| scholarly article | Q13442814 |
| review article | Q7318358 |
| P50 | author | Ruth Nussinov | Q7383152 |
| Buyong Ma | Q30348466 | ||
| P2093 | author name string | Jun Zhao | |
| P2860 | cites work | Immunotherapy for Alzheimer's disease: hoops and hurdles | Q26823877 |
| Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change | Q27620158 | ||
| Molecular basis for passive immunotherapy of Alzheimer's disease | Q27648521 | ||
| X-ray structure of the PHF core C-terminus: insight into the folding of the intrinsically disordered protein tau in Alzheimer's disease | Q27649220 | ||
| Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope | Q27649747 | ||
| Crystal structure of human prion protein bound to a therapeutic antibody | Q27653698 | ||
| Structures of Aβ-Related Peptide−Monoclonal Antibody Complexes , | Q27655072 | ||
| Structural Correlates of Antibodies Associated with Acute Reversal of Amyloid -related Behavioral Deficits in a Mouse Model of Alzheimer Disease | Q27658233 | ||
| Monoclonal antibody MN423 as a stable mold facilitates structure determination of disordered tau protein | Q27660055 | ||
| Structure and properties of a complex of α-synuclein and a single-domain camelid antibody | Q27663303 | ||
| His-tag binding by antibody C706 mimics β-amyloid recognition | Q27664463 | ||
| Amyloid fibril recognition with the conformational B10 antibody fragment depends on electrostatic interactions | Q27665654 | ||
| Molecular basis of -amyloid oligomer recognition with a conformational antibody fragment | Q27670832 | ||
| Gantenerumab: a novel human anti-Aβ antibody demonstrates sustained cerebral amyloid-β binding and elicits cell-mediated removal of human amyloid-β | Q27674567 | ||
| An Ultra-specific Avian Antibody to Phosphorylated Tau Protein Reveals a Unique Mechanism for Phosphoepitope Recognition | Q27675104 | ||
| 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 | ||
| The crystal structure of an octapeptide repeat of the Prion protein in complex with a Fab fragment of the POM2 antibody | Q27677854 | ||
| Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme | Q27679412 | ||
| Structural studies on the folded domain of the human prion protein bound to the Fab fragment of the antibody POM1 | Q27682988 | ||
| Crystal structure reveals conservation of amyloid-β conformation recognized by 3D6 following humanization to bapineuzumab | Q27684692 | ||
| Linear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10 | Q27684844 | ||
| Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody | Q27688102 | ||
| X-ray structural and molecular dynamical studies of the globular domains of cow, deer, elk and Syrian hamster prion proteins | Q27702024 | ||
| The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics | Q27860914 | ||
| Systems biology of neurodegenerative diseases | Q28080741 | ||
| Extended disordered proteins: targeting function with less scaffold | Q28208096 | ||
| Protein folding and misfolding | Q28235199 | ||
| Conformational disease | Q28244193 | ||
| Insight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants | Q28270774 | ||
| Bound water at protein-protein interfaces: partners, roles and hydrophobic bubbles as a conserved motif | Q28744655 | ||
| Alzheimer's disease: the amyloid cascade hypothesis | Q29547160 | ||
| Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis | Q29547501 | ||
| 3D structure of Alzheimer's amyloid-beta(1-42) fibrils | Q29617475 | ||
| Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders | Q29619537 | ||
| Similarities between the spectrin SH3 domain denatured state and its folding transition state | Q30175164 | ||
| Interaction between bound water molecules and local protein structures: A statistical analysis of the hydrogen bond structures around bound water molecules. | Q30380846 | ||
| From the globular to the fibrous state: protein structure and structural conversion in amyloid formation. | Q30431328 | ||
| Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell | Q31039692 | ||
| Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging | Q33227600 | ||
| Folding funnels, binding funnels, and protein function | Q33674287 | ||
| Folding and binding cascades: shifts in energy landscapes | Q33723481 | ||
| Folding funnels and binding mechanisms | Q33743626 | ||
| Folding and binding cascades: dynamic landscapes and population shifts | Q33876426 | ||
| Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases | Q33909288 | ||
| Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states | Q34006345 | ||
| Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape | Q34059772 | ||
