PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32916822-7 2020 GM1 has been shown to induce specific changes in the spatial organization of Abeta, which lead to enhanced peptide accumulation and deleterious effect especially on neuronal membranes containing clusters of this ganglioside. Gangliosides 212-223 amyloid beta precursor protein Homo sapiens 77-82 32142821-2 2020 Accumulating evidence, both in vivo and in vitro, suggests that the binding of Abeta to gangliosides, especially monosialoganglioside GM1, plays an important role in the aggregation of Abeta. Gangliosides 88-100 amyloid beta precursor protein Homo sapiens 79-84 32142821-2 2020 Accumulating evidence, both in vivo and in vitro, suggests that the binding of Abeta to gangliosides, especially monosialoganglioside GM1, plays an important role in the aggregation of Abeta. Gangliosides 88-100 amyloid beta precursor protein Homo sapiens 185-190 32142821-3 2020 This review summarizes the molecular details of the binding of Abeta to ganglioside-containing membranes and subsequent structural changes, as revealed by liposomal and cellular studies. Gangliosides 72-83 amyloid beta precursor protein Homo sapiens 63-68 30257562-3 2018 According to evidence from spectroscopic studies, ganglioside clusters are key to the fibrillization process of Abeta. Gangliosides 50-61 amyloid beta precursor protein Homo sapiens 112-117 32567070-9 2020 Moreover, lipid rafts and especially gangliosides play a critical role in the formation and toxicity of Abeta oligomers. Gangliosides 37-49 amyloid beta precursor protein Homo sapiens 104-109 31474736-2 2019 A toxic fibril formation of Abeta is known to be enhanced on the ganglioside-rich lipid membrane containing some amounts of cholesterol and sphingomyelin. Gangliosides 65-76 amyloid beta precursor protein Homo sapiens 28-33 31474736-3 2019 This ganglioside-rich membrane is supposed to provide a hydrophobic environment that promotes the formation of Abeta fibrils. Gangliosides 5-16 amyloid beta precursor protein Homo sapiens 111-116 30457145-1 2018 Alzheimer"s disease (AD) is characterized by the overproduction of the amyloid-beta peptide (Abeta) which forms fibrils under the influence of raft microdomains containing the ganglioside GM1. Gangliosides 176-187 amyloid beta precursor protein Homo sapiens 93-98 29747822-0 2018 Ganglioside-Mediated Assembly of Amyloid beta-Protein: Roles in Alzheimer"s Disease. Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 33-45 30018137-2 2018 Abeta accumulates at nanoclusters enriched in neuronal lipids called gangliosides in the presynaptic neuronal membrane, and the resulting oligomeric and/or fibrous forms accelerate the development of Alzheimer"s disease. Gangliosides 69-81 amyloid beta precursor protein Homo sapiens 0-5 30018137-6 2018 We also found that the fibrils obtained at GM1-rich nanoclusters were generated from turn Abeta40 Our findings indicate that Abeta generally self-assembles into antiparallel beta-structures but can also form protofibrils with parallel beta-sheets by interacting with ganglioside-bound Abeta. Gangliosides 267-278 amyloid beta precursor protein Homo sapiens 90-95 30018137-6 2018 We also found that the fibrils obtained at GM1-rich nanoclusters were generated from turn Abeta40 Our findings indicate that Abeta generally self-assembles into antiparallel beta-structures but can also form protofibrils with parallel beta-sheets by interacting with ganglioside-bound Abeta. Gangliosides 267-278 amyloid beta precursor protein Homo sapiens 125-130 30018137-7 2018 We concluded that by promoting the formation of parallel beta-sheets, highly ganglioside-enriched nanoclusters help accelerate the elongation of Abeta fibrils. Gangliosides 77-88 amyloid beta precursor protein Homo sapiens 145-150 30018137-8 2018 These results advance our understanding of ganglioside-induced Abeta fibril formation in neuronal membranes and may help inform the development of additional therapies for Alzheimer"s disease. Gangliosides 43-54 amyloid beta precursor protein Homo sapiens 63-68 29747822-3 2018 In 1995, ganglioside-bound Abeta (GAbeta), with unique molecular characteristics, including its altered immunoreactivity and its conspicuous ability to accelerate Abeta assembly, was discovered in an autopsied brain