PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33333060-2 2021 This research reports a modified ELISA with graphene for the detection of AD biomarker amyloid beta (Abeta) oligomer. Graphite 44-52 amyloid beta precursor protein Homo sapiens 87-99 33333060-2 2021 This research reports a modified ELISA with graphene for the detection of AD biomarker amyloid beta (Abeta) oligomer. Graphite 44-52 amyloid beta precursor protein Homo sapiens 101-106 26515666-3 2015 In this work, efficient and low-cytotoxicity inhibitors, graphene quantum dots (GQDs) are reported for their application in inhibiting the aggregation of Abeta peptides. Graphite 57-65 amyloid beta precursor protein Homo sapiens 154-159 31914730-6 2020 The Abeta ion channel was then detected by graphene-based field-effect transistors. Graphite 43-51 amyloid beta precursor protein Homo sapiens 4-9 30467942-4 2019 Herein, we characterized the assembly structures of Abeta1-42, Abeta(-5)-42, Abeta(-10)-42 and Abeta(-15)-42 with both normal and reversed sequences on highly oriented pyrolytic graphite (HOPG) surfaces with scanning tunneling microscopy (STM). Graphite 178-186 amyloid beta precursor protein Homo sapiens 52-57 30467942-4 2019 Herein, we characterized the assembly structures of Abeta1-42, Abeta(-5)-42, Abeta(-10)-42 and Abeta(-15)-42 with both normal and reversed sequences on highly oriented pyrolytic graphite (HOPG) surfaces with scanning tunneling microscopy (STM). Graphite 178-186 amyloid beta precursor protein Homo sapiens 63-68 29244487-2 2018 Herein, a new high-efficiency and low-cytotoxicity Abeta aggregation inhibitors, GQD-T, was designed through the combination of two Abeta aggregation inhibitors, graphene quantum dots (GQDs) and tramiprosate. Graphite 162-170 amyloid beta precursor protein Homo sapiens 51-56 26503908-3 2015 We here provide both experimental and computational evidence that pristine graphene and graphene-oxide nanosheets can inhibit Abeta peptide monomer fibrillation and clear mature amyloid fibrils, thus impacting the central molecular superstructures correlated with AD pathogenesis. Graphite 75-83 amyloid beta precursor protein Homo sapiens 126-131 26503908-4 2015 Our molecular dynamics simulations for the first time reveal that graphene nanosheets can penetrate and extract a large number of peptides from pre-formed amyloid fibrils; these effects seem to be related to exceptionally strong dispersion interactions between peptides and graphene that are further enhanced by strong pi-pi stacking between the aromatic residues of extracted Abeta peptides and the graphene surface. Graphite 66-74 amyloid beta precursor protein Homo sapiens 377-382 21918653-4 2011 Here, we use atomic force microscopy (AFM) and molecular dynamics (MD) simulations to demonstrate that at room temperature a truncated Abeta peptide which is generated in vivo and shown to be toxic in vitro forms fibrillar structures on hydrophobic graphite surfaces, but not on hydrophilic mica or lipid bilayers. Graphite 249-257 amyloid beta precursor protein Homo sapiens 135-140 32262329-3 2015 Herein, we report the use of strongly ferromagnetic few-layer graphene-coated magnetic nanoparticles (C/Co), which were functionalized with a cationic polymer, poly[3-(methacryloyl amino)propyl]trimethylammonium chloride (polyMAPTAC), C/Co@polyMAPTAC, for the adsorption and magnetic separation of Abeta aggregates. Graphite 62-70 amyloid beta precursor protein Homo sapiens 298-303 22468636-0 2012 Structure, orientation, and surface interaction of Alzheimer amyloid-beta peptides on the graphite. Graphite 90-98 amyloid beta precursor protein Homo sapiens 61-73 22468636-3 2012 Here, we perform all-atom explicit-water molecular dynamics (MD) simulations to study the orientation change, conformational dynamics, surface interaction of small Abeta aggregates with different sizes (monomer to tetramer), and conformations (alpha-helix and beta-hairpin) upon adsorption on the graphite surface, in comparison with Abeta structures in bulk solution. Graphite 297-305 amyloid beta precursor protein Homo sapiens 164-169 22468636-4 2012 Simulation results show that hydrophobic graphite induces the quick adsorption of Abeta peptides regardless of their initial conformations and sizes. Graphite 41-49 amyloid beta precursor protein Homo sapiens 82-87 22468636-6 2012 More importantly, due to the amphiphilic sequence of