| Structural Insight into Tau Protein's Paradox of Intrinsically Disordered Behavior, Self-Acetylation Activity, and Aggregation | Q34133863 | ||
| Polymorphic C-terminal β-Sheet Interactions Determine the Formation of Fibril or Amyloid β-derived Diffusible Ligand-like Globulomer for the Alzheimer Aβ42 Dodecamer | Q34299359 | ||
| The amyloid state and its association with protein misfolding diseases. | Q34421102 | ||
| Prion protein-specific antibodies-development, modes of action and therapeutics application | Q34423386 | ||
| Molecular basis for mid-region amyloid-β capture by leading Alzheimer's disease immunotherapies | Q34472054 | ||
| Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies | Q34811887 | ||
| Polymorphic triple beta-sheet structures contribute to amide hydrogen/deuterium (H/D) exchange protection in the Alzheimer amyloid beta42 peptide | Q35311079 | ||
| Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings | Q35547043 | ||
| Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease | Q35766611 | ||
| Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration | Q35795163 | ||
| Cross-seeding and conformational selection between three- and four-repeat human Tau proteins | Q35922551 | ||
| Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases | Q35934211 | ||
| Conformational basis for asymmetric seeding barrier in filaments of three- and four-repeat tau. | Q36051973 | ||
| In vitro neutralization of prions with PrP(Sc)-specific antibodies | Q36147958 | ||
| Atomic-level characterization of disordered protein ensembles | Q36717589 | ||
| Evidence for prion-like mechanisms in several neurodegenerative diseases: potential implications for immunotherapy | Q37280507 | ||
| Is there still any hope for amyloid-based immunotherapy for Alzheimer's disease? | Q38180298 | ||
| Coupling of the non-amyloid-component (NAC) domain and the KTK(E/Q)GV repeats stabilize the α-synuclein fibrils | Q39999661 | ||
| Antibody Recognition of Disordered Antigens | Q40163594 | ||
| Structure of a single-chain Fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression. | Q41518158 | ||
| Identification of structural determinants on tau protein essential for its pathological function: novel therapeutic target for tau immunotherapy in Alzheimer's disease. | Q42026368 | ||
| Amyloid beta-protein monomer structure: a computational and experimental study. | Q42150321 | ||
| Minimal Zn(2+) binding site of amyloid-β. | Q42364819 | ||
| Persistence of native-like topology in a denatured protein in 8 M urea | Q43682045 | ||
| The "nonamyloidogenic" p3 fragment (amyloid beta17-42) is a major constituent of Down's syndrome cerebellar preamyloid | Q46178460 | ||
| Antibodies and protein misfolding: From structural research tools to therapeutic strategies | Q46842526 | ||
| Structural biology: Breaking the protein rules | Q57071963 | ||
| Amyloidosis | Q68008389 | ||
| Surface structure of amyloid-beta fibrils contributes to cytotoxicity | Q80739930 | ||
| Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts | Q87298784 | ||
| Introduction to intrinsically disordered proteins (IDPs) | Q87368165 | ||
| P433 | issue | 11 Pt B | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | crystal structure | Q895901 |
| immunotherapy | Q1427096 | ||
| P304 | page(s) | 2672-2681 | |
| P577 | publication date | 2016-06-03 | |
| P1433 | published in | Biochimica et Biophysica Acta | Q864239 |
| P1476 | title | Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes | |
| P478 | volume | 1860 |
| Q41496847 | A coiled conformation of amyloid-β recognized by antibody C706. |
| Q47567087 | Allosteric control of antibody-prion recognition through oxidation of a disulfide bond between the CH and CL chains |
| Q91808144 | Antibody Structure and Function: The Basis for Engineering Therapeutics |
| Q57903229 | Computational Analysis for the Rational Design of Anti-Amyloid Beta (Aβ) Antibodies |
| Q47316363 | Local and global anatomy of antibody-protein antigen recognition |
| Q47565290 | Mechanisms of recognition of amyloid-β (Aβ) monomer, oligomer, and fibril by homologous antibodies |
| Q90212307 | Molecular Recognition between Aβ-Specific Single-Domain Antibody and Aβ Misfolded Aggregates |
| Q93070094 | Monolayer Sensitivity Enables a 2D IR Spectroscopic Immuno-biosensor for Studying Protein Structures: Application to Amyloid Polymorphs |
| Q93039579 | Mutual population-shift driven antibody-peptide binding elucidated by molecular dynamics simulations |
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