showing early pathological changes of AD. Gangliosides 9-20 amyloid beta precursor protein Homo sapiens 27-32 29747822-6 2018 First, the conformational changes of Abeta from a random coil to an alpha-helix, and then to a beta-sheet in the presence of ganglioside were validated by several techniques. Gangliosides 125-136 amyloid beta precursor protein Homo sapiens 37-42 29747822-8 2018 Third, it was found that the Abeta binding to ganglioside to form GAbeta occurs under limited conditions, which were provided by the lipid environment surrounding ganglioside. Gangliosides 46-57 amyloid beta precursor protein Homo sapiens 29-34 29747822-8 2018 Third, it was found that the Abeta binding to ganglioside to form GAbeta occurs under limited conditions, which were provided by the lipid environment surrounding ganglioside. Gangliosides 163-174 amyloid beta precursor protein Homo sapiens 29-34 29747822-10 2018 In this chapter, further progress of the study of ganglioside-mediated Abeta assembly, especially from the aspects of physicochemistry, structural biology, and neuropathology, is reviewed. Gangliosides 50-61 amyloid beta precursor protein Homo sapiens 71-76 23688073-1 2013 Accumulation and fibril formation of amyloid beta (Abeta) peptides onto a ganglioside-rich lipid membrane is a cause of neuro-disturbance diseases. Gangliosides 74-85 amyloid beta precursor protein Homo sapiens 51-56 27373967-1 2016 Evidence has suggested that ganglioside abnormalities may be linked to the proteolytic processing of amyloid precursor protein (APP) in Alzheimer"s disease (AD) and that pharmacological inhibition of ganglioside synthesis may reduce amyloid beta-peptide (Abeta) production. Gangliosides 28-39 amyloid beta precursor protein Homo sapiens 101-126 25406316-2 2015 Abeta peptides were previously considered to interact specifically with ganglioside-containing membranes. Gangliosides 72-83 amyloid beta precursor protein Homo sapiens 0-5 26149926-8 2015 Upon interaction with the lipid raft components, such as cholesterol, gangliosides and phospholipids, Abeta can aggregate on the cell membrane and thereby disrupt it, perhaps by forming channel-like pores. Gangliosides 70-82 amyloid beta precursor protein Homo sapiens 102-107 25399921-5 2014 We have proposed that the binding of Abeta to membranes with ganglioside clusters plays an important role in the abnormal aggregation of Abeta. Gangliosides 61-72 amyloid beta precursor protein Homo sapiens 37-42 25399921-5 2014 We have proposed that the binding of Abeta to membranes with ganglioside clusters plays an important role in the abnormal aggregation of Abeta. Gangliosides 61-72 amyloid beta precursor protein Homo sapiens 137-142 25399921-9 2014 Thus, our ganglioside cluster-mediated amyloidogenesis hypothesis explains the immunity of rodents from cerebral Abeta amyloid deposition, strengthening the importance of ganglioside clusters as a platform of abnormal Abeta deposition in the pathology of AD. Gangliosides 10-21 amyloid beta precursor protein Homo sapiens 113-118 25399921-9 2014 Thus, our ganglioside cluster-mediated amyloidogenesis hypothesis explains the immunity of rodents from cerebral Abeta amyloid deposition, strengthening the importance of ganglioside clusters as a platform of abnormal Abeta deposition in the pathology of AD. Gangliosides 10-21 amyloid beta precursor protein Homo sapiens 218-223 25399921-9 2014 Thus, our ganglioside cluster-mediated amyloidogenesis hypothesis explains the immunity of rodents from cerebral Abeta amyloid deposition, strengthening the importance of ganglioside clusters as a platform of abnormal Abeta deposition in the pathology of AD. Gangliosides 171-182 amyloid beta precursor protein Homo sapiens 218-223 24995708-5 2014 The purified PIB-binding site comprises a distinct, highly insoluble subfraction of the Abeta in AD brain with low buoyant density because of the sodium dodecyl sulfate-resistant association with a limited subset of brain proteins and lipids with physical properties similar to lipid rafts and to a ganglioside:Abeta complex in AD and Down syndrome brain. Gangliosides 299-310 amyloid beta precursor protein Homo sapiens 88-93 27933798-3 2016 The physiological role of the Abeta interaction with the ganglioside GM1 is still unclear. Gangliosides 57-68 amyloid