PubMed:8376413 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":62},"obj":"Sentence"},{"id":"T2","span":{"begin":63,"end":199},"obj":"Sentence"},{"id":"T3","span":{"begin":200,"end":321},"obj":"Sentence"},{"id":"T4","span":{"begin":322,"end":444},"obj":"Sentence"},{"id":"T5","span":{"begin":445,"end":529},"obj":"Sentence"},{"id":"T6","span":{"begin":530,"end":613},"obj":"Sentence"},{"id":"T7","span":{"begin":614,"end":755},"obj":"Sentence"},{"id":"T8","span":{"begin":756,"end":841},"obj":"Sentence"},{"id":"T9","span":{"begin":842,"end":963},"obj":"Sentence"},{"id":"T10","span":{"begin":964,"end":1219},"obj":"Sentence"},{"id":"T11","span":{"begin":1220,"end":1345},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":62},"obj":"Sentence"},{"id":"T2","span":{"begin":63,"end":199},"obj":"Sentence"},{"id":"T3","span":{"begin":200,"end":321},"obj":"Sentence"},{"id":"T4","span":{"begin":322,"end":444},"obj":"Sentence"},{"id":"T5","span":{"begin":445,"end":529},"obj":"Sentence"},{"id":"T6","span":{"begin":530,"end":613},"obj":"Sentence"},{"id":"T7","span":{"begin":614,"end":755},"obj":"Sentence"},{"id":"T8","span":{"begin":756,"end":841},"obj":"Sentence"},{"id":"T9","span":{"begin":842,"end":963},"obj":"Sentence"},{"id":"T10","span":{"begin":964,"end":1219},"obj":"Sentence"},{"id":"T11","span":{"begin":1220,"end":1345},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structural prerequisites for serum amyloid A fibril formation.\nMost studies of experimental amyloid A protein (AA) amyloidosis in mice have been performed in type A mice with BALB/c as the prototype. In these mice the products of two genes, SAA1 and SAA2, are the major apo-SAA isoforms on high density lipoprotein (HDL). Of these two isoforms, that differ at nine amino acids, only apo-SAA2 is rapidly cleared and deposited as amyloid fibrils. No mouse strain has ever been shown to be completely resistant to amyloid induction. We have found the CE/J mouse strain to be exceedingly resistant to amyloidogenesis. Data indicate that this resistance is not due to a lack of apo-SAA synthesis but rather resides in the unique apo-SAA isoform in this strain. CE/J mice have a single major apo-SAA isoform (pI 6.15) the product of a single gene. This is a hybrid molecule with features of both apo-SAA1 and apo-SAA2, differing from the latter at only six amino acids. When CD studies were performed to explore the structural relationship of this isoform to apo-SAA1 and apo-SAA2, we found that when bound to heparan sulfate proteoglycan the CE/J pI 6.15 isoform fails to undergo the beta-sheet folding typical for apo-SAA2. This evidence suggests that the folding effect of heparan sulfate proteoglycan on apo-SAA2 is important in amyloid formation."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1104,"end":1119},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"T2","span":{"begin":1270,"end":1285},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"Structural prerequisites for serum amyloid A fibril formation.\nMost studies of experimental amyloid A protein (AA) amyloidosis in mice have been performed in type A mice with BALB/c as the prototype. In these mice the products of two genes, SAA1 and SAA2, are the major apo-SAA isoforms on high density lipoprotein (HDL). Of these two isoforms, that differ at nine amino acids, only apo-SAA2 is rapidly cleared and deposited as amyloid fibrils. No mouse strain has ever been shown to be completely resistant to amyloid induction. We have found the CE/J mouse strain to be exceedingly resistant to amyloidogenesis. Data indicate that this resistance is not due to a lack of apo-SAA synthesis but rather resides in the unique apo-SAA isoform in this strain. CE/J mice have a single major apo-SAA isoform (pI 6.15) the product of a single gene. This is a hybrid molecule with features of both apo-SAA1 and apo-SAA2, differing from the latter at only six amino acids. When CD studies were performed to explore the structural relationship of this isoform to apo-SAA1 and apo-SAA2, we found that when bound to heparan sulfate proteoglycan the CE/J pI 6.15 isoform fails to undergo the beta-sheet folding typical for apo-SAA2. This evidence suggests that the folding effect of heparan sulfate proteoglycan on apo-SAA2 is important in amyloid formation."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":35,"end":42},"obj":"Disease"},{"id":"T2","span":{"begin":92,"end":99},"obj":"Disease"},{"id":"T3","span":{"begin":110,"end":126},"obj":"Disease"},{"id":"T4","span":{"begin":428,"end":435},"obj":"Disease"},{"id":"T5","span":{"begin":511,"end":518},"obj":"Disease"},{"id":"T6","span":{"begin":1327,"end":1334},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0019065"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0019065"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0019439"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0019065"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0019065"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0019065"}],"text":"Structural prerequisites for serum amyloid A fibril formation.\nMost studies of experimental amyloid A protein (AA) amyloidosis in mice have been performed in type A mice with BALB/c as the prototype. In these mice the products of two genes, SAA1 and SAA2, are the major apo-SAA isoforms on high density lipoprotein (HDL). Of these two isoforms, that differ at nine amino acids, only apo-SAA2 is rapidly cleared and deposited as amyloid fibrils. No mouse strain has ever been shown to be completely resistant to amyloid induction. We have found the CE/J mouse strain to be exceedingly resistant to amyloidogenesis. Data indicate that this resistance is not due to a lack of apo-SAA synthesis but rather resides in the unique apo-SAA isoform in this strain. CE/J mice have a single major apo-SAA isoform (pI 6.15) the product of a single gene. This is a hybrid molecule with features of both apo-SAA1 and apo-SAA2, differing from the latter at only six amino acids. When CD studies were performed to explore the structural relationship of this isoform to apo-SAA1 and apo-SAA2, we found that when bound to heparan sulfate proteoglycan the CE/J pI 6.15 isoform fails to undergo the beta-sheet folding typical for apo-SAA2. This evidence suggests that the folding effect of heparan sulfate proteoglycan on apo-SAA2 is important in amyloid formation."