Process Biochemistry, ISSN 1359-5113, 06/2017, Volume 57, p. 105
Metals such as Cu2+, Fe3+, and Zn2+ are major contributors to the biology of a brain in stages of health, aging, and disease because of their unique effects on...
Oxidative stress | Cystatin | Brain | Metals | Fluorescence | Iron | pH effects | Proteins | Hydrogen ions | Neurodegeneration | Protein folding | Dichroism | Aging | Copper | Metal ions | Neurodegenerative diseases | Fibrils | Ions | Secondary structure | Zinc | Circular dichroism | Neurological diseases | Aggregates | Microscopy | β-Amyloid | Protein structure
Oxidative stress | Cystatin | Brain | Metals | Fluorescence | Iron | pH effects | Proteins | Hydrogen ions | Neurodegeneration | Protein folding | Dichroism | Aging | Copper | Metal ions | Neurodegenerative diseases | Fibrils | Ions | Secondary structure | Zinc | Circular dichroism | Neurological diseases | Aggregates | Microscopy | β-Amyloid | Protein structure
Journal Article
2.
Full Text
Denaturation induced aggregation in [alpha]-crystallin: differential action of chaotropes
Journal of Molecular Recognition, ISSN 0952-3499, 11/2016, Volume 29, Issue 11, p. 536
 [alpha]-Crystallin is a member of small heat shock proteins and is believed to play an exceptional role in the stability of eye lens proteins. The disruption...
Proteins | Heat shock proteins | Urea | Denaturation
Proteins | Heat shock proteins | Urea | Denaturation
Journal Article
Environmental Science: Processes and Impacts, ISSN 2050-7887, 7/2016, Volume 18, Issue 7, pp. 872 - 881
The binding study of pesticides with proteins is of great importance in ecotoxicology. In this study, a comparative interaction mechanism of phytocystatin with...
PROGRAMMED CELL-DEATH | CHEMISTRY, ANALYTICAL | ENVIRONMENTAL SCIENCES | IN-VITRO | METABOLITES | CHLORPYRIFOS | GLYPHOSATE | HUMAN SERUM-ALBUMIN | ENZYMES | GLYCATION | GENERATION | RESIDUES | Maneb - chemistry | Glycine - analogs & derivatives | Zineb - toxicity | Cicer - chemistry | Animals | Chlorpyrifos - chemistry | Glycine - toxicity | Reactive Oxygen Species - chemistry | Glycine - chemistry | Maneb - toxicity | Pesticides - toxicity | Cystatins - chemistry | Chlorpyrifos - toxicity | Pesticides - chemistry | Zineb - chemistry | Index Medicus
PROGRAMMED CELL-DEATH | CHEMISTRY, ANALYTICAL | ENVIRONMENTAL SCIENCES | IN-VITRO | METABOLITES | CHLORPYRIFOS | GLYPHOSATE | HUMAN SERUM-ALBUMIN | ENZYMES | GLYCATION | GENERATION | RESIDUES | Maneb - chemistry | Glycine - analogs & derivatives | Zineb - toxicity | Cicer - chemistry | Animals | Chlorpyrifos - chemistry | Glycine - toxicity | Reactive Oxygen Species - chemistry | Glycine - chemistry | Maneb - toxicity | Pesticides - toxicity | Cystatins - chemistry | Chlorpyrifos - toxicity | Pesticides - chemistry | Zineb - chemistry | Index Medicus
Journal Article
Current topics in medicinal chemistry, 2017, Volume 17, Issue 12, p. 1371
The maintenance of health requires successful cell functioning, which in turn depends upon the proper and active conformation of proteins besides other...
Biological Products - chemistry | Humans | Neurodegenerative Diseases - diagnosis | Neurodegenerative Diseases - drug therapy | Drug Discovery | Biological Products - therapeutic use
Biological Products - chemistry | Humans | Neurodegenerative Diseases - diagnosis | Neurodegenerative Diseases - drug therapy | Drug Discovery | Biological Products - therapeutic use
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 11/2014, Volume 562, pp. 51 - 61
Conformational alterations and aggregates of chickpea cystatin (CPC) were investigated upon sequential addition of trifluoroethanol (TFE) over a range of 0–70%...
