63627
Transthyretin (TTR) is a known carrier protein for thyroxine (T-4) and retinol-binding protein in the blood that is primarily synthesized in the liver and... 
RESPONSE ELEMENT | SKELETAL-MUSCLE | OVEREXPRESSION | CA2+ ENTRY | CALCIUM-CHANNELS | THYROID-HORMONE | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | IDENTIFICATION | CELL-FUSION | MYOGENIN | Cell Line | Prealbumin - genetics | Calcium Channels - metabolism | Gene Expression - genetics | Mice, Inbred C57BL | Muscle Development - physiology | Male | Muscle, Skeletal - metabolism | Up-Regulation - genetics | Myogenin - genetics | Muscle Fibers, Skeletal - metabolism | Muscle, Skeletal - physiology | Cell Differentiation - genetics | Myoblasts - metabolism | Animals | Prealbumin - metabolism | Muscle Development - genetics | Mice | Cell Differentiation - physiology | Muscle Fibers, Skeletal - physiology | Myogenin - metabolism | Myoblasts - physiology | Muscles | Calcium channels | Retinoids | Gene expression | Genes | Protein binding | Choroid plexus | Brain | Biotechnology | Calcium | Liver | Zoology | STIM1 protein | Thyroid gland | Experiments | Vitamin A | Cell growth | Rodents | Cell cycle | Thyroxine | Myogenin | Calcium channels (voltage-gated) | Transthyretin | Animal sciences | Orai1 protein | Myogenesis | Skeletal muscle | Musculoskeletal system | Laboratory animals | Differentiation | Endoplasmic reticulum | Binding sites | Retinol-binding protein | Index Medicus
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7. Full Text Left Ventricular Structure and Function in Transthyretin-Related Versus Light-Chain Cardiac Amyloidosis
by Quarta, Candida Cristina and Solomon, Scott D and Uraizee, Imran and Kruger, Jenna and Longhi, Simone and Ferlito, Marinella and Gagliardi, Christian and Milandri, Agnese and Rapezzi, Claudio and Falk, Rodney H
Circulation, ISSN 0009-7322, 05/2014, Volume 129, Issue 18, pp. 1840 - 1849
BACKGROUND—Immunoglobulin amyloid light-chain (AL)-related cardiac amyloidosis (CA) has a worse prognosis than either wild-type (ATTRwt) or mutant (ATTRm)... 
amyloid | amyloidosis | transthyretin | echocardiography | hereditary | cardiomyopathies | transthyretin-related | DIAGNOSIS | CARDIAC & CARDIOVASCULAR SYSTEMS | MANAGEMENT | MYOCARDIAL-FUNCTION | HEART-FAILURE | VALIDATION | HEREDITARY AMYLOIDOSIS | LONGITUDINAL STRAIN | AL PRIMARY AMYLOIDOSIS | PERIPHERAL VASCULAR DISEASE | DYSFUNCTION | SPECKLE-TRACKING ECHOCARDIOGRAPHY | Multivariate Analysis | Cardiomyopathies - diagnostic imaging | Prevalence | Prognosis | Follow-Up Studies | Amyloid Neuropathies, Familial - metabolism | Humans | Middle Aged | Male | Incidence | Cardiomyopathies - mortality | Systole - physiology | Aged, 80 and over | Female | Ventricular Function, Left - physiology | Echocardiography | Amyloidosis - pathology | Amyloidosis - mortality | Diastole - physiology | Amyloid Neuropathies, Familial - pathology | Immunoglobulin Light Chains - metabolism | Prealbumin - metabolism | Cardiomyopathies - metabolism | Aged | Amyloid Neuropathies, Familial - mortality | Longitudinal Studies | Amyloidosis - metabolism | Case studies | Physiological aspects | Amyloidosis | Diagnosis | Research | Heart ventricle, Left | Index Medicus | Abridged Index Medicus
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8. Full Text Fate tracing of mature hepatocytes in mouse liver homeostasis and regeneration
by Malato, Yann and Naqvi, Syed and Schürmann, Nina and Ng, Raymond and Wang, Bruce and Zape, Joan and Kay, Mark A and Grimm, Dirk and Willenbring, Holger
Journal of Clinical Investigation, ISSN 0021-9738, 12/2011, Volume 121, Issue 12, pp. 4850 - 4860
Recent evidence has contradicted the prevailing view that homeostasis and regeneration of the adult liver are mediated by self duplication of... 