beta precursor protein Homo sapiens 30-35 27352802-6 2016 Moreover, alpha-synuclein (Parkinson) and Abeta peptide (Alzheimer) did no longer form Ca(2+)-permeable pores in presence of drugs that target either cholesterol or ganglioside or both membrane lipids. Gangliosides 165-176 amyloid beta precursor protein Homo sapiens 42-47 25140899-5 2014 By modulating the amino acid sequence of alpha-synuclein at only two positions in which we introduced a pair of histidine residues found in Abeta, we created a chimeric alpha-synuclein/Abeta peptide with extended ganglioside-binding properties. Gangliosides 213-224 amyloid beta precursor protein Homo sapiens 140-145 25140899-5 2014 By modulating the amino acid sequence of alpha-synuclein at only two positions in which we introduced a pair of histidine residues found in Abeta, we created a chimeric alpha-synuclein/Abeta peptide with extended ganglioside-binding properties. Gangliosides 213-224 amyloid beta precursor protein Homo sapiens 185-190 22947931-7 2012 Whereas pore formation by freshly dissolved Abeta(1-40) is weakly observed in the absence of gangliosides, fiber-dependent membrane fragmentation can only be observed in their presence. Gangliosides 93-105 amyloid beta precursor protein Homo sapiens 44-49 22470521-7 2012 The first mechanism directly targets the enzymatic activity of GD3S: Upon binding of Abeta to the ganglioside GM3, the immediate substrate of the GD3S, enzymatic turnover of GM3 by GD3S was strongly reduced. Gangliosides 98-109 amyloid beta precursor protein Homo sapiens 85-90 22470521-13 2012 GM3 decreased, whereas the ganglioside GD3, the GD3S product, increased Abeta production, resulting in a regulatory feedback cycle, directly linking ganglioside metabolism with APP processing and Abeta generation. Gangliosides 27-38 amyloid beta precursor protein Homo sapiens 72-77 22470521-13 2012 GM3 decreased, whereas the ganglioside GD3, the GD3S product, increased Abeta production, resulting in a regulatory feedback cycle, directly linking ganglioside metabolism with APP processing and Abeta generation. Gangliosides 27-38 amyloid beta precursor protein Homo sapiens 196-201 20831659-0 2011 Ganglioside-mediated aggregation of amyloid beta-proteins (Abeta): comparison between Abeta-(1-42) and Abeta-(1-40). Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 86-91 21682276-3 2011 We have proposed that ganglioside clusters in lipid rafts mediate the formation of amyloid fibrils by Abeta, the toxicity and physicochemical properties of which are different from those of amyloids formed in solution. Gangliosides 22-33 amyloid beta precursor protein Homo sapiens 102-107 21214549-2 2011 A body of evidence is growing to suggest that Abeta binds to ganglioside on neuronal membranes, and then, is converted to an endogenous seed with an altered conformation (ganglioside-bound Abeta, GAbeta) for amyloid fibril formation in the brain. Gangliosides 61-72 amyloid beta precursor protein Homo sapiens 46-51 21214549-2 2011 A body of evidence is growing to suggest that Abeta binds to ganglioside on neuronal membranes, and then, is converted to an endogenous seed with an altered conformation (ganglioside-bound Abeta, GAbeta) for amyloid fibril formation in the brain. Gangliosides 61-72 amyloid beta precursor protein Homo sapiens 189-194 21214549-2 2011 A body of evidence is growing to suggest that Abeta binds to ganglioside on neuronal membranes, and then, is converted to an endogenous seed with an altered conformation (ganglioside-bound Abeta, GAbeta) for amyloid fibril formation in the brain. Gangliosides 171-182 amyloid beta precursor protein Homo sapiens 46-51 21214549-2 2011 A body of evidence is growing to suggest that Abeta binds to ganglioside on neuronal membranes, and then, is converted to an endogenous seed with an altered conformation (ganglioside-bound Abeta, GAbeta) for amyloid fibril formation in the brain. Gangliosides 171-182 amyloid beta precursor protein Homo sapiens 189-194 20831659-0 2011 Ganglioside-mediated aggregation of amyloid beta-proteins (Abeta): comparison between Abeta-(1-42) and Abeta-(1-40). Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 59-64 20831659-0 2011 Ganglioside-mediated aggregation of amyloid beta-proteins (Abeta): comparison between Abeta-(1-42) and Abeta-(1-40). Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 86-91 20831659-3 2011 We have proposed that Abeta-(1-40) specifically bound to a ganglioside cluster forms cytotoxic fibrils via a conformational transition from an alpha-helix-rich structure to a beta-sheet-rich one. Gangliosides 59-70 amyloid beta precursor protein Homo sapiens 22-27 21318142-4 2011 This paper summarizes the molecular mechanisms by which Abeta aggregates on membranes containing ganglioside clusters, forming amyloid fibrils. Gangliosides 97-108 amyloid beta precursor protein Homo sapiens 56-61 20117237-5 2010 To date, various in vitro and in vivo studies on GAbeta have revealed how Abeta binds to gangliosides, i.e., what are the favorable physicochemical and neurobiological conditions for generating GAbeta, and what is the pathological significance of ganglioside-induced Abeta assembly in the development of AD. Gangliosides 89-101 amyloid beta precursor protein Homo sapiens 50-55 20930481-5 2010 Our group demonstrated that amyloid formation by amyloid beta-protein (Abeta) was facilitated by gangliosides in lipid raft-like model membranes. Gangliosides 97-109 amyloid beta precursor protein Homo sapiens 71-76 20117237-0 2010 Abeta polymerization through interaction with membrane gangliosides. Gangliosides 55-67 amyloid beta precursor protein Homo sapiens 0-5 20117237-3 2010 The ganglioside-bound Abeta (GAbeta) possessed unique characteristics, including its altered immunoreactivity, which suggests its distinct conformation from native Abeta, and its strong potency to accelerate Abeta assembly into fibrils. Gangliosides 4-15 amyloid beta precursor protein Homo sapiens 22-27 20117237-3 2010 The ganglioside-bound Abeta (GAbeta) possessed unique characteristics, including its altered immunoreactivity, which suggests its distinct conformation from native Abeta, and its strong potency to accelerate Abeta assembly into fibrils. Gangliosides 4-15 amyloid beta precursor protein Homo sapiens 30-35 20117237-5 2010 To date, various in vitro and in vivo studies on GAbeta have revealed how Abeta binds to gangliosides, i.e., what are the favorable physicochemical and neurobiological conditions for generating GAbeta, and what is the pathological significance of ganglioside-induced Abeta assembly in the development of AD. Gangliosides 89-101 amyloid beta precursor protein Homo sapiens 74-79 20117237-5 2010 To date, various in vitro and in vivo studies on GAbeta have revealed how Abeta binds to gangliosides, i.e., what are the favorable physicochemical and neurobiological conditions for generating GAbeta, and what is the pathological significance of ganglioside-induced Abeta assembly in the development of AD. Gangliosides 89-100 amyloid beta precursor protein Homo sapiens 50-55 20117237-5 2010 To date, various in vitro and in vivo studies on GAbeta have revealed how Abeta binds to gangliosides, i.e., what are the favorable physicochemical and neurobiological conditions for generating GAbeta, and what is the pathological significance of ganglioside-induced Abeta assembly in the development of AD. Gangliosides 89-100 amyloid beta precursor protein Homo sapiens 74-79 20117237-7 2010 Furthermore, the conformational change of Abeta in the presence of ganglioside has been characterized by an NMR study. Gangliosides 67-78 amyloid beta precursor protein Homo sapiens 42-47 20226163-1 2010 Ganglioside GM1 mediates the amyloid beta (Abeta) aggregation that is the hallmark of Alzheimer"s disease (AD). Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 29-41 20423299-4 2010 Abeta induced changes in membrane fluidity could be explained by physico-chemical interactions of the peptide with membrane components such as cholesterol, phospholipids and gangliosides. Gangliosides 174-186 amyloid beta precursor protein Homo sapiens 0-5 20226163-1 2010 Ganglioside GM1 mediates the amyloid beta (Abeta) aggregation that is the hallmark of Alzheimer"s disease (AD). Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 43-48 20226163-2 2010 To investigate how ganglioside-containing lipid bilayers interact with Abeta, we examined the interaction between Abeta40 and supported planar lipid bilayers (SPBs) on mica and SiO(2) substrates by using atomic force microscopy, fluorescence microscopy, and molecular dynamics computer simulations. Gangliosides 19-30 amyloid beta precursor protein Homo sapiens 71-76 19217912-3 2009 More specifically, it is thought that A beta interacts with ganglioside rich and sialic acid rich regions of cell surfaces. Gangliosides 60-71 amyloid beta precursor protein Homo sapiens 38-44 19052862-2 2009 To characterize the conformation of Abeta bound to the ganglioside, we performed 920 MHz ultra-high field NMR analyses using isotopically labeled Abeta(1-40) in association with GM1 and lyso-GM1 micelles. Gangliosides 55-66 amyloid beta precursor protein Homo sapiens 36-41 19052862-2 2009 To characterize the conformation of Abeta bound to the ganglioside, we performed 920 MHz ultra-high field NMR analyses using isotopically labeled Abeta(1-40) in association with GM1 and lyso-GM1 micelles. Gangliosides 55-66 amyloid beta precursor protein Homo sapiens 146-151 19052862-4 2009 These findings suggest that the ganglioside clusters serve as a unique platform for binding coupled with conformational transition of Abeta molecules, rendering their spatial rearrangements restricted to promote specific intermolecular interactions. Gangliosides 32-43 amyloid beta precursor protein Homo sapiens 134-139 20074569-1 2010 Gangliosides are targets for a variety of pathologically relevant proteins, including amyloid beta (Abeta), an important component implicated in Alzheimer"s disease (AD). Gangliosides 0-12 amyloid beta precursor protein Homo sapiens 86-98 20074569-1 2010 Gangliosides are targets for a variety of pathologically relevant proteins, including amyloid beta (Abeta), an important component implicated in Alzheimer"s disease (AD). Gangliosides 0-12 amyloid beta precursor protein Homo sapiens 100-105 20074569-2 2010 To provide a structural basis for this pathogenic interaction associated with AD, we conducted NMR analyses of the Abeta interactions with gangliosides using lyso-GM1 micelles as a model system. Gangliosides 139-151 amyloid beta precursor protein Homo sapiens 115-120 20074569-3 2010 Our NMR data revealed that the sugar-lipid interface is primarily perturbed upon binding of Abeta to the micelles, underscoring the importance of the inner part of the ganglioside cluster for accommodating Abeta in comparison with the outer carbohydrate branches that provide microbial toxin- and virus-binding sites. Gangliosides 168-179 amyloid beta precursor protein Homo sapiens 92-97 20074569-3 2010 Our NMR data revealed that the sugar-lipid interface is primarily perturbed upon binding of Abeta to the micelles, underscoring the importance of the inner part of the ganglioside cluster for accommodating Abeta in comparison with the outer carbohydrate branches that provide microbial toxin- and virus-binding sites. Gangliosides 168-179 amyloid beta precursor protein Homo sapiens 206-211 19138679-4 2009 The ganglioside GM1 potentiated the effect of Abeta (1-40), as viewed from (31)P NMR. Gangliosides 4-15 amyloid beta precursor protein Homo sapiens 46-51 18508118-3 2008 More specifically, it is thought that Abeta interacts with ganglioside rich and sialic acid rich regions of cell surfaces. Gangliosides 59-70 amyloid beta precursor protein Homo sapiens 38-43 18975139-5 2008 We first provide an overview of recent work, starting with findings regarding the amphiphatic amyloid-beta protein (Abeta), which give evidence that membranes can directly promote aggregation, and that the effectiveness in this process can be related to the presence of specific neuronal ganglioside lipids. Gangliosides 288-299 amyloid beta precursor protein Homo sapiens 116-121 16721824-7 2006 In addition, lipid raft-induced Abeta oligomerization was shown to be inhibited in CHO-K1 cells which were defective with regard to ganglioside biosynthesis. Gangliosides 132-143 amyloid beta precursor protein Homo sapiens 32-37 17887730-5 2007 The peptide forms an alpha-helical or a beta-sheet structure on the ganglioside-containing membranes. Gangliosides 68-79 amyloid beta precursor protein Homo sapiens 38-44 17321494-6 2007 Regarding the role of gangliosides in the facilitation of Abeta assembly, it has recently been reported that region-specific deposition of hereditary variant-type Abetas is determined by local gangliosides in the brain. Gangliosides 193-205 amyloid beta precursor protein Homo