Tannic acid | Aggregation | Polyphenols | Trifluoroethanol | Chick pea cystatin | Secondary structure | Aggregation Polyphenols | AQUEOUS-SOLUTIONS | FLUORESCENCE SPECTROSCOPY | INSULIN AGGREGATION | PROTEIN AGGREGATION | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA AGGREGATION | AMYLOID-FIBRIL FORMATION | IN-VITRO | INHIBITION | BIOPHYSICS | STEFIN-B | Microscopy, Electron, Transmission | Nephelometry and Turbidimetry | Protein Structure, Secondary | Spectrometry, Fluorescence | Tannins - chemistry | Amyloid - chemistry | Calibration | Cicer - chemistry | Spectroscopy, Fourier Transform Infrared | Cystatins - chemistry | Protein Denaturation | Protein Binding | Thiazoles - chemistry | Trifluoroethanol - chemistry | Circular Dichroism | Catechin - chemistry | Papain - chemistry
Tannic acid | Aggregation | Polyphenols | Trifluoroethanol | Chick pea cystatin | Secondary structure | Aggregation Polyphenols | AQUEOUS-SOLUTIONS | FLUORESCENCE SPECTROSCOPY | INSULIN AGGREGATION | PROTEIN AGGREGATION | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA AGGREGATION | AMYLOID-FIBRIL FORMATION | IN-VITRO | INHIBITION | BIOPHYSICS | STEFIN-B | Microscopy, Electron, Transmission | Nephelometry and Turbidimetry | Protein Structure, Secondary | Spectrometry, Fluorescence | Tannins - chemistry | Amyloid - chemistry | Calibration | Cicer - chemistry | Spectroscopy, Fourier Transform Infrared | Cystatins - chemistry | Protein Denaturation | Protein Binding | Thiazoles - chemistry | Trifluoroethanol - chemistry | Circular Dichroism | Catechin - chemistry | Papain - chemistry
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 08/2016, Volume 603, pp. 38 - 47
Fib having intrinsically disordered αC domains is involved in coagulation cascade and thrombosis. Fib molecules forms prefibrillar oligomers at 30%, and...
Fibrillar | Trifluoroethanol | Aggregates | Prefibrillar | Fibrinogen | FLUORESCENCE SPECTROSCOPY | ACID | PROTEIN AGGREGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | STATE | PEPTIDE | BIOPHYSICS | 2,2,2-TRIFLUOROETHANOL | Protein Structure, Secondary | Humans | Fibrinogen - chemistry | Spectroscopy, Fourier Transform Infrared | Fibrinolysis | Protein Folding | Thermodynamics | Intrinsically Disordered Proteins - chemistry | Blood Coagulation | Protein Denaturation | Hydrophobic and Hydrophilic Interactions | Microscopy, Atomic Force | Thiazoles - chemistry | Scattering, Radiation | Kinetics | Congo Red - chemistry | Circular Dichroism | Oligomers | Fibrin | Hydrogen | Polymerization | Islamic schools | Hydrogen bonding
Fibrillar | Trifluoroethanol | Aggregates | Prefibrillar | Fibrinogen | FLUORESCENCE SPECTROSCOPY | ACID | PROTEIN AGGREGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | STATE | PEPTIDE | BIOPHYSICS | 2,2,2-TRIFLUOROETHANOL | Protein Structure, Secondary | Humans | Fibrinogen - chemistry | Spectroscopy, Fourier Transform Infrared | Fibrinolysis | Protein Folding | Thermodynamics | Intrinsically Disordered Proteins - chemistry | Blood Coagulation | Protein Denaturation | Hydrophobic and Hydrophilic Interactions | Microscopy, Atomic Force | Thiazoles - chemistry | Scattering, Radiation | Kinetics | Congo Red - chemistry | Circular Dichroism | Oligomers | Fibrin | Hydrogen | Polymerization | Islamic schools | Hydrogen bonding
Journal Article
Current Topics in Medicinal Chemistry, ISSN 1568-0266, 04/2017, Volume 17, Issue 12, pp. 1371 - 1378
The maintenance of health requires successful cell functioning, which in turn depends upon the proper and active conformation of proteins besides other...
