| P50 | author | Charles Eigenbrot | Q28037170 |
| | Mike Reichelt | Q130280492 |
| P2093 | author name string | Germaine Fuh | |
| | Jasvinder K Atwal | |
| | Ryan J Watts | |
| | Weiru Wang | |
| | James A Ernst | |
| | Till Maurer | |
| | Travis W Bainbridge | |
| | Bing Li | |
| | Andrea Pfeifer | |
| | Andreas Muhs | |
| | Oskar Adolfsson | |
| | Maria Pihlgren | |
| | Mary Mathieu | |
| | Mark Ultsch | |
| P2860 | cites work | PHENIX: a comprehensive Python-based system for macromolecular structure solution | Q24654617 |
| | Processing of X-ray diffraction data collected in oscillation mode | Q26778468 |
| | Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope | Q27649747 |
| | Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils | Q27652925 |
| | A therapeutic antibody targeting BACE1 inhibits amyloid-β production in vivo | Q27668018 |
| | Gantenerumab: a novel human anti-Aβ antibody demonstrates sustained cerebral amyloid-β binding and elicits cell-mediated removal of human amyloid-β | Q27674567 |
| | Structural basis of C-terminal β-amyloid peptide binding by the antibody ponezumab for the treatment of Alzheimer's disease | Q27676406 |
| | Bapineuzumab captures the N-terminus of the Alzheimer's disease amyloid-beta peptide in a helical conformation | Q27676409 |
| | Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils | Q27714742 |
| | Phasercrystallographic software | Q27860930 |
| | Shape complementarity at protein/protein interfaces | Q27860963 |
| | Refinement of macromolecular structures by the maximum-likelihood method | Q27861011 |
| | Features and development of Coot | Q27861079 |
| | Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide | Q28131750 |
| | Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo | Q28131779 |
| | Neuroinflammation in Alzheimer's disease | Q28259238 |
| | The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding | Q28294445 |
| | A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR | Q28387681 |
| | 3D structure of Alzheimer's amyloid-beta(1-42) fibrils | Q29617475 |
| | Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers | Q30365652 |
| | Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril | Q30391127 |
| | The A4 study: stopping AD before symptoms begin? | Q33725775 |
| | Modulation of β-amyloid by a single dose of GSK933776 in patients with mild Alzheimer's disease: a phase I study | Q33746272 |
| | Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR | Q34228566 |
| | Molecular basis for mid-region amyloid-β capture by leading Alzheimer's disease immunotherapies | Q34472054 |
| | X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation | Q35587166 |
| | Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease | Q35766611 |
| | Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23 | Q36012349 |
| | The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes | Q37979641 |
| | Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer's disease | Q38240609 |
| | New roles for Fc receptors in neurodegeneration-the impact on Immunotherapy for Alzheimer's Disease. | Q38246262 |
| | The Essential Role of Soluble Aβ Oligomers in Alzheimer's Disease | Q38400601 |
| | 2015 Alzheimer's disease facts and figures | Q40928952 |
| | Alzheimer's disease: Structure of aggregates revealed | Q41435277 |
| | Passive anti-amyloid immunotherapy in Alzheimer's disease: What are the most promising targets? | Q42021752 |
| | Microglial p38α MAPK is critical for LPS-induced neuron degeneration, through a mechanism involving TNFα | Q42608624 |
| | Identification of physiological and toxic conformations in Abeta42 aggregates. | Q46179719 |
| | Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease | Q47208290 |
| | An effector-reduced anti-β-amyloid (Aβ) antibody with unique aβ binding properties promotes neuroprotection and glial engulfment of Aβ. | Q47393680 |
| | Deglycosylated anti-amyloid-beta antibodies eliminate cognitive deficits and reduce parenchymal amyloid with minimal vascular consequences in aged amyloid precursor protein transgenic mice. | Q48535203 |
| | Abeta40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid | Q57187810 |
| | X-ray diffraction studies on amyloid filaments | Q72224075 |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 39374 | |
| P577 | publication date | 2016-12-20 | |
| P1433 | published in | Scientific Reports | Q2261792 |
| P1476 | title | Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin | |
| P478 | volume | 6 | |