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1. Full Text Shear‐Stress‐Mediated Refolding of Proteins from Aggregates and Inclusion Bodies
by Yuan, Tom Z and Ormonde, Callum F. G and Kudlacek, Stephan T and Kunche, Sameeran and Smith, Joshua N and Brown, William A and Pugliese, Kaitlin M and Olsen, Tivoli J and Iftikhar, Mariam and Raston, Colin L and Weiss, Gregory A
Chembiochem : a European journal of chemical biology, ISSN 1439-4227, 02/2015, Volume 16, Issue 3, pp. 393 - 396
protein folding | shear stress | green chemistry | protein expression | Shear stress | Protein expression | Green chemistry | Protein folding | Pharmacology & Pharmacy | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Chemistry, Medicinal | Science & Technology | Cyclic AMP-Dependent Protein Kinases - metabolism | Recombinant Proteins - metabolism | Catalytic Domain | Protein Structure, Secondary | Caveolin 1 - chemistry | Muramidase - chemistry | Cyclic AMP-Dependent Protein Kinases - chemistry | Protein Refolding | Recombinant Proteins - chemistry | Muramidase - metabolism | Equipment Design | Caveolin 1 - metabolism | Inclusion Bodies - metabolism | Green Chemistry Technology - instrumentation | Thin films | Proteins | Yuan (China) | Green technology | Measuring instruments | Bacteria | Dielectric films | Lysozyme | Kinases | Index Medicus | proteins
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2. Full Text Cellular milieu imparts distinct pathological α-synuclein strains in α-synucleinopathies
by Peng, Chao and Gathagan, Ronald J and Covell, Dustin J and Medellin, Coraima and Stieber, Anna and Robinson, John L and Zhang, Bin and Pitkin, Rose M and Olufemi, Modupe F and Luk, Kelvin C and Trojanowski, John Q and Lee, Virginia M.-Y
Nature (London), ISSN 0028-0836, 05/2018, Volume 557, Issue 7706, pp. 558 - 563
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Neurons - pathology | Oligodendroglia - metabolism | alpha-Synuclein - classification | Humans | Cytoplasm - metabolism | Male | Cytoplasm - pathology | Female | Neurons - metabolism | Lewy Bodies - metabolism | Lewy Bodies - pathology | Oligodendroglia - chemistry | Cytoplasm - chemistry | Lewy Bodies - chemistry | Neurons - chemistry | Mice, Inbred C57BL | Lewy Body Disease - pathology | Organ Specificity | Protein Folding | alpha-Synuclein - chemistry | Lewy Body Disease - metabolism | Oligodendroglia - pathology | Animals | Mice | alpha-Synuclein - metabolism | Parkinson's disease | Seeds | Neurodegenerative diseases | Neurons | Lewy body disease | Synuclein | Seeding | Lewy bodies | Atrophy | Pathology | Axons | Hypotheses | Neurodegeneration | Inclusion bodies | Oligodendrocytes | Dementia disorders | Intracellular | Alzheimers disease | Alzheimer's disease | Movement disorders | Dementia | Index Medicus
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3. Full Text Presynaptic α-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with lewy bodies
by Kramer, Michael L and Schulz-Schaeffer, Walter J
The Journal of neuroscience, ISSN 0270-6474, 02/2007, Volume 27, Issue 6, pp. 1405 - 1410
Dendritic spines | Parkinson's disease | Neurodegeneration | α-synuclein | Dementia with Lewy bodies | Lewy bodies | Presynaptic | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Centrifugation, Density Gradient | Filtration | Presynaptic Terminals - pathology | Presynaptic Terminals - chemistry | Humans | Lewy Body Disease - pathology | Dendrites - ultrastructure | Frontal Lobe - chemistry | Lewy Bodies | Synaptosomes - chemistry | Nerve Degeneration - pathology | Synaptic Transmission | Paraffin Embedding - methods | alpha-Synuclein - analysis | Inclusion Bodies - pathology | Nerve Degeneration - etiology | Lewy Body Disease - physiopathology | Index Medicus | dementia with Lewy bodies | presynaptic | Brief Communications | neurodegeneration | dendritic spines
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4. Full Text Exploring the nature of inclusion bodies by MALDI mass spectrometry using recombinant proinsulin as a model protein
by Gardner, Qurratulann Afza and Hassan, Nadia and Hafeez, Shakir and Arif, Muhammad and Akhtar, Muhammad
International journal of biological macromolecules, ISSN 0141-8130, 10/2019, Volume 139, pp. 647 - 653