Aggregation | Conformational disease | Alzheimer’s disease | Neuropsychiatry | Amyotrophic lateral sclerosis | Neurodegenerative disorders | Parkinson’s disease | RILUZOLE | CHEMISTRY, MEDICINAL | Parkinson's disease | PROTEIN AGGREGATION | ALZHEIMERS-DISEASE | SOD1 MUTATION | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | ALPHA-SYNUCLEIN | MODEL | IDENTIFICATION | Alzheimer's disease | HUNTINGTONS-DISEASE
Aggregation | Conformational disease | Alzheimer’s disease | Neuropsychiatry | Amyotrophic lateral sclerosis | Neurodegenerative disorders | Parkinson’s disease | RILUZOLE | CHEMISTRY, MEDICINAL | Parkinson's disease | PROTEIN AGGREGATION | ALZHEIMERS-DISEASE | SOD1 MUTATION | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | ALPHA-SYNUCLEIN | MODEL | IDENTIFICATION | Alzheimer's disease | HUNTINGTONS-DISEASE
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 11/2015, Volume 81, pp. 60 - 68
Several mammalian proteins fold abnormally under non physiological conditions, to form pathological deposits that are associated with many degenerative...
Catechin | Amyloidosis | Fibrillation | Goat brain cystatin | Kaempferol | FIBRIL FORMATION | POLYMER SCIENCE | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GREEN | BETA | IN-VITRO | INHIBITION | STEFIN-B | (-)-EPIGALLOCATECHIN GALLATE | PRECURSOR PROTEIN | CHEMISTRY, APPLIED | AGGREGATION | Amyloidosis - pathology | Goats | Polyphenols - pharmacology | Spectrometry, Fluorescence | Amyloidosis - drug therapy | Cystatins - metabolism | Protein Aggregation, Pathological - drug therapy | Brain - drug effects | Brain - metabolism | Animals | Amyloid - metabolism | Protein Structure, Secondary - drug effects | Cystatins - chemistry | Brain - pathology | Kaempferols - pharmacology | Catechin - pharmacology | Circular Dichroism | Amyloidosis - metabolism | Protein Aggregation, Pathological - metabolism | Hydrogen-Ion Concentration | Comparative analysis | Therapeutics | Homeopathy | Materia medica and therapeutics
Catechin | Amyloidosis | Fibrillation | Goat brain cystatin | Kaempferol | FIBRIL FORMATION | POLYMER SCIENCE | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GREEN | BETA | IN-VITRO | INHIBITION | STEFIN-B | (-)-EPIGALLOCATECHIN GALLATE | PRECURSOR PROTEIN | CHEMISTRY, APPLIED | AGGREGATION | Amyloidosis - pathology | Goats | Polyphenols - pharmacology | Spectrometry, Fluorescence | Amyloidosis - drug therapy | Cystatins - metabolism | Protein Aggregation, Pathological - drug therapy | Brain - drug effects | Brain - metabolism | Animals | Amyloid - metabolism | Protein Structure, Secondary - drug effects | Cystatins - chemistry | Brain - pathology | Kaempferols - pharmacology | Catechin - pharmacology | Circular Dichroism | Amyloidosis - metabolism | Protein Aggregation, Pathological - metabolism | Hydrogen-Ion Concentration | Comparative analysis | Therapeutics | Homeopathy | Materia medica and therapeutics
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 07/2018, Volume 650, pp. 103 - 115
Reactive dicarbonyl species such as methylglyoxal (MGO) and glyoxal (GO) have recently received extensive attention due to their high reactivity and ability to...