MEDICINE, RESEARCH & EXPERIMENTAL | PARTIAL-HEPATECTOMY | STEM-CELLS | SOMATIC MUTAGENESIS | RAT LIVER | ADENOASSOCIATED VIRUS | DEOXYRIBONUCLEIC ACID | BILIARY DUCTULAR CELLS | OVAL CELLS | MESENCHYMAL TRANSITION | TRANSGENIC MICE | Dependovirus - genetics | Prealbumin - genetics | Liver - pathology | Species Specificity | Hepatic Duct, Common - pathology | Stem Cells - cytology | Bacterial Proteins - analysis | Hepatectomy | Liver - injuries | Hepatocytes - cytology | Luminescent Proteins - analysis | Chemical and Drug Induced Liver Injury - pathology | Transgenes | Genes, Reporter | Mice, Inbred C57BL | Bacterial Proteins - genetics | Epithelial Cells - pathology | Carbon Tetrachloride Poisoning - pathology | Liver Regeneration - physiology | Genetic Vectors - genetics | Cell Lineage | Animals | Pyridines - toxicity | Homeostasis - physiology | Liver - physiology | Luminescent Proteins - genetics | Mice | Hepatic Duct, Common - injuries | Integrases - genetics | Homeostasis | Regeneration | Genetic aspects | Growth | Liver cells | Liver | Index Medicus | Abridged Index Medicus
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9. Full Text Misfolded transthyretin causes behavioral changes in a Drosophila model for transthyretin-associated amyloidosis
by Pokrzywa, Malgorzata and Dacklin, Ingrid and Hultmark, Dan and Lundgren, Erik and Medicinska fakulteten and Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten) and Institutionen för molekylärbiologi (Medicinska fakulteten) and Umeå universitet
European Journal of Neuroscience, ISSN 0953-816X, 08/2007, Volume 26, Issue 4, pp. 913 - 924
Familial amyloidotic polyneuropathy is an autosomal dominant neurodegenerative disorder caused by accumulation of mutated transthyretin (TTR) amyloid fibrils... 
Amyloid | Amyloidosis | Neurodegeneration | Drosophila | Transthyretin | Familial amyloidotic polyneuropathy | POLYNEUROPATHY | amyloidosis | VARIANTS | transthyretin | neurodegeneration | TOXICITY | BINDING PROTEIN | NEUROSCIENCES | PRION PROTEIN | MUTANTS | amyloid | familial amyloidotic polyneuropathy | DISEASE | NEURAL DEGENERATION | TRANSGENIC MICE | Immunohistochemistry | Motor Activity - physiology | Prealbumin - genetics | Drosophila melanogaster - physiology | Amyloidosis - psychology | DNA, Complementary - genetics | Aging - psychology | Behavior, Animal - physiology | Longevity - genetics | Neuropeptides - physiology | Blotting, Western | Protein Folding | Flight, Animal - physiology | Microscopy, Confocal | Phenotype | Animals | Wings, Animal - anatomy & histology | Amyloidosis - genetics | DNA, Complementary - biosynthesis | Hemolymph - chemistry | Prealbumin - chemistry | Transgenes | Prealbumin - physiology | Index Medicus
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10. Full Text Making sense of the amyloid precursor protein: its tail tells an interesting tale
by Cappai, Roberto
Journal of Neurochemistry, ISSN 0022-3042, 08/2014, Volume 130, Issue 3, pp. 325 - 327
Read the full article ‘The Aβ ‐clearance protein transthyretin, like neprilysin, is epigenetically regulated by the amyloid precursor protein intracellular... 
