ovalbumin and Amyloidosis

ovalbumin has been researched along with Amyloidosis* in 7 studies

Reviews

2 review(s) available for ovalbumin and Amyloidosis

Article	Year
Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study. Biomacromolecules, 2022, 09-12, Volume: 23, Issue:9 Highly ordered, straight amyloid fibrils readily lend themselves to structure determination techniques and have therefore been extensively characterized. However, the less ordered curly fibrils remain relatively understudied, and the structural organization underlying their specific characteristics remains poorly understood. We found that the exemplary curly fibril-forming protein ovalbumin contains multiple aggregation prone regions (APRs) that form straight fibrils when isolated as peptides or when excised from the full-length protein through hydrolysis. In the context of the intact full-length protein, however, the regions separating the APRs facilitate curly fibril formation. In fact, a meta-analysis of previously reported curly fibril-forming proteins shows that their inter-APRs are significantly longer and more hydrophobic when compared to straight fibril-forming proteins, suggesting that they may cause strain in the amyloid state. Hence, inter-APRs driving curly fibril formation may not only apply to our model protein but rather constitute a more general mechanism. Topics: Amyloid; Amyloidosis; Humans; Hydrophobic and Hydrophilic Interactions; Ovalbumin; Peptides	2022
Glycoproteins: their biochemistry, biology and role in human disease. The New England journal of medicine, 1969, Nov-06, Volume: 281, Issue:19 Topics: Amyloidosis; Animals; Antigens; Basement Membrane; Blood Group Antigens; Brain Chemistry; Carbohydrates; Cell Membrane; Collagen; Connective Tissue; Cystic Fibrosis; Diabetic Angiopathies; Enzymes; gamma-Globulins; Glycoproteins; Hormones; Humans; Mucins; Mucous Membrane; Neoplasms; Ovalbumin	1969

Article

Year

Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study.

Biomacromolecules, 2022, 09-12, Volume: 23, Issue:9

Highly ordered, straight amyloid fibrils readily lend themselves to structure determination techniques and have therefore been extensively characterized. However, the less ordered curly fibrils remain relatively understudied, and the structural organization underlying their specific characteristics remains poorly understood. We found that the exemplary curly fibril-forming protein ovalbumin contains multiple aggregation prone regions (APRs) that form straight fibrils when isolated as peptides or when excised from the full-length protein through hydrolysis. In the context of the intact full-length protein, however, the regions separating the APRs facilitate curly fibril formation. In fact, a meta-analysis of previously reported curly fibril-forming proteins shows that their inter-APRs are significantly longer and more hydrophobic when compared to straight fibril-forming proteins, suggesting that they may cause strain in the amyloid state. Hence, inter-APRs driving curly fibril formation may not only apply to our model protein but rather constitute a more general mechanism.

Topics: Amyloid; Amyloidosis; Humans; Hydrophobic and Hydrophilic Interactions; Ovalbumin; Peptides

2022

Glycoproteins: their biochemistry, biology and role in human disease.

The New England journal of medicine, 1969, Nov-06, Volume: 281, Issue:19

Topics: Amyloidosis; Animals; Antigens; Basement Membrane; Blood Group Antigens; Brain Chemistry; Carbohydrates; Cell Membrane; Collagen; Connective Tissue; Cystic Fibrosis; Diabetic Angiopathies; Enzymes; gamma-Globulins; Glycoproteins; Hormones; Humans; Mucins; Mucous Membrane; Neoplasms; Ovalbumin

1969

Other Studies

5 other study(ies) available for ovalbumin and Amyloidosis

Article	Year
[Antigen-induced development of amyloidosis in mice]. Biulleten' eksperimental'noi biologii i meditsiny, 1972, Volume: 73, Issue:8 Topics: Acid Phosphatase; Alkaline Phosphatase; Amyloidosis; Animals; Antigens; Beta-Globulins; Caseins; gamma-Globulins; Male; Mice; Ovalbumin; Serum Albumin; Serum Albumin, Bovine	1972
[Production of amyloidosis in mice in conditions of stimulation and inhibition of immunogenesis]. Biulleten' eksperimental'noi biologii i meditsiny, 1972, Volume: 73, Issue:9 Topics: Amyloidosis; Animals; Antibody Formation; Antigens; Fluorescent Antibody Technique; Freund's Adjuvant; Hemagglutination Tests; Immune Tolerance; Immunodiffusion; Male; Mice; Mice, Inbred BALB C; Ovalbumin	1972
[Induction of amyloidosis in mice using an adjuvant]. Arkhiv patologii, 1971, Volume: 33, Issue:9 Topics: Acid Phosphatase; Amyloidosis; Animals; Antigens; Caseins; Fibrinogen; Freund's Adjuvant; Humans; L-Lactate Dehydrogenase; Mice; Mice, Inbred Strains; Ovalbumin; Serum Albumin	1971
[Amyloidosis in mice under conditions of immunization with 2 antigens]. Biulleten' eksperimental'noi biologii i meditsiny, 1970, Volume: 69, Issue:5 Topics: Acid Phosphatase; Amyloidosis; Animals; Antigens; Caseins; Hypersensitivity; Male; Mice; Ovalbumin; Serum Albumin	1970
[Nonspecific factor stimulating amyloidogenesis in mice]. Arkhiv patologii, 1970, Volume: 32, Issue:10 Topics: Amyloidosis; Animals; Antigens; Caseins; Immune Sera; Male; Mice; Ovalbumin; Spleen	1970