Aggregation | Chickpea cystatin | Methylglyoxal | Redox state | Glyoxal | Reactive dicarbonyl species | HUMAN SERUM-ALBUMIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | LENS PROTEINS | DAMAGE | BIOPHYSICS | DEGRADATION | COMPLICATIONS | STRESS | END-PRODUCTS | BINDING | Protein Aggregates | Cystatins - ultrastructure | Glyoxal - metabolism | Oxidation-Reduction | Glycosylation | Cicer - chemistry | Cystatins - metabolism | Cicer - metabolism | Pyruvaldehyde - metabolism | Plant Proteins - chemistry | Glycation End Products, Advanced - metabolism | Cystatins - chemistry | Lysine - metabolism | Plant Proteins - metabolism | Arginine - metabolism
Aggregation | Chickpea cystatin | Methylglyoxal | Redox state | Glyoxal | Reactive dicarbonyl species | HUMAN SERUM-ALBUMIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | LENS PROTEINS | DAMAGE | BIOPHYSICS | DEGRADATION | COMPLICATIONS | STRESS | END-PRODUCTS | BINDING | Protein Aggregates | Cystatins - ultrastructure | Glyoxal - metabolism | Oxidation-Reduction | Glycosylation | Cicer - chemistry | Cystatins - metabolism | Cicer - metabolism | Pyruvaldehyde - metabolism | Plant Proteins - chemistry | Glycation End Products, Advanced - metabolism | Cystatins - chemistry | Lysine - metabolism | Plant Proteins - metabolism | Arginine - metabolism
Journal Article
Amino Acids, ISSN 0939-4451, 1/2015, Volume 47, Issue 1, pp. 135 - 146
Thiol protease inhibitors (cystatins) are implicated in various disease states from cancer to neurodegenerative conditions and immune responses. Cystatins have...
Biochemistry, general | Caprine brain cystatin | Neurobiology | Fluorescence | Life Sciences | Methylglyoxal | Analytical Chemistry | Life Sciences, general | Biochemical Engineering | Proteomics | β-Sheet | Amyloid | Diabetes | FIBRIL FORMATION | PROTEIN | SPONTANEOUSLY HYPERTENSIVE-RATS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCATION | beta-Sheet | GLYOXALASE SYSTEM | DIABETES-MELLITUS | KETONE-BODIES | STEFIN-B | BOVINE SERUM-ALBUMIN | Brain - metabolism | Protein Aggregates | Pyruvaldehyde - metabolism | Animals | Amyloid - metabolism | Goats | Cystatins - chemistry | Protein Binding | Amyloid - chemistry | Cystatins - metabolism | In Vitro Techniques | Type 2 diabetes | Thiols | Protease inhibitors | Proteases | Analysis | Amyloidosis | Alzheimer's disease | Brain | Elevated | Aggregates | Filaments | Dichroism | Amino acids
Biochemistry, general | Caprine brain cystatin | Neurobiology | Fluorescence | Life Sciences | Methylglyoxal | Analytical Chemistry | Life Sciences, general | Biochemical Engineering | Proteomics | β-Sheet | Amyloid | Diabetes | FIBRIL FORMATION | PROTEIN | SPONTANEOUSLY HYPERTENSIVE-RATS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCATION | beta-Sheet | GLYOXALASE SYSTEM | DIABETES-MELLITUS | KETONE-BODIES | STEFIN-B | BOVINE SERUM-ALBUMIN | Brain - metabolism | Protein Aggregates | Pyruvaldehyde - metabolism | Animals | Amyloid - metabolism | Goats | Cystatins - chemistry | Protein Binding | Amyloid - chemistry | Cystatins - metabolism | In Vitro Techniques | Type 2 diabetes | Thiols | Protease inhibitors | Proteases | Analysis | Amyloidosis | Alzheimer's disease | Brain | Elevated | Aggregates | Filaments | Dichroism | Amino acids
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 12/2016, Volume 93, Issue Pt A, pp. 493 - 500
Many protein misfolding diseases in mammalian system are characterised by the accumulation of protein aggregates in amyloid fibrillar forms. Several...
