| scholarly article | Q13442814 |
| P818 | arXiv ID | 1712.00813 |
| P356 | DOI | 10.1016/J.BPJ.2018.03.019 |
| P932 | PMC publication ID | 5937719 |
| P698 | PubMed publication ID | 29653837 |
| P2093 | author name string | Simcha Srebnik | |
| Boris Haimov | |||
| P2860 | cites work | The Protein Data Bank | Q24515306 |
| A helix propensity scale based on experimental studies of peptides and proteins | Q24537262 | ||
| VMD: visual molecular dynamics | Q27860554 | ||
| Structure validation by Calpha geometry: phi,psi and Cbeta deviation | Q27860657 | ||
| Protein misfolding, functional amyloid, and human disease | Q28131732 | ||
| Stereochemistry of polypeptide chain configurations | Q28190300 | ||
| Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case | Q30164098 | ||
| Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom metalloproteinase, atrolysin A. | Q30304588 | ||
| A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins. | Q30342690 | ||
| Sequence-similar, structure-dissimilar protein pairs in the PDB. | Q30365843 | ||
| Sequence determinants of amyloid fibril formation | Q30502750 | ||
| The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR. | Q30769903 | ||
| A closer look into the α-helix basin | Q30830738 | ||
| α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes | Q33356614 | ||
| Prediction of amyloid fibril-forming segments based on a support vector machine | Q33407865 | ||
| BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis | Q33422947 | ||
| Alpha-helical stabilization by side chain shielding of backbone hydrogen bonds | Q34014321 | ||
| Helix geometry in proteins | Q34049849 | ||
| Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study | Q34155536 | ||
| Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau. | Q34305798 | ||
| Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases | Q34443878 | ||
| MetAmyl: a METa-predictor for AMYLoid proteins | Q35048682 | ||
| Mechanisms of amyloid fibril self-assembly and inhibition. Model short peptides as a key research tool | Q36319498 | ||
| Computational models for the prediction of polypeptide aggregation propensity | Q36552509 | ||
| Revisiting the Ramachandran plot: Hard‐sphere repulsion, electrostatics, and H‐bonding in the α‐helix | Q36631418 | ||
| An improved hydrogen bond potential: impact on medium resolution protein structures. | Q36639400 | ||
| A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides | Q37285511 | ||
| Driving Forces for Nonnative Protein Aggregation and Approaches to Predict Aggregation-Prone Regions | Q39358138 | ||
| Implications of peptide assemblies in amyloid diseases | Q39431937 | ||
| Amyloidogenic sequences in native protein structures | Q40403530 | ||
| Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties | Q40902557 | ||
| The role of protein stability, solubility, and net charge in amyloid fibril formation | Q42107622 | ||
| NetCSSP: web application for predicting chameleon sequences and amyloid fibril formation | Q42139451 | ||
| Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure | Q43043429 | ||
| Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin | Q44049224 | ||
| Kinetic studies of amyloid beta-protein fibril assembly. Differential effects of alpha-helix stabilization | Q44083672 | ||
| Exploring the sequence determinants of amyloid structure using position-specific scoring matrices | Q44106880 | ||
| Investigating the effects of mutations on protein aggregation in the cell. | Q45195856 | ||
| Diversity of kinetic pathways in amyloid fibril formation | Q46109123 | ||
| Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides | Q46233133 | ||
| Anatomy of an amyloidogenic intermediate: conversion of beta-sheet to alpha-sheet structure in transthyretin at acidic pH. | Q47608981 | ||
| FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence | Q48239540 | ||
| Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis. | Q48597012 | ||
| Cysteine as a potential anti-amyloidogenic agent with protective ability against amyloid induced cytotoxicity. | Q50885392 | ||
| AmyLoad: website dedicated to amyloidogenic protein fragments. | Q53204623 | ||
| The protofilament substructure of amyloid fibrils11Edited by F. E. Cohen | Q57843307 | ||
| X-ray diffraction studies on amyloid filaments | Q72224075 | ||
| Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide | Q78338258 | ||
| P433 | issue | 8 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 1869-1877 | |
| P577 | publication date | 2018-04-10 | |
| P1433 | published in | Biophysical Journal | Q2032955 |
| P1476 | title | The Relation between α-Helical Conformation and Amyloidogenicity. | |
| P478 | volume | 114 |
| Q64251983 | Mechanisms of Strain Diversity of Disease-Associated in-Register Parallel β-Sheet Amyloids and Implications About Prion Strains | cites work | P2860 |
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