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PubMed:25538238 JSONTXT 39 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-105 Sentence denotes Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans.
T2 106-328 Sentence denotes Amyloid light chain (AL) amyloidosis is a protein misfolding disease where immunoglobulin light chains sample partially folded states that lead to misfolding and amyloid formation, resulting in organ dysfunction and death.
T3 329-521 Sentence denotes In vivo, amyloid deposits are found in the extracellular space and involve a variety of accessory molecules, such as glycosaminoglycans, one of the main components of the extracellular matrix.
T4 522-638 Sentence denotes Glycosaminoglycans are a group of negatively charged heteropolysaccharides composed of repeating disaccharide units.
T5 639-792 Sentence denotes In this study, we investigated the effect of glycosaminoglycans on the kinetics of amyloid fibril formation of three AL cardiac amyloidosis light chains.
T6 793-896 Sentence denotes These proteins have similar thermodynamic stability but exhibit different kinetics of fibril formation.
T7 897-995 Sentence denotes We also studied single restorative and reciprocal mutants and wild type germ line control protein.
T8 996-1202 Sentence denotes We found that the type of glycosaminoglycan has a different effect on the kinetics of fibril formation, and this effect seems to be associated with the natural propensity of each AL protein to form fibrils.
T9 1203-1414 Sentence denotes Heparan sulfate accelerated AL-12, AL-09, κI Y87H, and AL-103 H92D fibril formation; delayed fibril formation for AL-103; and did not promote any fibril formation for AL-12 R65S, AL-103 delP95aIns, or κI O18/O8.
T10 1415-1518 Sentence denotes Chondroitin sulfate A, on the other hand, showed a strong fibril formation inhibition for all proteins.
T11 1519-1890 Sentence denotes We propose that heparan sulfate facilitates the formation of transient amyloidogenic conformations of AL light chains, thereby promoting amyloid formation, whereas chondroitin sulfate A kinetically traps partially unfolded intermediates, and further fibril elongation into fibrils is inhibited, resulting in formation/accumulation of oligomeric/protofibrillar aggregates.