SDS | Gemini surfactant | Goat brain cystatin | CTAB | PREFORMED FIBRILS | ALTERNATIVE CONFORMATIONS | POLYMER SCIENCE | ACID | PROTEIN AGGREGATION | ALZHEIMERS-DISEASE | SERUM-ALBUMIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-SYNUCLEIN | PEPTIDE | FLAVONOID BAICALEIN | BETA | CHEMISTRY, APPLIED | Brain | Animals | Goats | Cystatins - chemistry | Amyloidosis | Brain Chemistry | Surface-Active Agents - chemistry | Amyloid - chemistry | Protein Aggregation, Pathological | Islamic schools | Surface active agents | Health aspects | Proteins | Fluorescence
SDS | Gemini surfactant | Goat brain cystatin | CTAB | PREFORMED FIBRILS | ALTERNATIVE CONFORMATIONS | POLYMER SCIENCE | ACID | PROTEIN AGGREGATION | ALZHEIMERS-DISEASE | SERUM-ALBUMIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-SYNUCLEIN | PEPTIDE | FLAVONOID BAICALEIN | BETA | CHEMISTRY, APPLIED | Brain | Animals | Goats | Cystatins - chemistry | Amyloidosis | Brain Chemistry | Surface-Active Agents - chemistry | Amyloid - chemistry | Protein Aggregation, Pathological | Islamic schools | Surface active agents | Health aspects | Proteins | Fluorescence
Journal Article
Process Biochemistry, ISSN 1359-5113, 06/2017, Volume 57, pp. 105 - 116
Metals such as Cu , Fe , and Zn are major contributors to the biology of a brain in stages of health, aging, and disease because of their unique effects on...
Amyloidosis | Fibrillation | Goat brain cystatin | Low pH | Metal ions | PROTEIN | MECHANISM | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | APOLIPOPROTEIN-E | CELL-DEATH | ENGINEERING, CHEMICAL | AMYLOID-BETA PEPTIDE | IN-VITRO | ZINC-DEFICIENCY | STEFIN-B | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | BRAIN | Zinc compounds | Medical research | Nervous system diseases | Goats | Analysis | Medicine, Experimental
Amyloidosis | Fibrillation | Goat brain cystatin | Low pH | Metal ions | PROTEIN | MECHANISM | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | APOLIPOPROTEIN-E | CELL-DEATH | ENGINEERING, CHEMICAL | AMYLOID-BETA PEPTIDE | IN-VITRO | ZINC-DEFICIENCY | STEFIN-B | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | BRAIN | Zinc compounds | Medical research | Nervous system diseases | Goats | Analysis | Medicine, Experimental
Journal Article
Journal of Molecular Recognition, ISSN 0952-3499, 11/2016, Volume 29, Issue 11, pp. 536 - 543
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 02/2017, Volume 95, pp. 1056 - 1063
ZnO-NPs have been widely used in biomedical fields such as therapeutics, cellular imaging, and drug delivery. However, the risk of exposure of nanoparticles to...