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":110,"end":126},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:4000041"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Structural prerequisites for serum amyloid A fibril formation.\nMost studies of experimental amyloid A protein (AA) amyloidosis in mice have been performed in type A mice with BALB/c as the prototype. In these mice the products of two genes, SAA1 and SAA2, are the major apo-SAA isoforms on high density lipoprotein (HDL). Of these two isoforms, that differ at nine amino acids, only apo-SAA2 is rapidly cleared and deposited as amyloid fibrils. No mouse strain has ever been shown to be completely resistant to amyloid induction. We have found the CE/J mouse strain to be exceedingly resistant to amyloidogenesis. Data indicate that this resistance is not due to a lack of apo-SAA synthesis but rather resides in the unique apo-SAA isoform in this strain. CE/J mice have a single major apo-SAA isoform (pI 6.15) the product of a single gene. This is a hybrid molecule with features of both apo-SAA1 and apo-SAA2, differing from the latter at only six amino acids. When CD studies were performed to explore the structural relationship of this isoform to apo-SAA1 and apo-SAA2, we found that when bound to heparan sulfate proteoglycan the CE/J pI 6.15 isoform fails to undergo the beta-sheet folding typical for apo-SAA2. This evidence suggests that the folding effect of heparan sulfate proteoglycan on apo-SAA2 is important in amyloid formation."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":130,"end":134},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":165,"end":169},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":209,"end":213},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":448,"end":453},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":553,"end":558},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":761,"end":765},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10088"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10088"},{"id":"A4","pred":"db_id","subj":"T4","obj":"10088"},{"id":"A5","pred":"db_id","subj":"T4","obj":"10090"},{"id":"A6","pred":"db_id","subj":"T6","obj":"10088"},{"id":"A7","pred":"db_id","subj":"T6","obj":"10090"},{"id":"A8","pred":"db_id","subj":"T8","obj":"10088"}],"text":"Structural prerequisites for serum amyloid A fibril formation.\nMost studies of experimental amyloid A protein (AA) amyloidosis in mice have been performed in type A mice with BALB/c as the prototype. In these mice the products of two genes, SAA1 and SAA2, are the major apo-SAA isoforms on high density lipoprotein (HDL). Of these two isoforms, that differ at nine amino acids, only apo-SAA2 is rapidly cleared and deposited as amyloid fibrils. No mouse strain has ever been shown to be completely resistant to amyloid induction. We have found the CE/J mouse strain to be exceedingly resistant to amyloidogenesis. Data indicate that this resistance is not due to a lack of apo-SAA synthesis but rather resides in the unique apo-SAA isoform in this strain. CE/J mice have a single major apo-SAA isoform (pI 6.15) the product of a single gene. This is a hybrid molecule with features of both apo-SAA1 and apo-SAA2, differing from the latter at only six amino acids. When CD studies were performed to explore the structural relationship of this isoform to apo-SAA1 and apo-SAA2, we found that when bound to heparan sulfate proteoglycan the CE/J pI 6.15 isoform fails to undergo the beta-sheet folding typical for apo-SAA2. This evidence suggests that the folding effect of heparan sulfate proteoglycan on apo-SAA2 is important in amyloid formation."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":45,"end":51},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0099512"}],"text":"Structural prerequisites for serum amyloid A fibril formation.\nMost studies of experimental amyloid A protein (AA) amyloidosis in mice have been performed in type A mice with BALB/c as the prototype. In these mice the products of two genes, SAA1 and SAA2, are the major apo-SAA isoforms on high density lipoprotein (HDL). Of these two isoforms, that differ at nine amino acids, only apo-SAA2 is rapidly cleared and deposited as amyloid fibrils. No mouse strain has ever been shown to be completely resistant to amyloid induction. We have found the CE/J mouse strain to be exceedingly resistant to amyloidogenesis. Data indicate that this resistance is not due to a lack of apo-SAA synthesis but rather resides in the unique apo-SAA isoform in this strain. CE/J mice have a single major apo-SAA isoform (pI 6.15) the product of a single gene. This is a hybrid molecule with features of both apo-SAA1 and apo-SAA2, differing from the latter at only six amino acids. When CD studies were performed to explore the structural relationship of this isoform to apo-SAA1 and apo-SAA2, we found that when bound to heparan sulfate proteoglycan the CE/J pI 6.15 isoform fails to undergo the beta-sheet folding typical for apo-SAA2. This evidence suggests that the folding effect of heparan sulfate proteoglycan on apo-SAA2 is important in amyloid formation."}