sapiens 58-63 17382287-5 2007 The importance of ganglioside clusters in the aggregation of Abeta is emphasized. Gangliosides 18-29 amyloid beta precursor protein Homo sapiens 61-66 17321494-6 2007 Regarding the role of gangliosides in the facilitation of Abeta assembly, it has recently been reported that region-specific deposition of hereditary variant-type Abetas is determined by local gangliosides in the brain. Gangliosides 22-34 amyloid beta precursor protein Homo sapiens 58-63 17135262-0 2007 A ganglioside-induced toxic soluble Abeta assembly. Gangliosides 2-13 amyloid beta precursor protein Homo sapiens 36-41 16721824-8 2006 This indicates that Abeta oligomerization requires gangliosides that are enriched in the lipid rafts. Gangliosides 51-63 amyloid beta precursor protein Homo sapiens 20-25 15002743-3 2004 Ganglioside GM1 binds tightly with Abeta and it is speculated that GM1 inhibits Abeta from undergoing alpha-helix to beta-sheet conformational changes. Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 35-40 15709486-2 2005 Using model membrane/liposome systems the interaction of Abeta with specific lipids (e.g. phospholipids, gangliosides, cholesterol) has been defined. Gangliosides 105-117 amyloid beta precursor protein Homo sapiens 57-62 15002743-3 2004 Ganglioside GM1 binds tightly with Abeta and it is speculated that GM1 inhibits Abeta from undergoing alpha-helix to beta-sheet conformational changes. Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 80-85 15002743-4 2004 Although the role of gangliosides in conformational changes of Abeta have been studied, the specific nature of these interactions have not been reported. Gangliosides 21-33 amyloid beta precursor protein Homo sapiens 63-68 15002743-5 2004 In the present report multidimensional NMR studies of ganglioside-Abeta interactions were conducted in sodium dodecyl sulphate (SDS) micelles, a membrane-mimicking environment. Gangliosides 54-65 amyloid beta precursor protein Homo sapiens 66-71 12659848-5 2003 These results suggest that the lipid raft containing a ganglioside cluster serves as a conformational catalyst or a chaperon generating a membrane-active form of A beta with seeding ability. Gangliosides 55-66 amyloid beta precursor protein Homo sapiens 162-168 12659848-2 2003 We have proposed that the aggregation proceeds in the lipid raft containing a ganglioside cluster, the formation of which is facilitated by cholesterol and for which A beta shows a specific affinity. Gangliosides 78-89 amyloid beta precursor protein Homo sapiens 166-172 11859933-7 2001 The release of IL-1beta from A beta 1-42-activated cells was significantly inhibited (33-48% of activated cells; p < 0.05 for the control value) by addition of gangliosides, suggesting that gangliosides inhibit the continuous cycle of the IL-1beta production in THP-1 cells. Gangliosides 163-175 amyloid beta precursor protein Homo sapiens 29-35 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 35-46 amyloid beta precursor protein Homo sapiens 119-124 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 35-46 amyloid beta precursor protein Homo sapiens 153-158 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 35-46 amyloid beta precursor protein Homo sapiens 153-158 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 135-146 amyloid beta precursor protein Homo sapiens 119-124 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 135-146 amyloid beta precursor protein Homo sapiens 153-158 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 135-146 amyloid beta precursor protein Homo sapiens 153-158 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 135-146 amyloid beta precursor protein Homo sapiens 119-124 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 135-146 amyloid beta precursor protein Homo sapiens 153-158 12044171-5 2002 In this study, we investigated the ganglioside species-specificity in its potency to induce a conformational change of Abeta, by which ganglioside-bound Abeta acts as a seed for Abeta fibrillogenesis, using a major ganglioside occurring in brains (GM1, GD1a, GD1b, and GT1b) in raft-like membranes composed of cholesterol and sphingomyelin. Gangliosides 135-146 amyloid beta precursor protein Homo sapiens 153-158 12044171-6 2002 Abeta recognized ganglioside clusters, the