Buffalo heart cystatin | SEM | XRD | ZnO-nanoparticles | TEM | Molten globule | POLYMER SCIENCE | PROTEIN | PARTICLES | MOLTEN GLOBULE STATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TOXICITY | FAILURE | ZINC | CATHEPSINS | DISEASE | HEALTH | CHEMISTRY, APPLIED | ASSOCIATION | Myocardium - chemistry | Nanoparticles - chemistry | Protein Structure, Secondary | Nanoparticles - ultrastructure | Spectrometry, Fluorescence | Anilino Naphthalenesulfonates - chemistry | Thermodynamics | Animals | Zinc Oxide - chemistry | Papain - antagonists & inhibitors | Cystatins - chemistry | Cystatins - isolation & purification | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein Domains | Thiazoles - chemistry | Buffaloes | Papain - chemistry | Nanoparticles | Zinc oxide | Real property | Chemical properties | Valuation | Index Medicus
Buffalo heart cystatin | SEM | XRD | ZnO-nanoparticles | TEM | Molten globule | POLYMER SCIENCE | PROTEIN | PARTICLES | MOLTEN GLOBULE STATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TOXICITY | FAILURE | ZINC | CATHEPSINS | DISEASE | HEALTH | CHEMISTRY, APPLIED | ASSOCIATION | Myocardium - chemistry | Nanoparticles - chemistry | Protein Structure, Secondary | Nanoparticles - ultrastructure | Spectrometry, Fluorescence | Anilino Naphthalenesulfonates - chemistry | Thermodynamics | Animals | Zinc Oxide - chemistry | Papain - antagonists & inhibitors | Cystatins - chemistry | Cystatins - isolation & purification | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein Domains | Thiazoles - chemistry | Buffaloes | Papain - chemistry | Nanoparticles | Zinc oxide | Real property | Chemical properties | Valuation | Index Medicus
Journal Article
BBA - Proteins and Proteomics, ISSN 1570-9639, 09/2018, Volume 1866, Issue 9, pp. 989 - 1000
Hyperglycaemic conditions facilitate the glycation of serum proteins which may have predisposition to aggregation and thus lead to complications. The current...
Aggregation | Chickpea cystatin | Biotoxic | Lymphocytes | DNA | Glycation | HUMAN SERUM-ALBUMIN | GLUCOSE-OXIDASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DNA-DAMAGE | GLOBULAR PROTEINS | INFRARED-SPECTRA | IN-VITRO | BIOPHYSICS | NONENZYMATIC GLYCATION | 1-ANILINO-8-NAPHTHALENE SULFONATE | END-PRODUCTS | METHYLGLYOXAL | Glucose | Analysis | Dextrose | Blood proteins
Aggregation | Chickpea cystatin | Biotoxic | Lymphocytes | DNA | Glycation | HUMAN SERUM-ALBUMIN | GLUCOSE-OXIDASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DNA-DAMAGE | GLOBULAR PROTEINS | INFRARED-SPECTRA | IN-VITRO | BIOPHYSICS | NONENZYMATIC GLYCATION | 1-ANILINO-8-NAPHTHALENE SULFONATE | END-PRODUCTS | METHYLGLYOXAL | Glucose | Analysis | Dextrose | Blood proteins
Journal Article
Current Topics in Medicinal Chemistry, ISSN 1568-0266, 05/2017, Volume 17, Issue 12, p. 1371
The maintenance of health requires successful cell functioning, which in turn depends upon the proper and active conformation of proteins besides other...
Multiple sclerosis | Parkinson's disease | Neurodegenerative diseases | Toxicity | Therapeutic applications | Disorders | Amyotrophic lateral sclerosis | Cures | Agglomeration | Management | Diseases | Proteins | Neurological diseases | Neurotoxicity | Neurodegeneration | Protein folding | Polyphenols | Biomolecules | Amyloid | Drug discovery | Alzheimers disease | Alzheimer's disease | Social impact | Movement disorders
Multiple sclerosis | Parkinson's disease | Neurodegenerative diseases | Toxicity | Therapeutic applications | Disorders | Amyotrophic lateral sclerosis | Cures | Agglomeration | Management | Diseases | Proteins | Neurological diseases | Neurotoxicity | Neurodegeneration | Protein folding | Polyphenols | Biomolecules | Amyloid | Drug discovery | Alzheimers disease | Alzheimer's disease | Social impact | Movement disorders
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 12/2018, Volume 120, Issue Pt A, pp. 45 - 58
Amyloid fibrils are highly ordered protein assemblies known to contribute to the pathology of a variety of genetic and aging-associated diseases. Here, we have...