13C and 15N labelled proinsulin | MALDI and redox nature of inclusion bodies | Orientation of thiols in inclusion bodies | Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Applied | Polymer Science | Science & Technology | Proinsulin - chemistry | Oxidation-Reduction | Peptides - chemistry | Inclusion Bodies - chemistry | Escherichia coli | Humans | Recombinant Proteins - chemistry | Cytoplasm - metabolism | Cysteine - chemistry | Methionine - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Domains | Nitrogen Isotopes - chemistry | Sulfhydryl Compounds - chemistry | Protein Processing, Post-Translational | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Carbon Isotopes - chemistry | Hydrogen-Ion Concentration | Iodoacetamide - chemistry | Index Medicus
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5. Full Text Bacterial Inclusion Bodies: Discovering Their Better Half
by Rinas, Ursula and Garcia-Fruitós, Elena and Corchero, José Luis and Vázquez, Esther and Seras-Franzoso, Joaquin and Villaverde, Antonio
Trends in biochemical sciences (Amsterdam. Regular ed.), ISSN 0968-0004, 09/2017, Volume 42, Issue 9, pp. 726 - 737
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Bacteria - metabolism | Bacteria - chemistry | Inclusion Bodies - metabolism | Inclusion Bodies - chemistry | Molecular biology | Recombinant proteins | Glycoproteins | Index Medicus
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6. Full Text Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
by Kim, Hong Joo and Kim, Nam Chul and Wang, Yong-Dong and Scarborough, Emily A and Moore, Jennifer and Diaz, Zamia and MacLea, Kyle S and Freibaum, Brian and Li, Songqing and Molliex, Amandine and Kanagaraj, Anderson P and Carter, Robert and Boylan, Kevin B and Wojtas, Aleksandra M and Rademakers, Rosa and Pinkus, Jack L and Greenberg, Steven A and Trojanowski, John Q and Traynor, Bryan J and Smith, Bradley N and Topp, Simon and Gkazi, Athina-Soragia and Miller, Jack and Shaw, Christopher E and Kottlors, Michael and Kirschner, Janbernd and Pestronk, Alan and Li, Yun R and Ford, Alice Flynn and Gitler, Aaron D and Benatar, Michael and King, Oliver D and Kimonis, Virginia E and Ross, Eric D and Weihl, Conrad C and Shorter, James and Taylor, J. Paul
Nature (London), ISSN 0028-0836, 03/2013, Volume 495, Issue 7442, pp. 467 - 473
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Prions - genetics | Humans | Molecular Sequence Data | Osteitis Deformans - metabolism | Male | Drosophila melanogaster - genetics | Osteitis Deformans - genetics | Drosophila melanogaster - metabolism | Frontotemporal Dementia - metabolism | Muscular Dystrophies, Limb-Girdle - genetics | Myositis, Inclusion Body - pathology | Female | Inclusion Bodies - metabolism | Muscular Dystrophies, Limb-Girdle - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Frontotemporal Dementia - pathology | RNA - metabolism | Frontotemporal Dementia - genetics | Amino Acid Sequence | Prions - metabolism | Peptide Termination Factors - genetics | Amyotrophic Lateral Sclerosis - genetics | Drosophila melanogaster - cytology | Mutant Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Mutant Proteins - metabolism | Protein Structure, Tertiary - genetics | Prions - chemistry | Saccharomyces cerevisiae Proteins - genetics | Mutation - genetics | Myositis, Inclusion Body - genetics | Peptide Termination Factors - metabolism | Amyotrophic Lateral Sclerosis - pathology | Inclusion Bodies - genetics | Osteitis Deformans - pathology | Animals | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Muscular Dystrophies, Limb-Girdle - metabolism | Mutant Proteins - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Inclusion Bodies - pathology | Myositis, Inclusion Body - metabolism | Mice | Peptide Termination Factors - chemistry | HeLa Cells | Saccharomyces cerevisiae Proteins - chemistry | Pathology | Insects | Genomics | Genetics | Software | Genomes | Mutation | Genetic testing | Patients | Index Medicus
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7. Full Text Cajal bodies: A long history of discovery
by Cioce, Mario and Lamond, Angus I
Annual review of cell and developmental biology, ISSN 1081-0706, 2005, Volume 21, Issue 1, pp. 105 - 131
Nucleus | Disease | Coilin | snRNP | Stress | Intranuclear Inclusion Bodies - chemistry | History, 20th Century | Humans | RNA-Binding Proteins - chemistry | Coiled Bodies - chemistry | Forecasting | Animals | Cell Nucleus - metabolism | Models, Biological | Coiled Bodies - metabolism | Cell Nucleus - chemistry | Ribonucleoproteins, Small Nuclear - chemistry | Intranuclear Inclusion Bodies - metabolism | RNA-Binding Proteins - metabolism | Ribonucleoproteins, Small Nuclear - metabolism | Index Medicus