density of which increased with the number of sialic acid residues. Gangliosides 17-28 amyloid beta precursor protein Homo sapiens 0-5 12044171-9 2002 Ganglioside-bound Abeta proteins exhibited seeding abilities for amyloid formation. Gangliosides 0-11 amyloid beta precursor protein Homo sapiens 18-23 11859933-7 2001 The release of IL-1beta from A beta 1-42-activated cells was significantly inhibited (33-48% of activated cells; p < 0.05 for the control value) by addition of gangliosides, suggesting that gangliosides inhibit the continuous cycle of the IL-1beta production in THP-1 cells. Gangliosides 193-205 amyloid beta precursor protein Homo sapiens 29-35 34768981-2 2021 Our study is based on the design of a small peptide inhibitor (AmyP53) that combines the ganglioside recognition properties of the beta-amyloid peptide (Abeta, Alzheimer) and alpha-synuclein (alpha-syn, Parkinson). Gangliosides 89-100 amyloid beta precursor protein Homo sapiens 131-151 9037173-6 1997 Binding to the ganglioside is likely to modulate the neurotoxic and/or amyloidogenic properties of A beta(1-40). Gangliosides 15-26 amyloid beta precursor protein Homo sapiens 99-105 10194329-2 1999 To gain insight into the molecular details of this association, we investigated the interactions of Abeta (1-40) with ganglioside-containing membranes by circular dichroism (CD) and Fourier transform infrared-polarized attenuated total reflection (FTIR-PATR) spectroscopy. Gangliosides 118-129 amyloid beta precursor protein Homo sapiens 100-105 10194329-3 1999 The CD study revealed that at physiological ionic strength Abeta (1-40) specifically binds to ganglioside-containing membranes inducing a two-state, unordered --> beta-sheet transition above a threshold intramembrane ganglioside concentration, which depends on the host lipid bilayers used. Gangliosides 94-105 amyloid beta precursor protein Homo sapiens 59-64 10194329-3 1999 The CD study revealed that at physiological ionic strength Abeta (1-40) specifically binds to ganglioside-containing membranes inducing a two-state, unordered --> beta-sheet transition above a threshold intramembrane ganglioside concentration, which depends on the host lipid bilayers used. Gangliosides 220-231 amyloid beta precursor protein Homo sapiens 59-64 10194329-6 1999 These results suggest that Abeta (1-40) imposes negative curvature strain on ganglioside-containing lipid bilayers, disturbing the structure and function of the membranes. Gangliosides 77-88 amyloid beta precursor protein Homo sapiens 27-32 9972868-5 1999 However, treatment of A beta-activated THP-1 cells with GM1 and several other complex gangliosides, but not hematosides and neutral glycosphingolipids such as asialo-GM1 (GA1), lactosylceramide, and globoside, significantly decreased the cytokine release. Gangliosides 86-98 amyloid beta precursor protein Homo sapiens 22-28 9972868-6 1999 In contrast, this effect was not observed for lipopolysaccharide (LPS)-activated and thrombin-activated THP-1 cells, indicating that the ganglioside effect is specific for A beta-induced cytokine release. Gangliosides 137-148 amyloid beta precursor protein Homo sapiens 172-178 34768981-2 2021 Our study is based on the design of a small peptide inhibitor (AmyP53) that combines the ganglioside recognition properties of the beta-amyloid peptide (Abeta, Alzheimer) and alpha-synuclein (alpha-syn, Parkinson). Gangliosides 89-100 amyloid beta precursor protein Homo sapiens 153-158 34110944-8 2021 EXPERT OPINION: We propose a mechanism through which activation of sigma-1R and autophagy could alter amyloid precursor protein processing to inhibit amyloid-beta production by reconstituting cholesterol and gangliosides in the lipid raft to offer neuroprotection against AD. Gangliosides 208-220 amyloid beta precursor protein Homo sapiens 102-127 35580354-10 2022 Moreover, the Abeta-membrane interaction was found to be governed by the repulsive electrostatic interaction between Abeta and the ganglioside GM1 lipid. Gangliosides 131-142 amyloid beta precursor protein Homo sapiens 14-19 35580354-10 2022 Moreover, the Abeta-membrane interaction was found to be governed by the repulsive electrostatic interaction between Abeta and the ganglioside GM1 lipid. Gangliosides 131-142 amyloid beta precursor protein Homo sapiens 117-122