SDS | Docking | Amyloid | Cytotoxcity | Rutin | Lysozyme | Genotoxcity | OXIDATIVE STRESS | POLYMER SCIENCE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | GREEN TEA | POLYPHENOLS | INHIBITION | METABOLISM | TEA CATECHINS | CHEMISTRY, APPLIED | EGG-WHITE LYSOZYME | AMYLOID FIBRIL FORMATION | HEN LYSOZYME | Protein Aggregates | Muramidase - chemistry | Humans | Amyloid - chemistry | Animals | Sodium Dodecyl Sulfate - analogs & derivatives | Sodium Dodecyl Sulfate - chemistry | Chickens | Surface Properties | Cytotoxins - chemistry | Cell Line, Tumor | Rutin - chemistry | Molecular Docking Simulation | Surface-Active Agents - chemistry | Medical research | Surface active agents | Analysis | Fluorescence | Medicine, Experimental | College teachers
SDS | Docking | Amyloid | Cytotoxcity | Rutin | Lysozyme | Genotoxcity | OXIDATIVE STRESS | POLYMER SCIENCE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | GREEN TEA | POLYPHENOLS | INHIBITION | METABOLISM | TEA CATECHINS | CHEMISTRY, APPLIED | EGG-WHITE LYSOZYME | AMYLOID FIBRIL FORMATION | HEN LYSOZYME | Protein Aggregates | Muramidase - chemistry | Humans | Amyloid - chemistry | Animals | Sodium Dodecyl Sulfate - analogs & derivatives | Sodium Dodecyl Sulfate - chemistry | Chickens | Surface Properties | Cytotoxins - chemistry | Cell Line, Tumor | Rutin - chemistry | Molecular Docking Simulation | Surface-Active Agents - chemistry | Medical research | Surface active agents | Analysis | Fluorescence | Medicine, Experimental | College teachers
Journal Article
Journal of Fluorescence, ISSN 1053-0509, 7/2014, Volume 24, Issue 4, pp. 1107 - 1117
The study shows the effect of nonenzymatic glycation on conformation and inhibitory activity of chick pea cystatin (CPC). CPC was incubated with different...
Biochemistry, general | Biotechnology | Analytical Chemistry | Anti-papain | Biomedicine | Maillard reaction | Biophysics and Biological Physics | AGEs | Chick pea cystatin | Biomedicine general | Glycation | GLYCERALDEHYDE | CHEMISTRY, ANALYTICAL | PROTEIN | HUMAN SERUM-ALBUMIN | LYSINE | BIOCHEMICAL RESEARCH METHODS | DISEASES | INHIBITORS | ENDPRODUCTS | END-PRODUCTS | IMMUNOGLOBULIN-G | Cystatins - chemistry | Cystatins - isolation & purification | Spectrometry, Fluorescence | Glycosylation | Seeds - chemistry | Cicer - chemistry | Spectrophotometry, Ultraviolet | Glucose metabolism | Tryptophan | Fluorescence | Papain | Glucose | Fructose | Dextrose | Proteins | Spectroscopy | Ribose | Pentose | Chicks | Age | Sugars
Biochemistry, general | Biotechnology | Analytical Chemistry | Anti-papain | Biomedicine | Maillard reaction | Biophysics and Biological Physics | AGEs | Chick pea cystatin | Biomedicine general | Glycation | GLYCERALDEHYDE | CHEMISTRY, ANALYTICAL | PROTEIN | HUMAN SERUM-ALBUMIN | LYSINE | BIOCHEMICAL RESEARCH METHODS | DISEASES | INHIBITORS | ENDPRODUCTS | END-PRODUCTS | IMMUNOGLOBULIN-G | Cystatins - chemistry | Cystatins - isolation & purification | Spectrometry, Fluorescence | Glycosylation | Seeds - chemistry | Cicer - chemistry | Spectrophotometry, Ultraviolet | Glucose metabolism | Tryptophan | Fluorescence | Papain | Glucose | Fructose | Dextrose | Proteins | Spectroscopy | Ribose | Pentose | Chicks | Age | Sugars
Journal Article