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Amino Acids, ISSN 0939-4451, 11/2011, Volume 41, Issue 5, pp. 1233 - 1245
The G170R variant of the alanine:glyoxylate aminotransferase (AGT) is the most common pathogenic allele associated to primary hyperoxaluria type I (PH1),... 
Life Sciences | Biochemistry, general | Analytical Chemistry | Life Sciences, general | Molecular chaperones | Neurobiology | Proteomics | Biochemical Engineering | Alanine:glyoxylate aminotransferase | Partially folded states | Protein kinetic stability | Primary hyperoxaluria type 1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DIFFERENTIAL SCANNING CALORIMETRY | TRANSITION-STATE | IMPORT | MOLTEN GLOBULE | ASPARTATE-AMINOTRANSFERASE | ALANINEGLYOXYLATE AMINOTRANSFERASE | ALPHA-LACTALBUMIN | ALANINE-GLYOXYLATE AMINOTRANSFERASE | HUMAN-LIVER ALANINE | Cell Line | HSC70 Heat-Shock Proteins - genetics | Protein Unfolding | Transaminases - genetics | HSC70 Heat-Shock Proteins - metabolism | Humans | Mitochondrial Proteins - genetics | Transaminases - chemistry | Hyperoxaluria, Primary - enzymology | Protein Transport | Hyperoxaluria, Primary - genetics | HSC70 Heat-Shock Proteins - chemistry | Mitochondrial Proteins - metabolism | Hyperoxaluria, Primary - metabolism | Mitochondrial Proteins - chemistry | Transaminases - metabolism | HSP90 Heat-Shock Proteins - chemistry | HSP90 Heat-Shock Proteins - metabolism | Protein Binding | HSP90 Heat-Shock Proteins - genetics | Kinetics | Phosphates | Proteins | Magneto-electric machines | Analysis | Escherichia coli | Heat shock proteins | Amino acids | Machinery | Trapping | Stability | Reaction kinetics | Folding
Journal Article
Journal of biomolecular NMR, ISSN 0925-2738, 2005, Volume 33, Issue 3, pp. 175 - 186
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 03/2009, Volume 74, Issue 4, pp. 895 - 904
In nature, some proteins partially unfold under specific environmental conditions. These unfolded states typically consist of a large ensemble of... 
ensemble selection | partially unfolded states | photoactive yellow protein | NMR | Partially unfolded states | Ensemble selection | Photoactive yellow protein
Journal Article
Pharmaceutical Research, ISSN 0724-8741, 11/2003, Volume 20, Issue 11, pp. 1721 - 1729
Purpose. To study the effect of solution conditions on the structural conformation of recombinant human interferon-α2a (IFNα2a) to investigate its tendency to... 
Biochemistry, general | Biomedical Engineering | Biomedicine | solution conformation | Pharmacy | fluorescence quenching | Medical Law | partially unfolded states | aggregation | Pharmacology/Toxicology | interferon α2a | Aggregation | Interferon α2a | Partially unfolded states | Solution conformation | Fluorescence quenching
Journal Article
Journal of Biomolecular NMR, ISSN 0925-2738, 11/2005, Volume 33, Issue 3, pp. 175 - 186
Journal Article
PHARMACEUTICAL RESEARCH, ISSN 0724-8741, 11/2003, Volume 20, Issue 11, pp. 1721 - 1729
Purpose. To study the effect of solution conditions on the structural conformation of recombinant human interferon-alpha2a (IFNalpha2a) to investigate its... 
solution conformation | MOLTEN GLOBULE STATE | fluorescence quenching | LYSOZYME | aggregation | CHEMISTRY, MULTIDISCIPLINARY | interferon alpha 2a | FLUORESCENCE | SPECTROSCOPY | partially unfolded states | INTERMEDIATE | PHARMACOLOGY & PHARMACY | SECONDARY STRUCTURE | TRANSITIONS
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 2009, Volume 5, Issue 1, pp. 15 - 22
Journal Article
JOURNAL OF MOLECULAR BIOLOGY, ISSN 0022-2836, 03/1995, Volume 247, Issue 3, pp. 501 - 520
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 03/2009, Volume 386, Issue 5, pp. 1312 - 1326
Although numerous measurements of amyloid assembly of different proteins under distinct conditions in vitro have been performed, the molecular mechanisms... 
proline isomerisation | aggregation kinetics | partially unfolded state | de novo amyloid assembly | dimer
Journal Article
Journal Article
Current Opinion in Structural Biology, ISSN 0959-440X, 02/2007, Volume 17, Issue 1, pp. 15 - 20
Journal Article
JOURNAL OF MOLECULAR BIOLOGY, ISSN 0022-2836, 03/2009, Volume 386, Issue 5, pp. 1312 - 1326
Although numerous measurements of amyloid assembly of different proteins under distinct conditions in vitro have been performed, the molecular mechanisms... 
FIBRIL FORMATION | HUMAN-DISEASE | aggregation kinetics | partially unfolded state | PROTEIN AGGREGATION | FORMATION IN-VITRO | BIOCHEMISTRY & MOLECULAR BIOLOGY | dimer | HUMAN BETA-2-MICROGLOBULIN REVEALS | de novo amyloid assembly | proline isomerisation | ANTIBODY DOMAIN | PROLYL ISOMERIZATION | PHYSIOLOGICAL CONDITIONS | RESIDUES | NATIVE-STATE
Journal Article