BETA-PROTEIN | NEUROSCIENCES | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INTRACELLULAR DOMAIN | Amyloid Precursor Protein Secretases - genetics | Prealbumin - genetics | Amyloid beta-Protein Precursor - genetics | Amyloid Precursor Protein Secretases - physiology | Amyloid beta-Protein Precursor - chemistry | Humans | Neprilysin - genetics | Alzheimer Disease - genetics | Amyloid beta-Protein Precursor - physiology | Neprilysin - physiology | Prealbumin - physiology | Amyloid beta-protein | Proteins | Alzheimers disease | Rodents | Index Medicus
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11. Full Text Amyloid fibrils trigger the release of neutrophil extracellular traps (NETs), causing fibril fragmentation by NET-associated elastase
by Azevedo, Estefania P.C and Guimarães-Costa, Anderson B and Torezani, Guilherme S and Braga, Carolina A and Palhano, Fernando L and Kelly, Jeffery W and Saraiva, Elvira M and Foguel, Debora
Journal of Biological Chemistry, ISSN 0021-9258, 10/2012, Volume 287, Issue 44, pp. 37206 - 37218
The accumulation of amyloid fibrils is a feature of amyloid diseases, where cell toxicity is due to soluble oligomeric species that precede fibril formation or... 
PATHOGENESIS | PROTEIN | DNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | MECHANISMS | EXPRESSION | VARIANT | ESCAPE | Chromatin - metabolism | Prealbumin - genetics | Reactive Oxygen Species - metabolism | Skin - metabolism | Humans | NADPH Oxidases - metabolism | alpha-Synuclein - physiology | Peptide Fragments - pharmacology | Amyloid - chemistry | Mutation, Missense | Lung - enzymology | Peptide Fragments - physiology | Extracellular Space - metabolism | Cell Nucleus - metabolism | Proteolysis | Acetophenones - pharmacology | Protein Structure, Quaternary | Lung - metabolism | Prealbumin - chemistry | alpha-Synuclein - genetics | Neutrophils - metabolism | Skin - pathology | Immunoglobulin Light-chain Amyloidosis | Neutrophils - pathology | Biomarkers - metabolism | Amyloid - genetics | Cell Survival - drug effects | Amyloid - physiology | Amyloidosis - enzymology | Cricetinae | Lung - pathology | Peptide Fragments - metabolism | Amyloidosis - pathology | Neutrophils - enzymology | Amyloid Neuropathies, Familial - genetics | NADPH Oxidases - antagonists & inhibitors | Amyloid Neuropathies, Familial - enzymology | Onium Compounds - pharmacology | Skin - enzymology | Amyloid Neuropathies, Familial - pathology | Hep G2 Cells | alpha-Synuclein - chemistry | Animals | Pancreatic Elastase | Chromatin - enzymology | Amyloidosis - metabolism | Prealbumin - physiology | Extracellular Space - enzymology | Index Medicus | Aggregation | Molecular Bases of Disease | α-Synuclein | Innate Immunity | Neutrophil Extracellular Trap | Amyloid | Toxic Oligomers | Neutrophil
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12. Full Text Transthyretin: A key gene involved in the maintenance of memory capacities during aging
by Brouillette, Jonathan and Quirion, Rémi
Neurobiology of Aging, ISSN 0197-4580, 2007, Volume 29, Issue 11, pp. 1721 - 1732
Abstract Aging is often associated with decline of memory function. Aged animals, like humans, can naturally develop memory impairments and thus represent a... 