Abeta and the hydrophobic nature of graphite, hydrophobic C-terminal residues of higher-order Abeta oligomers appear to have preferential interactions with the graphite surface for facilitating Abeta fibril formation and fibril growth. Graphite 89-97 amyloid beta precursor protein Homo sapiens 147-152 22468636-6 2012 More importantly, due to the amphiphilic sequence of Abeta and the hydrophobic nature of graphite, hydrophobic C-terminal residues of higher-order Abeta oligomers appear to have preferential interactions with the graphite surface for facilitating Abeta fibril formation and fibril growth. Graphite 89-97 amyloid beta precursor protein Homo sapiens 147-152 22468636-6 2012 More importantly, due to the amphiphilic sequence of Abeta and the hydrophobic nature of graphite, hydrophobic C-terminal residues of higher-order Abeta oligomers appear to have preferential interactions with the graphite surface for facilitating Abeta fibril formation and fibril growth. Graphite 213-221 amyloid beta precursor protein Homo sapiens 53-58 22468636-6 2012 More importantly, due to the amphiphilic sequence of Abeta and the hydrophobic nature of graphite, hydrophobic C-terminal residues of higher-order Abeta oligomers appear to have preferential interactions with the graphite surface for facilitating Abeta fibril formation and fibril growth. Graphite 213-221 amyloid beta precursor protein Homo sapiens 147-152 22468636-6 2012 More importantly, due to the amphiphilic sequence of Abeta and the hydrophobic nature of graphite, hydrophobic C-terminal residues of higher-order Abeta oligomers appear to have preferential interactions with the graphite surface for facilitating Abeta fibril formation and fibril growth. Graphite 213-221 amyloid beta precursor protein Homo sapiens 147-152 10097098-1 1999 We have applied in situ atomic force microscopy to directly observe the aggregation of Alzheimer"s beta-amyloid peptide (Abeta) in contact with two model solid surfaces: hydrophilic mica and hydrophobic graphite. Graphite 203-211 amyloid beta precursor protein Homo sapiens 99-119 19564953-4 2009 AFM images on graphite surfaces revealed the morphology of Abeta aggregates with gold colloids. Graphite 14-22 amyloid beta precursor protein Homo sapiens 59-64 16752395-5 2006 Steps formed by edge-plane surface defects on the graphite were found to act as a template to promote the assembly of Abeta into fibrils. Graphite 50-58 amyloid beta precursor protein Homo sapiens 118-123 16752395-6 2006 Initially, after being deposited on the graphite surface, Abeta had a uniform beaded morphology. Graphite 40-48 amyloid beta precursor protein Homo sapiens 58-63 10097098-1 1999 We have applied in situ atomic force microscopy to directly observe the aggregation of Alzheimer"s beta-amyloid peptide (Abeta) in contact with two model solid surfaces: hydrophilic mica and hydrophobic graphite. Graphite 203-211 amyloid beta precursor protein Homo sapiens 121-126 10097098-6 1999 In contrast, on hydrophobic graphite Abeta formed uniform, elongated sheets. Graphite 28-36 amyloid beta precursor protein Homo sapiens 37-42 10097098-8 1999 The sheets of Abeta were oriented along three directions at 120 degrees to each other, resembling the crystallographic symmetry of a graphite surface. Graphite 133-141 amyloid beta precursor protein Homo sapiens 14-19 34878460-0 2021 Graphene quantum dots obstruct the membrane axis of Alzheimer"s amyloid beta. Graphite 0-8 amyloid beta precursor protein Homo sapiens 64-76 33806971-5 2021 The C-O, C=O, P-O, and N-C bonds in the flame-retardant APP/EP composite were broken during the laser scribing, while the remaining carbon atoms recombined to generate the graphene layer. Graphite 172-180 amyloid beta precursor protein Homo sapiens 56-62 33806971-11 2021 The direct laser scribing of graphene from APP/EP in an air atmosphere provides a convenient and practical approach for the fabrication of flame-retardant electronics. Graphite 29-37 amyloid beta precursor protein Homo sapiens 43-49 35468173-3 2022 Specifically, graphite carbon nitride (g-C3N4) as an effective ECL luminescent substrate and Au nanoparticles were sequentially assembled on the Au electrode surface, and then a thiol-modified aptamer for capturing Abeta peptide was attached to the surface of the electrode through the Au-S bond. Graphite 14-22 amyloid beta precursor protein Homo sapiens 215-220