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8. Full Text Amyloid-like Properties of Bacterial Inclusion Bodies
by Carrió, Mar and González-Montalbán, Nuria and Vera, Andrea and Villaverde, Antonio and Ventura, Salvador
Journal of molecular biology, ISSN 0022-2836, 2005, Volume 347, Issue 5, pp. 1025 - 1037
inclusion bodies | protein folding | protein misfolding | protein aggregation | protein production | Protein aggregation | Protein misfolding | Protein production | Protein folding | Inclusion bodies | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Microscopy, Electron, Transmission | Capsid Proteins - metabolism | Inclusion Bodies - chemistry | Solubility | Spectrometry, Fluorescence | Amyloid - chemistry | Escherichia coli - chemistry | Protein Folding | Amyloid - metabolism | Escherichia coli - genetics | Capsid Proteins - chemistry | Escherichia coli - metabolism | Protein Denaturation | beta-Galactosidase - metabolism | Protein Binding | beta-Galactosidase - chemistry | Kinetics | beta-Galactosidase - genetics | Inclusion Bodies - metabolism | Circular Dichroism | Escherichia coli - ultrastructure | Capsid Proteins - genetics | Polypeptides | Analysis | Water quality | Glycoproteins | Recombinant DNA | Rain and rainfall | Dyes and dyeing | Index Medicus
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9. Full Text Characterization of recombinant pectate lyase refolded from inclusion bodies generated in E. coli BL21(DE3)
by Kumar, Sandeep and Jain, Kavish Kumar and Singh, Anupam and Panda, Amulya K and Kuhad, Ramesh Chander
Protein expression and purification, ISSN 1046-5928, 06/2015, Volume 110, pp. 43 - 51
Recombinant pectate lyase | CD spectra | Inclusion bodies | Refolding | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Biochemical Research Methods | Science & Technology | Temperature | Inclusion Bodies - chemistry | Bacterial Proteins - chemistry | Bacillus subtilis - chemistry | Calcium - chemistry | Urea - chemistry | Recombinant Proteins - isolation & purification | Cloning, Molecular | Escherichia coli - metabolism | Polysaccharide-Lyases - chemistry | Catalytic Domain | Gene Expression | Polysaccharide-Lyases - genetics | Polysaccharide-Lyases - isolation & purification | Bacterial Proteins - genetics | Enzyme Stability | Protein Refolding | Solubility | Recombinant Proteins - chemistry | Bacillus subtilis - enzymology | Recombinant Proteins - genetics | Plasmids - metabolism | Pectins - chemistry | Escherichia coli - genetics | Plasmids - chemistry | Protein Binding | Protein Conformation | Kinetics | Bacterial Proteins - isolation & purification | Hydrogen-Ion Concentration | Escherichia coli | Chemical properties | Index Medicus
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10. Full Text One-pot refolding of core histones from bacterial inclusion bodies allows rapid reconstitution of histone octamer
by Lee, Young-Tae and Gibbons, Garrett and Lee, Shirley Y and Nikolovska-Coleska, Zaneta and Dou, Yali
Protein expression and purification, ISSN 1046-5928, 06/2015, Volume 110, pp. 89 - 94
Histone methyltransferase | Histone octamer | Small angle X-ray scattering | Nucleosome | Refolding | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Biochemical Research Methods | Science & Technology | Recombinant Fusion Proteins - isolation & purification | Guanidine - chemistry | Histones - chemistry | Inclusion Bodies - chemistry | Nucleosomes - chemistry | Humans | Protein Multimerization | Crystallography, X-Ray | Myeloid-Lymphoid Leukemia Protein - chemistry | Amphibian Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Amphibian Proteins - isolation & purification | Sodium Chloride - chemistry | Cell Line | Methyltransferases - chemistry | Gene Expression | Protein Structure, Secondary | Protein Refolding | Solubility | Models, Molecular | Nucleosomes - metabolism | Recombinant Fusion Proteins - chemistry | Plasmids - metabolism | Histone-Lysine N-Methyltransferase - chemistry | Histones - isolation & purification | Animals | Histones - genetics | Amphibian Proteins - chemistry | Escherichia coli - genetics | Xenopus laevis - metabolism | Plasmids - chemistry | Recombinant Fusion Proteins - genetics | Histones | DNA binding proteins | Index Medicus
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