Neurology | Internal Medicine | Aging | Morris water maze | Gene expression | Retinoic acid | Hippocampus | Transthyretin | hippocampus | WATER-MAZE | PROBE LEVEL DATA | transthyretin | AMYLOID PRECURSOR PROTEIN | SYNAPTIC PLASTICITY | NEUROSCIENCES | GERIATRICS & GERONTOLOGY | retinoic acid | MESSENGER-RNA | ONSET ALZHEIMERS-DISEASE | QUINONE REDUCTASE 2 | RETINOL-BINDING PROTEIN | SPATIAL MEMORY | aging | LONG-TERM POTENTIATION | gene expression | Animals | Aging - physiology | Prealbumin | Rats, Long-Evans | Rats | Behavior, Animal - physiology | Male | Hippocampus - physiology | Task Performance and Analysis | Memory - physiology | Genetic research | Index Medicus
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13. Full Text Post‐translational modifications of transthyretin affect the triiodonine‐binding potential
by Henze, Andrea and Homann, Thomas and Serteser, Mustafa and Can, Ozge and Sezgin, Ozlem and Coskun, Abdurrahman and Unsal, Ibrahim and Schweigert, Florian J and Ozpinar, Aysel
Journal of Cellular and Molecular Medicine, ISSN 1582-1838, 02/2015, Volume 19, Issue 2, pp. 359 - 370
Transthyretin ( TTR ) is a visceral protein, which facilitates the transport of thyroid hormones in blood and cerebrospinal fluid. The homotetrameric structure... 
transthyretin | molecular modelling | thyroid hormones | post‐translational modifications | mass spectrometry | triiodthyronine | cysteine oxidation | Cysteine oxidation | Molecular modelling | Post-translational modifications | Transthyretin | Thyroid hormones | Triiodthyronine | Mass spectrometry | MEDICINE, RESEARCH & EXPERIMENTAL | ISOFORMS | VARIANTS | STABILITY | THYROXINE-BINDING | PREALBUMIN | CELL BIOLOGY | TRANSPORT | GLUTATHIONE | THYROID-HORMONES | post-translational modifications | MICROHETEROGENEITY | PROTEINS | Triiodothyronine - metabolism | Prealbumin - metabolism | Humans | Middle Aged | Female | Male | Biological Transport - physiology | Cysteine - metabolism | Protein Processing, Post-Translational - physiology | Protein Binding - physiology | Post-translational modification | Cysteine | Chemical properties | Hypothyroidism | Analysis | Proteins | Hormones | Rodents | Thyroid diseases | Immunoprecipitation | Menopause | Thyroid gland | Cerebrospinal fluid | Experiments | Physiology | Triiodothyronine | Protein transport | Glutathione | Thyroid | Binding | Translation | Mass spectroscopy | Metabolism | Studies | Data collection | Binding sites | Index Medicus | Original
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14. Full Text Severe Iron Deficiency Anemia in Transgenic Mice Expressing Liver Hepcidin
by Gaël Nicolas and Myriam Bennoun and Arlette Porteu and Sandrine Mativet and Carole Beaumont and Bernard Grandchamp and Mario Sirito and Michéle Sawadogo and Axel Kahn and Sophie Vaulont
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2002, Volume 99, Issue 7, pp. 4596 - 4601
We recently reported the hemochromatosis-like phenotype observed in our Usf2 knockout mice. In these mice, as in murine models of hemochromatosis and patients... 
Biological Sciences | Phenotypes | Transgenic animals | Anemia | Liver | Iron deficiency anemia | Erythrocytes | Fetus | Iron | Mice | Gene expression | HOMEOSTASIS | TRANSPORTER | TRANSFERRIN RECEPTOR | GENE | MODELS | ROLES | MULTIDISCIPLINARY SCIENCES | DISTINCT | HEREDITARY HEMOCHROMATOSIS | Transcription Factors - physiology | Anemia, Iron-Deficiency - etiology | Antimicrobial Cationic Peptides - physiology | Mice, Inbred C57BL | Mice, Transgenic | Iron - metabolism | Upstream Stimulatory Factors | Animals | Biological Transport | Iron Overload - metabolism | Hepcidins | Antimicrobial Cationic Peptides - genetics | Transgenes | Prealbumin - physiology | DNA-Binding Proteins | Disease Models, Animal | Deficiency diseases | Genetically modified mice | Physiological aspects | Research | Peptide hormones | Rodents | Index Medicus
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